Page last updated: 2024-08-17

histidine and heme

histidine has been researched along with heme in 745 studies

Research

Studies (745)

TimeframeStudies, this research(%)All Research%
pre-1990143 (19.19)18.7374
1990's165 (22.15)18.2507
2000's268 (35.97)29.6817
2010's148 (19.87)24.3611
2020's21 (2.82)2.80

Authors

AuthorsStudies
Appleby, CA; Bradbury, JH; Johnson, RN1
Cohen, JS; Hagenmaier, H; Hayes, MB; Ohms, JP1
Rein, H; Ristau, O; Ruckpaul, K1
Gelin, BR; Karplus, M1
Bethge, PH; Czerwinski, EW; Mathews, FS; Xavier, AV1
Phillips, SE1
Morgan, WT3
Perutz, MF1
Mazza, G; Welinder, KG1
Morgan, WT; Muller-eberhard, U1
Bazile, J; Cordier, JP; Frourin, A; Jondeau, D; Thenot, M1
Vuk Pavlović, S1
Caughey, WS; Maxwell, JC1
Frye, JS; La Mar, GN; Satterlee, JD1
Calhoun, MW; Gennis, RB; Ingledew, WJ; Lemieux, LJ; Thomas, JW1
Babcock, GT; Ferguson-Miller, S; Gennis, RB; Hosler, JP; Kim, Y; Shapleigh, JP; Tecklenburg, MM1
Dugad, LB; Goff, HM1
Bollen, A; Deleersnyder, V; Garcia-Quintana, L; Jacquet, A; Moguilevsky, N1
Cai, M; Timkovich, R1
Adachi, S; Morishima, I1
Andersson, LA; George, GN; Hori, H; Ikeda-Saito, M; Lutz, RS; Mattera, R; McKelvey, EJ; Pickering, IJ; Prince, RC; Sanders, CR1
Salemme, FR; Weber, PC; Wendoloski, JJ1
Crofts, AR; Gennis, RB; Yun, CH1
Kraut, J; Miller, MA; Smulevich, G; Spiro, TG1
Gersonde, K; La Mar, GN; Peyton, DH; Ramaprasad, S; Sankar, S; Unger, SW1
Dugad, LB; Goff, HM; Lukat, GS; Wang, CC; Wang, X1
DeWitt, DL; Shimokawa, T; Smith, WL1
Shimokawa, T; Smith, WL1
De Ciechi, P; Pakrasi, HB; Whitmarsh, J1
Baboulène, M; Lattes, A; Seris, JL; Souppe, J; Urrutigoïty, M1
Peyton, DH; Yee, S1
Champion, PM; Li, PS; Sage, JT1
Bax, A; Highet, RJ; Osawa, Y; Pohl, LR1
Chiu, ML; La Mar, GN; Lee, KB; Sligar, SG; Walker, FA; Wu, JZ; Yu, LP1
Fridén, H; Hederstedt, L1
Berry, MJ; George, SJ; Santos, H; Thomson, AJ; Turner, DL1
Kuppusamy, P; Levy, A; Rifkind, JM1
Andersson, KK; Cheesman, MR; Fridén, H; Hederstedt, L; Thomson, AJ1
Mathews, FS; Xia, ZX1
La Mar, GN; Mizukami, H; Yu, LP1
Chûjô, R; Nanai, N; Suzuki, T; Yamamoto, Y1
Cully, BC; Holeman, B; Muller-Eberhard, U; Vincent, SH1
Muller-Eberhard, U; Vincent, SH1
Gadsby, PM; Hartshorn, RT; Moura, JJ; Sinclair-Day, JD; Sykes, AG; Thomson, AJ1
Han, KH; La Mar, GN; Nagai, K1
Lieutenant, K; Redhardt, A; Steinhoff, HJ1
Behere, DV; Mitra, S; Modi, S1
Gray, HB; Raphael, AL1
Adachi, S; Morishima, I; Orii, Y; Shiro, Y; Yano, Y1
Fang, H; Gennis, RB; Lin, RJ1
Esposti, MD1
Champion, PM; Morikis, D; Sligar, SG; Springer, BA1
Konopka, K; Waskell, L1
English, AM; Fishel, LA; Kraut, J; Mauro, JM; Smulevich, G; Spiro, TG1
Behere, DV; Goff, HM; Gonzalez-Vergara, E1
Senn, H; Wüthrich, K1
Hashimoto, S; Inubushi, T; Kitagawa, T; Teraoka, J; Yonetani, T1
Moench, S; Satterlee, JD1
de Ropp, JS; La Mar, GN; Thanabal, V1
Brady, JC; Everse, J; Lin, H; McFaul, SJ1
Blouquit, Y; Craescu, CT; Rosa, J; Schaeffer, C1
Yamamoto, Y3
Shaklai, N; Shviro, Y1
Dasgupta, S; Rousseau, DL; Sassaroli, M1
Bianconi, A; Burattini, E; Congiu-Castellano, A; Dell'Ariccia, M; Durham, PJ; Giacometti, GM; Giovannelli, A1
Alden, RG; Ondrias, MR; Shelnutt, JA1
Dreybrodt, W; el Naggar, S; Schweitzer-Stenner, R1
Dalvit, C; Ho, C1
Levy, A; Rifkind, JM1
Biserte, G; Havez, R; Hayem-Lévy, A; Moschetto, Y1
Kon, H1
Alpert, Y; Banerjee, R; Leterrier, F; Williams, RJ1
Burris, RH; Swank, RT1
Loew, GM1
Jänig, GR; Jung, F; Rein, H; Ristau, O; Ruckpaul, K1
Dervartanian, DV; Legall, J1
Caughey, WS1
Branefors-Helander, P1
Babul, G; Rysavy, R; Stellwagen, E1
Azzi, A; Folin, M; Jori, G; Tamburro, AM1
Momenteau, M1
Campbell, LL; Trousil, EB1
Cohen, JS; Fisher, WR; Schechter, AN1
Aviram, I; Krauss, Y1
LeGall, J; McDonald, CC; Phillips, WD1
Loock, B; Momenteau, M1
Bitar, KG; Lowenkron, S; Vinogradov, SN1
Gurd, FR; Hanania, GI; Shire, SJ1
Perutz, MF; TenEyck, LF1
Comi, P; Gianni, AM; Giglioni, B; Ottolenghi, S; Rungger, D1
Irving, EA; Porra, RJ; Tennick, AM1
Byrne, MJ; Davison, AJ; Kaminsky, LS1
Hutner, SH1
Atassi, MZ; Singhal, RP1
Ho, C; Lindstrom, TR1
Balegh, MS; Sandberg, HE1
Antonini, E; Bonaventura, C; Bonaventura, J; Bossa, F; Brunori, M; Giardina, B; Wyman, J1
Love, WE; Padlan, EA1
Gibson, QH; Olson, JS1
Coulson, AF; Yonetani, T1
Fisher, JM; Mizuno, S; Rabinovitz, M1
Babul, J; McGowan, EB; Stellwagen, E1
Chang, JY; Schroeder, WA1
Ogawa, S; Shulman, RG; Yamane, T1
Fujiwara, M; Ogawa, S; Shulman, RG; Yamane, T1
Folin, M; Galiazzo, G; Gennari, G; Jori, G1
Bucci, E; Fronticelli, C1
Maruyama, K; Yagi, T1
Antonini, E; Forlani, L; Phelps, C1
Chien, JC; Dickinson, LC1
Gurdon, JB; Lane, CD; Marbaix, G1
Reed, T1
Nakaya, K; Shibata, K; Suzuki, T; Takenaka, O1
Molday, RS; Steinhardt, J1
Caughey, W; McCoy, S1
Hager, LP; Warme, PK2
Gaĭduk, VI; Koreneva, LG1
Jacob, HS; Winterhalter, KH1
Amit, N; Formanek, H1
de Bruin, SH; Janssen, LH; van Os, GA1
Tentori, L1
Geraci, G; Gibson, QH; Parkhurst, LJ1
Guerritore, D; Zito, R1
Craigie, JS; Laycock, MV1
Braunitzer, G; Neuwirth, H; Reinhard, F1
Bucci, E; Fronticelli, C; Ragatz, B1
Clark, JF; Gurd, FR; Hartzell, CR1
Nanzyo, N; Sano, S1
Efron, ML; Shahidi, NT1
Stellwagen, E1
Imai, K1
Brill, AS; Sandberg, HE1
Galiazzo, G; Jori, G; Scoffone, E1
Shichi, H1
Horinishi, H; Kurihara, K; Shibata, K1
Stotz, E; Vanderkooi, G1
Kraut, J; Poulos, TL1
Cleary, ML; Haynes, JR; Lingrel, JB; Schon, EA1
Hayashi, K; Kobayashi, K; Tamura, M1
Krogmann, DW; Markley, JL; Ulrich, EL1
Eglinton, DG; Greenwood, C; Hill, BC; Thomson, AJ1
Han, K; Jue, T; La Mar, GN; Yamamoto, Y1
Gelin, BR; Karplus, M; Lee, AW1
Cutnell, JD; Kong, SB; La Mar, GN2
Layrisse, M; Leets, I; Martínez-Torres, C; Ramírez, J; Taylor, P1
Friedman, JM; Ikeda-Saito, M; Scott, TW; Yonetani, T1
Kitagawa, T; Nagai, K1
Ondrias, MR; Rousseau, DL; Simon, SR2
Braunitzer, G; Liljeqvist, G; Paléus, S1
Ho, C; Lin, AK; Takahashi, S1
Friedman, JM; Ondrias, MR; Rousseau, DL; Stepnoski, RA1
Kitagawa, T; Teraoka, J1
Adams, ML; Asher, SA; Schuster, TM1
Anderson, RR; Budd, DL; Gersonde, K; La Mar, GN; Langry, KC; Sick, H; Smith, KM1
Asher, S1
de Ropp, JS; La Mar, GN; Langry, KC; Smith, KM1
Krümpelmann, D; Ribbing, W; Rüterjans, H1
Ribbing, W; Rüterjans, H2
Bucci, E; Fronticelli, C; Scholberg, HP1
Masters, BS; McMillan, K1
Ferrer, JC; Hildebrand, DP; Mauk, AG; Smith, M; Tang, HL1
Banci, L; Pierattelli, R; Turner, DL1
Choudhury, K; Marzocchi, MP; Neri, F; Poulos, TL; Smulevich, G; Willemsen, O1
Gennis, RB; Georgiou, C; Ghaim, JB; Kaysser, TM1
Meunier, B; Rich, PR; Rodriguez-Lopez, JN; Smith, AT; Thorneley, RN1
Fetrow, JS; Fumo, G; Spitzer, JS1
Admiraal, SJ; Dou, Y; George, GN; Ikeda-Saito, M; Krzywda, S; Li, T; Olson, JS; Pickering, IJ; Prince, RC; Wilkinson, AJ1
Ahmed, I; Blackburn, NJ; Boswell, JS; Fann, YC; Hoffman, BM; Verkhovskaya, ML; Wikström, M1
Newmyer, SL; Ortiz de Montellano, PR1
Amada, F; Fukuyama, K; Kubota, T; Kunishima, N; Matsubara, H1
Funasaki, N; Neya, S1
Alam, J; Kao, SM; Morgan, WT; Muster, P; Smith, A; Tatum, F1
Jewsbury, P; Kitagawa, T1
Burstyn, JN; Dawson, JH; Dierks, EA; Hawkins, BK; Yu, AE1
Goldberg, DE; Kloek, AP; Mathews, FS; Yang, J1
Cheesman, MR; Gennis, RB; Kaysser, T; Peng, Q; Peterson, J; Spinner, F; Thomson, AJ1
Desbois, A; Le Lirzin, A; Othman, S2
Fitzgerald, MM; Goodin, DB; Jensen, GM; McRee, DE; Siegel, HA1
Bohn, B; Franzen, S; Martin, JL; Poyart, C1
Ditta, GS; Helinski, DR; Monson, EK1
Joshi, AA; McDonald, MJ1
Böhme, E; Foerster, J; Harteneck, C; Humbert, P; Koesling, D; Malkewitz, J; Schultz, G; Wedel, B1
Loehr, TM; Ortiz de Montellano, PR; Sun, J; Wilks, A1
Doseeva, VV; Galkin, AG; Gazaryan, IG; Tishkov, VI1
Bruschi, M; Czjzek, M; Guerlesquin, F; Haser, R; Payan, F1
Gennis, RB; Peterson, J; Vibat, C1
Burke, JF; Paoli, M; Sanders, SA; Smith, AT; Smulevich, G; Thorneley, RN1
Bogumil, R; Brayer, GD; Hunter, CL; Lee, H; Lloyd, E; Mauk, AG; Maurus, R; Smith, M; Tang, HL1
Banci, L; Bertini, I; Ferrer, JC; Mauk, AG; Morris, IK; Smith, KM; Smith, M; Turano, P1
Campos, AP; Canters, GW; Hill, HA; Hunt, NI; Teixeira, M; Ubbink, M1
Hrkal, Z; Iwahara, S; Muller-Eberhard, U; Peyton, DH; Satoh, H; Satoh, T1
Conover, RC; Finnegan, MG; Garcia Castillo, MC; Johnson, MK; Knaff, DB1
Bogumil, R; Brayer, GD; Luo, Y; Mauk, AG; Maurus, R; Smith, M; Tang, HL1
Barrick, D1
Hori, H; Masuya, F1
Alben, JO; Calhoun, MW; Gennis, RB; Goswitz, VC; Hill, JJ; Lemieux, LJ; Thomas, JW1
Admiraal, SJ; Dou, Y; Ikeda-Saito, M; La Mar, GN; Qin, J1
Marzluf, GA; Okamoto, PM1
Adachi, S; Egawa, T; Ishimori, K; Kitagawa, T; Makino, R; Morishima, I; Nagano, S; Watanabe, Y1
Aguiar, AP; Campos, AP; Costa, HS; Santos, H; Teixeira, M; Turner, DL; Xavier, AV1
Goodin, DB; McRee, DE1
Barker, PD; Eltis, LD; Guillemette, JG; Inglis, SC; Mauk, AG; Miller, CM; Northrup, SH; Thomasson, KA1
Blauer, G; Sreerama, N; Woody, RW1
Aguiar, AP; Campos, AP; De La Rosa, MA; Hervás, M; Navarro, JA; Ortega, JM; Regalla, M; Teixeira, M; Xavier, AV1
Brown, KA; Erman, JE; Kraut, J; Miller, MA; Shaw, A; Vitello, LB1
Chapman, SK; Manson, FD; Miles, CS; Reid, GA1
Fujii, M; Iizuka, T; Isogai, Y; Iwata, T; Makino, R; Shiro, Y1
Alben, JO; Babcock, GT; Calhoun, MW; Ferguson-Miller, S; Gennis, RB; Hill, JJ; Hosler, JP; Shapleigh, JP; Tecklenburg, MM; Thomas, JW1
Barnard, ML; Diep, D; Gurdian, S; Ladd, M; Turrens, JF1
Boffi, A; Chiancone, E; Friedman, JM; Rousseau, DL; Song, S1
Maines, MD; McCoubrey, WK1
Chiu, ML; La Mar, GN; Qin, J; Rajarathnam, K; Sligar, SG1
Craescu, CT; Martineau, L1
Cox, MC; Le Brun, N; Moore, GR; Morgan, WT; Smith, A; Thomson, AJ1
Doseeva, VV; Galkin, AG; Gazarian, IG; Tishkov, VI1
Amada, F; Fukuyama, K; Kawamoto, M; Kunishima, N; Matsubara, H; Matsunaga, T1
Anraku, Y; Hori, H; Mogi, T; Tsubaki, M1
Gerber, NC; Ortiz de Montellano, PR; Rodríguez-Crespo, I1
Phillips, GN; Yang, F1
de Montellano, PR; Newmyer, SL1
Chance, MR; Fischetti, RF; Hai, Y; Huang, WX; Miller, LM; Scheuring, E; Sclavi, B; Sullivan, M1
Desbois, A; Othman, S; Richaud, P; Verméglio, A1
Bertolucci, C; Gilles-Gonzalez, MA; Gonzalez, G; Ming, LJ1
Hennecke, H; Thöny-Meyer, L; Zufferey, R1
Döpner, S; Gerscher, S; Gleissner, M; Hildebrandt, P; Schäfer, G1
Ishimori, K; Matsui, T; Morishima, I; Nagano, S; Watanabe, Y1
Ishimori, K; Morishima, I; Tanaka, M1
Cooper, CE; Pezeshk, A; Symons, MR; Torres, J; Wilson, M1
Gao, Y; Veitch, NC; Welinder, KG1
Adachi, S; Bourgeois, D; Moffat, K; Pradervand, C; Ren, Z; Schildkamp, W; Srajer, V; Teng, T; Ursby, T; Wulff, M1
Polm, MW; Schaafsma, TJ1
Kushkuley, B; Stavrov, SS1
Chen, YP; Dawson, JH; Lincoln, DE; Lovell, CR; Roach, MP; Woodin, SA1
Beck, R; Rambach, A; Raux, E; Thermes, C; Warren, M1
Chen, Y; Liu, G; Lu, J; Shao, W; Tang, W1
Oganesyan, VS; Sharonov, YA1
Furlong Nickels, E; Gennis, RB; Rumbley, JN1
Dodson, G; Liddington, RC; Paoli, M; Wilkinson, AJ1
Dyer, RB; Hummer, G; Puustinen, A; Riistama, S; Wikström, M; Woodruff, WH1
Blasco, F; Frixon, C; Lemesle-Meunier, D; Magalon, A; Rothery, RA; Weiner, JH1
Baker, AR; Brittain, T; Butler, CS; Greenwood, C; Little, RH; Lowe, DJ; Watmough, NJ1
Buchter, S; Galkin, O; Schulte, A; Tabirian, A1
Büschlen, S; Choquet, Y; Culler, D; de Vitry, C; Girard-Bascou, J; Kuras, R; Merchant, S; Wollman, FA1
Fujii, H; Ikeda-Saito, M; Ishikawa, K; Matera, KM; Sato, M; Yoshida, T; Yoshimura, T; Zhou, H1
Bucci, E; Fronticelli, C; Gilliland, GL; Ji, X; Karavitis, M; Kwansa, H; Razynska, A; Vásquez, G1
Bowler, BE; Godbole, S; Hammack, B2
Indiani, C; Neri, F; Smulevich, G; Welinder, KG1
Hellinga, HW1
Cecchini, G; Gennis, RB; Kita, K; Nakamura, K; Vibat, CR1
Babcock, GT; Marletta, MA; Schelvis, JP; Zhao, Y2
Boffi, A; Chiancone, E; Colotti, G; Das, TK; Gibson, QH; Guarrera, L; Rousseau, DL1
Beck, DL; Goldman, BS; Kranz, RG; Monika, EM1
Chien, EY; La Mar, GN; Sligar, SG; Wu, Y1
Bocian, DF; Kalsbeck, WA; Olson, JS; Tang, Q1
Barquera, B; García-Horsman, JA; Gennis, RB; Toledo-Cuevas, M; Wikström, M1
Hennecke, H; Schulz, H; Thöny-Meyer, L1
Chien, EY; Friedman, JM; Peterson, ES; Sligar, SG1
Akutsu, H; Cusanovich, MA; Nakamura, H; Niki, K; Ohmura, T1
Rivera, M; Rodríguez, JC1
Lukat-Rodgers, GS; Rexine, JL; Rodgers, KR1
Inaba, K; Ishimori, K; Morishima, I1
Saruta, F; Tatsuzawa, O; Tsunawaki, S; Yoshida, LS; Yoshikawa, K1
Bocian, DF; Dutton, PL; Kalsbeck, WA; Moser, CC; Shifman, JM1
Feis, A; Nissum, M; Smulevich, G1
de Ropp, JS; La Mar, GN; Mandal, PK1
Liong, E; Matsui, T; Ozaki, Si; Phillips, GN; Watanabe, Y1
Boffi, A; Chiancone, E; Das, TK; Rousseau, DL1
Das, TK; Duff, SM; Hill, RD; Lee, HC; Peisach, J; Rousseau, DL; Wittenberg, BA; Wittenberg, JB1
Burstyn, JN; Chung, SY; Kerby, RL; Parks, RB; Reynolds, MF; Roberts, GP; Shelver, D; Thorsteinsson, MV1
Hori, H; Iizuka, T; Makino, R; Matsuda, H; Obayashi, E; Shiro, Y1
Hildebrand, DP; Liu, Y; Loehr, TM; Mauk, AG; Moënne-Loccoz, P; Ortiz de Montellano, PR; Wilks, A1
Ramadas, N; Rifkind, JM1
Bartunik, HD; Kachalova, GS; Popov, AN1
Boxer, SG; Dawson, JH; Dou, Y; Franzen, S; Hu, R; Ikeda-Saito, M; Ortiz de Montellano, PR; Pond, AE; Roach, MP; Rux, AH; Sono, M; Thomas, MR; Wilks, A; Woodruff, WH1
Daldal, F; Darrouzet, E; Knaff, DB; Li, J; Mandaci, S; Qin, H1
Sagnella, DE; Straub, JE1
Lu, Y; Wang, X1
de Montellano, PR; Knudsen, GM; Nishida, CR; Rodríguez-Crespo, I1
Kitagawa, T; Nagai, M; Nagatomo, S; Tsuneshige, A; Yonetani, T1
Chien, EY; McMahon, BH; Müller, JD; Nienhaus, GU; Sligar, SG1
Adachi, S; Hasnain, SS; Iizuka, T; Miyatake, H; Mukai, M; Nakamura, H; Shiro, Y; Strange, RW; Tamura, K1
Becker, OM; Margoliash, E; Navon, G; Qin, W; Schejter, A; Taler, G1
Dawson, JH; Lu, Y; Pond, AE; Sigman, JA1
Ortiz de Montellano, PR; Poulos, TL; Schuller, DJ; Wilks, A1
Bravo, J; Bujons, J; Ens, W; Fita, I; Hu, B; Loewen, PC; Maté, MJ; Sevinc, MS; Switala, J1
Abdur-Rashid, A; Baer, MT; Bracken, CS; Helms, W; Stojiljkovic, I1
Berendzen, J; Chu, K; Schlichting, I; Sweet, RM; Vojtechovský, J1
Hager, LP; Manoj, KM; Mroczko, M; Wang, X; Yi, X1
Bertini, I; Luchinat, C; Parigi, G; Walker, FA1
Koesling, D1
Barker, PD; Fearnley, IM; Rice, JK1
Babcock, GT; Cerda, JF; Choi, CY; Chu, HA; Marletta, MA1
Anthony, LC; Donohue, TJ; Falkowski, MJ; Newman, JD; Schilke, BA1
Chen, JJ; Guo, Y; Matts, RL; Uma, S; White, S1
Bruschi, M; Chottard, G; Kazanskaya, I1
Cho, YS; Pakrasi, HB; Whitmarsh, J1
Behr, J; Hellwig, P; Mäntele, W; Michel, H1
Ozaki, S; Roach, MP; Watanabe, Y1
Brunori, M; Cutruzzolà, F; Federici, L; Musto, R; Savino, C; Travaglini-Allocatelli, C1
Das, TK; Ferguson-Miller, S; Gennis, RB; Lee, HM; Mills, D; Rousseau, DL1
Boffi, A; Chiancone, E; Giangiacomo, L; Guarrera, L; Spagnuolo, C1
Bemski, G; Flores, M; Wajnberg, E1
Chu, GC; Ikeda-Saito, M; Katakura, K; Kayama, T; Sasahara, M; Sato, M; Sun, D; Tomita, T; Yoshida, T; Zhang, X1
Allen, JW; Chapman, SK; Ferguson, SJ; Koppenhöfer, A; Turner, KL1
Moënne-Loccoz, P; Wilks, A1
Nall, BT; Pierce, MM1
Feis, A; Howes, BD; Indiani, C; Marzocchi, MP; Smulevich, G1
Goodwin, DC; Marnett, LJ; Rowlinson, SW1
Ihara, M; Ishimori, K; Morishima, I; Takahashi, S1
Arakawa, T; Babcock, GT; Cerda, JF; Garavito, RM; Mulichak, AM; Seibold, SA; Smith, WL; Song, I1
Arp, DJ; Meek, L1
Chapman, SK; Cuthbertson, PM; Gordon, EH; Hill, AE; Pike, AD; Reid, GA1
Couture, M; Das, TK; Guertin, M; Ouellet, Y; Rousseau, DL; Savard, PY; Wittenberg, BA; Wittenberg, JB1
Turner, DL1
Fang, TY; Ho, C; Ho, NT; Lukin, JA; Simplaceanu, V; Zou, M1
Lukat-Rodgers, GS; Rodgers, KR; Rusnak, F; Wengenack, NL1
Gibson, QH; Olson, JS; Scott, EE1
Aono, S; Ishikawa, H; Ishimori, K; Kitagawa, T; Mizutani, Y; Morishima, I; Nakajima, H; Uchida, T1
Puspita, WJ; Roach, MP; Watanabe, Y1
Aki, M; Jin, Y; Kitagawa, T; Li, R; Nagai, M; Nagatomo, S; Sakai, H1
Bowler, BE; Nelson, CJ1
Iizuka, T; Mukai, M; Nakamura, H; Nakamura, K; Shiro, Y1
Chapman, SK; Cheesman, MR; Miles, CS; Mowat, CG; Munro, AW; Quaroni, LG; Reid, GA1
Aono, S; Honma, Y; Kato, T; Miyatake, H; Nakajima, H; Park, SY; Shiro, Y; Tawara, T1
Blankenship, J; Goodin, DB; Hirst, J; McRee, DE; Wilcox, SK; Williams, PA1
Ai, J; Goodin, DB; Hirst, J; Loehr, TM; Moënne-Loccoz, P; Wilcox, SK1
Brennan, L; Chapman, SK; Cuthbertson, PM; Pessanha, M; Reid, GA; Salgueiro, CA; Turner, DL; Xavier, AV1
Bhattacharya, S; Falzone, CJ; Lecomte, JT; Scott, NL; Vu, BC; Wang, Y1
Estabrook, RW; Gilep, AA; Guryev, OL; Usanov, SA1
Bailey, J; Boxer, SG; Dyer, RB; Franzen, S; Hu, RB; Thomas, MR; Woodruff, WH1
Brennan, L; Fareleira, P; Santos, H; Turner, DL1
Cao, W; Champion, PM; Christian, JF; Rosca, F; Sage, JT1
Falzone, CJ; Lecomte, JT; Scott, NL; Vu, BC1
Arciero, DM; Hooper, AB; Iverson, TM; Rees, DC1
Arnaudeau, S; Banfi, B; Demaurex, N; Hossle, JP; Krause, KH; Maturana, A; Ryser, S; Schlegel, W1
Gold, MH; Li, B; Renganathan, V; Rotsaert, FA1
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Quigg, A; Raee, E; Raibaud, P; Ramanitrahasimbola, D; Rapoport, L; Rasby, RJ; Rasoanirina, BNV; Raspini, B; Ratner, JR; Razafindrakoto, Z; Redd, MA; Ren, H; Ren, N; Rey, J; Reynolds, CP; Rich, PR; Richards, CJ; Rigol, M; Rimoldi, S; Robert, P; Rodrigues, AE; Roe, JH; Rohde, S; Rokita, JL; Roland, J; Rombaut, L; Ronkainen, J; Rothenberg, SM; Roy, SC; Ruan, Z; Rucker, PV; Rueda, D; Ruhwald, M; Rungrotmongkol, T; Rupert, AS; Rusjan, P; Ryabov, AD; Rysä, J; Saad, NES; Sabioni, P; Sadow, PM; Sahai, N; Salem, HF; Salinas, B; Salonurmi, T; Samé Guerra, D; Sánchez, J; Sanchez-González, J; Sanmamed, MF; Sansores-Peraza, P; Santoro, JC; Santschi, PH; Saritas, T; Sarkisova, Y; Savolainen, MJ; Scherberich, JE; Schlom, DG; Schmelz, EM; Schmid, MC; Schneider, MP; Schumacher, S; Schwartz, JC; Schwartzer, JJ; Schwehr, K; Schweitzer, DH; Scott, ME; Sedky, NK; See Hoe, L; Sejian, V; Selvaraju, S; Sen, SK; Seo, G; Šerý, O; Settles, JA; Sfar, S; Shaffer, J; Shan, GL; Shang, Q; Shannahan, JH; Shao, B; Shao, H; 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Reviews

24 review(s) available for histidine and heme

ArticleYear
Structure and mechanism of haemoglobin.
    British medical bulletin, 1976, Volume: 32, Issue:3

    Topics: Allosteric Regulation; Animals; Chemical Phenomena; Chemistry; Cobalt; Heme; Hemoglobins; Hemoglobins, Abnormal; Histidine; Horses; Humans; Iron; Lampreys; Ligands; Methemoglobin; Models, Structural; Myoglobin; Oxygen; Protein Conformation; Structure-Activity Relationship; Whales

1976
Prediction and comparison of the haem-binding sites in membrane haemoproteins.
    Biochimica et biophysica acta, 1989, Dec-07, Volume: 977, Issue:3

    Topics: Amino Acid Sequence; Animals; Binding Sites; Biological Evolution; Cytochrome b Group; Heme; Hemeproteins; Histidine; Membrane Proteins; Molecular Sequence Data; Quinones

1989
Amino acid sequence, haem-iron co-ordination geometry and functional properties of mitochondrial and bacterial c-type cytochromes.
    Quarterly reviews of biophysics, 1985, Volume: 18, Issue:2

    Topics: Amino Acid Sequence; Animals; Bacteria; Cytochrome c Group; Heme; Histidine; Iron; Ligands; Methionine; Mitochondria; Phylogeny; Protein Binding; Protein Conformation

1985
Inorganic nutrition.
    Annual review of microbiology, 1972, Volume: 26

    Topics: Bacteria; Blood Proteins; Carbon Dioxide; Cells, Cultured; Chelating Agents; Culture Media; Culture Techniques; Eukaryota; Fungi; Growth Substances; Heme; Histidine; Hydrogen-Ion Concentration; Hydroxamic Acids; Iron; Metals; Phenols; Phosphates; Sulfates; Trace Elements; Urea

1972
[Rotational dynamics of the heme in myoglobin].
    Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 1995, Volume: 40, Issue:9

    Topics: Globins; Heme; Histidine; Iron; Myoglobin; Oxygen; Protein Conformation; Rotation

1995
The construction of metal centers in proteins by rational design.
    Folding & design, 1998, Volume: 3, Issue:1

    Topics: Calcium; Enzymes; Heme; Histidine; Iron-Sulfur Proteins; Metals; Proteins

1998
Studying the structure and regulation of soluble guanylyl cyclase.
    Methods (San Diego, Calif.), 1999, Volume: 19, Issue:4

    Topics: Animals; Biochemistry; Cysteine; DNA Mutational Analysis; Enzyme Activation; Guanylate Cyclase; Heme; Histidine; Isoenzymes; Solubility

1999
Models of the bis-histidine-ligated electron-transferring cytochromes. Comparative geometric and electronic structure of low-spin ferro- and ferrihemes.
    Chemical reviews, 2004, Volume: 104, Issue:2

    Topics: Animals; Cytochromes; Electron Spin Resonance Spectroscopy; Electron Transport; Electrons; Heme; Histidine; Humans; Ligands; Models, Molecular; Molecular Structure

2004
The use of stable isotopes and spectroscopy to investigate the energy transducing function of cytochrome c oxidase.
    Biochimica et biophysica acta, 2004, Apr-12, Volume: 1655, Issue:1-3

    Topics: Animals; Cattle; Electrochemistry; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Energy Metabolism; Heme; Histidine; Manganese; Models, Biological; Nitrogen Isotopes; Oxygen Isotopes; Rhodobacter sphaeroides; Spectroscopy, Fourier Transform Infrared

2004
Redox reactions of hemoglobin.
    Antioxidants & redox signaling, 2004, Volume: 6, Issue:3

    Topics: Animals; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Hemoglobins; Histidine; Humans; Hydrogen Peroxide; Iron; Magnetics; Models, Chemical; Nitric Oxide; Nitrites; Oxidation-Reduction; Oxygen; Peroxynitrous Acid; Pressure; Superoxides; Temperature; Time Factors

2004
The heme environment of mouse neuroglobin: histidine imidazole plane orientations obtained from solution NMR and EPR spectroscopy as compared with X-ray crystallography.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2006, Volume: 11, Issue:4

    Topics: Animals; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Globins; Heme; Hemeproteins; Histidine; Humans; Imidazoles; Mice; Models, Molecular; Nerve Tissue Proteins; Neuroglobin; Nuclear Magnetic Resonance, Biomolecular

2006
Bis-histidine-coordinated hemes in four-helix bundles: how the geometry of the bundle controls the axial imidazole plane orientations in transmembrane cytochromes of mitochondrial complexes II and III and related proteins.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2008, Volume: 13, Issue:4

    Topics: Cell Membrane; Cytochromes; Heme; Histidine; Imidazoles; Mitochondria

2008
Structural and functional comparison of 2-His-1-carboxylate and 3-His metallocentres in non-haem iron(II)-dependent enzymes.
    Biochemical Society transactions, 2008, Volume: 36, Issue:Pt 6

    Topics: Amino Acid Motifs; Catalysis; Heme; Histidine; Iron; Proteins

2008
The chemistry and biochemistry of heme c: functional bases for covalent attachment.
    Natural product reports, 2008, Volume: 25, Issue:6

    Topics: Heme; Histidine; Models, Molecular; Molecular Structure

2008
Cytochromes: Reactivity of the "dark side" of the heme.
    Biophysical chemistry, 2010, Volume: 152, Issue:1-3

    Topics: Alcaligenes; Animals; Cardiolipins; Cytochrome c Group; Heme; Histidine; Horses; Models, Molecular; Nitric Oxide

2010
Occurrence and formation of endogenous histidine hexa-coordination in cold-adapted hemoglobins.
    IUBMB life, 2011, Volume: 63, Issue:5

    Topics: Adaptation, Biological; Animals; Cold Temperature; Crystallography, X-Ray; Heme; Hemeproteins; Hemoglobins; Histidine; Humans; Iron; Models, Molecular; Oxidation-Reduction; Protein Conformation

2011
The reaction mechanisms of heme catalases: an atomistic view by ab initio molecular dynamics.
    Archives of biochemistry and biophysics, 2012, Sep-15, Volume: 525, Issue:2

    Topics: Catalase; Catalysis; Electrons; Enzymes; Helicobacter pylori; Heme; Histidine; Hydrogen Peroxide; Models, Chemical; Models, Molecular; Molecular Conformation; Molecular Dynamics Simulation; Oxidation-Reduction; Oxidative Stress; Oxygen; Peroxidase; Protons; Singlet Oxygen

2012
Dynamic motion and rearranged molecular shape of heme in myoglobin: structural and functional consequences.
    Molecules (Basel, Switzerland), 2013, Mar-11, Volume: 18, Issue:3

    Topics: Carbon Monoxide; Crystallography, X-Ray; Heme; Histidine; Iron; Molecular Structure; Motion; Myoglobin; Nuclear Magnetic Resonance, Biomolecular; Oxygen; Rotation

2013
Multi-haem cytochromes in Shewanella oneidensis MR-1: structures, functions and opportunities.
    Journal of the Royal Society, Interface, 2015, Jan-06, Volume: 12, Issue:102

    Topics: Amino Acid Motifs; Biotechnology; Computer Simulation; Cytochromes; Cytoplasm; Electrodes; Electron Transport; Ferric Compounds; Heme; Histidine; Ligands; Models, Molecular; Oxidation-Reduction; Peptides; Protein Interaction Mapping; Shewanella; Spectrophotometry; Structure-Activity Relationship; Substrate Specificity

2015
Utility of heme analogues to intentionally modify heme-globin interactions in myoglobin.
    Biochimica et biophysica acta, 2016, Volume: 1857, Issue:5

    Topics: Animals; Electron Transport; Globins; Heme; Histidine; Humans; Iron; Magnetic Resonance Spectroscopy; Myoglobin; Protein Binding; Protein Interaction Mapping

2016
The role of the K-channel and the active-site tyrosine in the catalytic mechanism of cytochrome c oxidase.
    Biochimica et biophysica acta, 2016, Volume: 1857, Issue:8

    Topics: Animals; Biocatalysis; Catalytic Domain; Cattle; Copper; Electron Transport; Electron Transport Complex IV; Gene Expression; Heme; Histidine; Ion Transport; Mitochondria; Protons; Tyrosine

2016
Is there correlation between Aβ-heme peroxidase activity and the peptide aggregation state? A literature review combined with hypothesis.
    International journal of biological macromolecules, 2017, Volume: 100

    Topics: Amyloid beta-Peptides; Animals; Heme; Histidine; Humans; Peroxidases; Protein Aggregates; Protein Multimerization

2017
    The Egyptian journal of chest diseases and tuberculosis, 2016, Volume: 65, Issue:1

    Topics: A549 Cells; Acetylmuramyl-Alanyl-Isoglutamine; Acinetobacter baumannii; Acute Lung Injury; Adaptor Proteins, Signal Transducing; Adenine; Adenocarcinoma; Adipogenesis; Administration, Cutaneous; Administration, Ophthalmic; Adolescent; Adsorption; Adult; Aeromonas hydrophila; Aerosols; Aged; Aged, 80 and over; Aging; Agriculture; Air Pollutants; Air Pollution; Airway Remodeling; Alanine Transaminase; Albuminuria; Aldehyde Dehydrogenase 1 Family; Algorithms; AlkB Homolog 2, Alpha-Ketoglutarate-Dependent Dioxygenase; Alzheimer Disease; Amino Acid Sequence; Ammonia; Ammonium Compounds; Anaerobiosis; Anesthetics, Dissociative; Anesthetics, Inhalation; Animals; Anti-Bacterial Agents; Anti-HIV Agents; Anti-Infective Agents; Anti-Inflammatory Agents; Antibiotics, Antineoplastic; Antibodies, Antineutrophil Cytoplasmic; Antibodies, Monoclonal, Humanized; Antifungal Agents; Antigens, Bacterial; Antigens, CD; Antigens, Differentiation, Myelomonocytic; Antimetabolites, Antineoplastic; Antineoplastic Agents; Antineoplastic Combined Chemotherapy Protocols; Antioxidants; Antitubercular Agents; Antiviral Agents; Apolipoproteins E; Apoptosis; Arabidopsis; Arabidopsis Proteins; Arsenic; Arthritis, Rheumatoid; Asthma; Atherosclerosis; ATP-Dependent Proteases; Attitude of Health Personnel; Australia; Austria; Autophagy; Axitinib; Bacteria; Bacterial Outer Membrane Proteins; Bacterial Proteins; Bacterial Toxins; Bacterial Typing Techniques; Bariatric Surgery; Base Composition; Bayes Theorem; Benzoxazoles; Benzylamines; beta Catenin; Betacoronavirus; Betula; Binding Sites; Biological Availability; Biological Oxygen Demand Analysis; Biomarkers; Biomarkers, Tumor; Biopsy; Bioreactors; Biosensing Techniques; Birth Weight; Blindness; Blood Chemical Analysis; Blood Gas Analysis; Blood Glucose; Blood Pressure; Blood Pressure Monitoring, Ambulatory; Blood-Brain Barrier; Blotting, Western; Body Mass Index; Body Weight; Bone and Bones; Bone Density; Bone Resorption; Borates; Brain; Brain Infarction; Brain Injuries, Traumatic; Brain Neoplasms; Breakfast; Breast Milk Expression; Breast Neoplasms; Bronchi; Bronchoalveolar Lavage Fluid; Buffaloes; Cadherins; Calcification, Physiologic; Calcium Compounds; Calcium, Dietary; Cannula; Caprolactam; Carbon; Carbon Dioxide; Carboplatin; Carcinogenesis; Carcinoma, Ductal; Carcinoma, Ehrlich Tumor; Carcinoma, Hepatocellular; Carcinoma, Non-Small-Cell Lung; Carcinoma, Pancreatic Ductal; Carcinoma, Renal Cell; Cardiovascular Diseases; Carps; Carrageenan; Case-Control Studies; Catalysis; Catalytic Domain; Cattle; CD8-Positive T-Lymphocytes; Cell Adhesion; Cell Cycle Proteins; Cell Death; Cell Differentiation; Cell Line; Cell Line, Tumor; Cell Movement; Cell Nucleus; Cell Phone Use; Cell Proliferation; Cell Survival; Cell Transformation, Neoplastic; Cell Transformation, Viral; Cells, Cultured; Cellulose; Chemical Phenomena; Chemoradiotherapy; Child; Child Development; Child, Preschool; China; Chitosan; Chlorocebus aethiops; Cholecalciferol; Chromatography, Liquid; Circadian Clocks; Circadian Rhythm; Circular Dichroism; Cisplatin; Citric Acid; Clinical Competence; Clinical Laboratory Techniques; Clinical Trials, Phase I as Topic; Clinical Trials, Phase II as Topic; Clostridioides difficile; Clostridium Infections; Coculture Techniques; Cohort Studies; Cold Temperature; Colitis; Collagen Type I; Collagen Type I, alpha 1 Chain; Collagen Type XI; Color; Connective Tissue Diseases; Copper; Coronary Angiography; Coronavirus 3C Proteases; Coronavirus Infections; Cost of Illness; Counselors; COVID-19; COVID-19 Testing; Creatine Kinase; Creatinine; Cross-Over Studies; Cross-Sectional Studies; Cryoelectron Microscopy; Cryosurgery; Crystallography, X-Ray; Cues; Cultural Competency; Cultural Diversity; Curriculum; Cyclic AMP Response Element-Binding Protein; Cyclin-Dependent Kinase Inhibitor p21; Cycloparaffins; Cysteine Endopeptidases; Cytokines; Cytoplasm; Cytoprotection; Databases, Factual; Denitrification; Deoxycytidine; Diabetes Complications; Diabetes Mellitus; Diabetes Mellitus, Experimental; Diabetes Mellitus, Type 1; Diabetes Mellitus, Type 2; Diagnosis, Differential; Diatoms; Diet; Diet, High-Fat; Dietary Exposure; Diffusion Magnetic Resonance Imaging; Diketopiperazines; Dipeptidyl Peptidase 4; Dipeptidyl-Peptidase IV Inhibitors; Disease Models, Animal; Disease Progression; Disease-Free Survival; DNA; DNA Damage; DNA Glycosylases; DNA Repair; DNA-Binding Proteins; DNA, Bacterial; DNA, Viral; Docetaxel; Dose Fractionation, Radiation; Dose-Response Relationship, Drug; Down-Regulation; Doxorubicin; Drosophila; Drosophila melanogaster; Drug Carriers; Drug Delivery Systems; Drug Liberation; Drug Repositioning; Drug Resistance, Bacterial; Drug Resistance, Multiple, Bacterial; Drug Resistance, Neoplasm; Drug Screening Assays, Antitumor; Drug Synergism; Drug Therapy, Combination; Edema; Edible Grain; Education, Graduate; Education, Medical, Graduate; Education, Pharmacy; Ehlers-Danlos Syndrome; Electron Transport Complex III; Electron Transport Complex IV; Electronic Nicotine Delivery Systems; Emergency Service, Hospital; Empathy; Emulsions; Endothelial Cells; Endurance Training; Energy Intake; Enterovirus A, Human; Environment; Environmental Monitoring; Enzyme Assays; Enzyme Inhibitors; Epithelial Cells; Epithelial-Mesenchymal Transition; Epoxide Hydrolases; Epoxy Compounds; Erythrocyte Count; Erythrocytes; Escherichia coli; Escherichia coli Infections; Escherichia coli Proteins; Esophageal Neoplasms; Esophageal Squamous Cell Carcinoma; Esophagectomy; Estrogens; Etanercept; Ethiopia; Ethnicity; Ethylenes; Exanthema; Exercise; Exercise Test; Exercise Tolerance; Extracellular Matrix; Extracorporeal Membrane Oxygenation; Eye Infections, Fungal; False Negative Reactions; Fatty Acids; Fecal Microbiota Transplantation; Feces; Female; Femur Neck; Fermentation; Ferritins; Fetal Development; Fibroblast Growth Factor-23; Fibroblast Growth Factors; Fibroblasts; Fibroins; Fish Proteins; Flavanones; Flavonoids; Focus Groups; Follow-Up Studies; Food Handling; Food Supply; Food, Formulated; Forced Expiratory Volume; Forests; Fractures, Bone; Fruit and Vegetable Juices; Fusobacteria; G1 Phase Cell Cycle Checkpoints; G2 Phase Cell Cycle Checkpoints; Gamma Rays; Gastrectomy; Gastrointestinal Microbiome; Gastrointestinal Stromal Tumors; Gefitinib; Gels; Gemcitabine; Gene Amplification; Gene Expression; Gene Expression Regulation; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Neoplastic; Gene Expression Regulation, Plant; Gene Knockdown Techniques; Gene-Environment Interaction; Genotype; Germany; Glioma; Glomerular Filtration Rate; Glucagon; Glucocorticoids; Glycemic Control; Glycerol; Glycogen Synthase Kinase 3 beta; Glycolipids; Glycolysis; Goblet Cells; Gram-Negative Bacterial Infections; Granulocyte Colony-Stimulating Factor; Graphite; Greenhouse Effect; Guanidines; Haemophilus influenzae; HCT116 Cells; Health Knowledge, Attitudes, Practice; Health Personnel; Health Services Accessibility; Health Services Needs and Demand; Health Status Disparities; Healthy Volunteers; Heart Failure; Heart Rate; Heart Transplantation; Heart-Assist Devices; HEK293 Cells; Heme; Heme Oxygenase-1; Hemolysis; Hemorrhage; Hepatitis B; Hepatitis B e Antigens; Hepatitis B Surface Antigens; Hepatitis B virus; Hepatitis B, Chronic; Hepatocytes; Hexoses; High-Throughput Nucleotide Sequencing; Hippo Signaling Pathway; Histamine; Histamine Agonists; Histidine; Histone Deacetylase 2; HIV Infections; HIV Reverse Transcriptase; HIV-1; Homebound Persons; Homeodomain Proteins; Homosexuality, Male; Hospice and Palliative Care Nursing; HSP70 Heat-Shock Proteins; Humans; Hyaluronan Receptors; Hydrogen; Hydrogen Peroxide; Hydrogen-Ion Concentration; Hydrolysis; Hydroxymethylglutaryl-CoA Reductase Inhibitors; Hypoglycemia; Hypoglycemic Agents; Hypoxia; Idiopathic Interstitial Pneumonias; Imaging, Three-Dimensional; Imatinib Mesylate; Immunotherapy; Implementation Science; Incidence; INDEL Mutation; Induced Pluripotent Stem Cells; Industrial Waste; Infant; Infant, Newborn; Inflammation; Inflammation Mediators; Infliximab; Infusions, Intravenous; Inhibitory Concentration 50; Injections; Insecticides; Insulin-Like Growth Factor Binding Protein 5; Insulin-Secreting Cells; Interleukin-1; Interleukin-17; Interleukin-8; Internship and Residency; Intestines; Intracellular Signaling Peptides and Proteins; Ion Transport; Iridaceae; Iridoid Glucosides; Islets of Langerhans Transplantation; Isodon; Isoflurane; Isotopes; Italy; Joint Instability; Ketamine; Kidney; Kidney Failure, Chronic; Kidney Function Tests; Kidney Neoplasms; Kinetics; Klebsiella pneumoniae; Knee Joint; Kruppel-Like Factor 4; Kruppel-Like Transcription Factors; Lactate Dehydrogenase 5; Laparoscopy; Laser Therapy; Lasers, Semiconductor; Lasers, Solid-State; Laurates; Lead; Leukocyte L1 Antigen Complex; Leukocytes, Mononuclear; Light; Lipid Peroxidation; Lipopolysaccharides; Liposomes; Liver; Liver Cirrhosis; Liver Neoplasms; Liver Transplantation; Locomotion; Longitudinal Studies; Lopinavir; Lower Urinary Tract Symptoms; Lubricants; Lung; Lung Diseases, Interstitial; Lung Neoplasms; Lymphocyte Activation; Lymphocytes, Tumor-Infiltrating; Lymphoma, Mantle-Cell; Lysosomes; Macrophages; Male; Manganese Compounds; MAP Kinase Kinase 4; Mass Screening; Maternal Health; Medicine, Chinese Traditional; Melanoma, Experimental; Memantine; Membrane Glycoproteins; Membrane Proteins; Mesenchymal Stem Cell Transplantation; Metal Nanoparticles; Metalloendopeptidases; Metalloporphyrins; Methadone; Methane; Methicillin-Resistant Staphylococcus aureus; Mexico; Mice; Mice, Inbred BALB C; Mice, Inbred C57BL; Mice, Inbred ICR; Mice, Knockout; Mice, Nude; Mice, SCID; Mice, Transgenic; Microarray Analysis; Microbial Sensitivity Tests; Microbiota; Micronutrients; MicroRNAs; Microscopy, Confocal; Microsomes, Liver; Middle Aged; Milk; Milk, Human; Minority Groups; Mitochondria; Mitochondrial Membranes; Mitochondrial Proteins; Models, Animal; Models, Molecular; Molecular Conformation; Molecular Docking Simulation; Molecular Dynamics Simulation; Molecular Epidemiology; Molecular Structure; Molecular Weight; Multilocus Sequence Typing; Multimodal Imaging; Muscle Strength; Muscle, Skeletal; Muscular Diseases; Mutation; Mycobacterium tuberculosis; Myocardial Stunning; Myristates; NAD(P)H Dehydrogenase (Quinone); Nanocomposites; Nanogels; Nanoparticles; Nanotechnology; Naphthalenes; Nasal Cavity; National Health Programs; Necrosis; Needs Assessment; Neoadjuvant Therapy; Neonicotinoids; Neoplasm Invasiveness; Neoplasm Metastasis; Neoplasm Proteins; Neoplasm Recurrence, Local; Neoplasm Staging; Neoplasm Transplantation; Neoplasms; Neoplastic Stem Cells; Netherlands; Neuroblastoma; Neuroprotective Agents; Neutrophils; NF-kappa B; NFATC Transcription Factors; Nicotiana; Nicotine; Nitrates; Nitrification; Nitrites; Nitro Compounds; Nitrogen; Nitrogen Dioxide; North Carolina; Nuclear Magnetic Resonance, Biomolecular; Nuclear Proteins; Nucleic Acid Hybridization; Nucleosomes; Nutrients; Obesity; Obesity, Morbid; Oceans and Seas; Oncogene Protein v-akt; Oncogenes; Oocytes; Open Reading Frames; Osteoclasts; Osteogenesis; Osteoporosis; Osteoporosis, Postmenopausal; Outpatients; Ovarian Neoplasms; Ovariectomy; Overweight; Oxazines; Oxidants; Oxidation-Reduction; Oxidative Stress; Oxides; Oxidoreductases; Oxygen; Oxygen Inhalation Therapy; Oxygenators, Membrane; Ozone; Paclitaxel; Paenibacillus; Pain Measurement; Palliative Care; Pancreatic Neoplasms; Pandemics; Parasympathetic Nervous System; Particulate Matter; Pasteurization; Patient Preference; Patient Satisfaction; Pediatric Obesity; Permeability; Peroxiredoxins; Peroxynitrous Acid; Pharmaceutical Services; Pharmacists; Pharmacy; Phaseolus; Phenotype; Phoeniceae; Phosphates; Phosphatidylinositol 3-Kinases; Phospholipid Transfer Proteins; Phospholipids; Phosphorus; Phosphorylation; Photoperiod; Photosynthesis; Phylogeny; Physical Endurance; Physicians; Pilot Projects; Piperidines; Pituitary Adenylate Cyclase-Activating Polypeptide; Plant Extracts; Plant Leaves; Plant Proteins; Plant Roots; Plaque, Atherosclerotic; Pneumonia; Pneumonia, Viral; Point-of-Care Testing; Polyethylene Glycols; Polymers; Polysorbates; Pore Forming Cytotoxic Proteins; Positron Emission Tomography Computed Tomography; Positron-Emission Tomography; Postprandial Period; Poverty; Pre-Exposure Prophylaxis; Prediabetic State; Predictive Value of Tests; Pregnancy; Pregnancy Trimester, First; Pregnancy, High-Risk; Prenatal Exposure Delayed Effects; Pressure; Prevalence; Primary Graft Dysfunction; Primary Health Care; Professional Role; Professionalism; Prognosis; Progression-Free Survival; Prolactin; Promoter Regions, Genetic; Proof of Concept Study; Proportional Hazards Models; Propylene Glycol; Prospective Studies; Prostate; Protein Binding; Protein Biosynthesis; Protein Isoforms; Protein Kinase Inhibitors; Protein Phosphatase 2; Protein Processing, Post-Translational; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Protein Transport; Proteoglycans; Proteome; Proto-Oncogene Proteins c-akt; Proto-Oncogene Proteins c-myc; Proto-Oncogene Proteins c-ret; Proto-Oncogene Proteins p21(ras); Proton Pumps; Protons; Protoporphyrins; Pseudomonas aeruginosa; Pseudomonas fluorescens; Pulmonary Artery; Pulmonary Disease, Chronic Obstructive; Pulmonary Gas Exchange; Pulmonary Veins; Pyrazoles; Pyridines; Pyrimidines; Qualitative Research; Quinoxalines; Rabbits; Random Allocation; Rats; Rats, Sprague-Dawley; Rats, Wistar; Receptors, Histamine H3; Receptors, Immunologic; Receptors, Transferrin; Recombinant Proteins; Recurrence; Reference Values; Referral and Consultation; Regional Blood Flow; Registries; Regulon; Renal Insufficiency, Chronic; Reperfusion Injury; Repressor Proteins; Reproducibility of Results; Republic of Korea; Research Design; Resistance Training; Respiration, Artificial; Respiratory Distress Syndrome; Respiratory Insufficiency; Resuscitation; Retinal Dehydrogenase; Retreatment; Retrospective Studies; Reverse Transcriptase Inhibitors; Rhinitis, Allergic; Ribosomal Proteins; Ribosomes; Risk Assessment; Risk Factors; Ritonavir; Rivers; RNA Interference; RNA-Seq; RNA, Messenger; RNA, Ribosomal, 16S; RNA, Small Interfering; Rosuvastatin Calcium; Rural Population; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Salivary Ducts; Salivary Gland Neoplasms; San Francisco; SARS-CoV-2; Satiation; Satiety Response; Schools; Schools, Pharmacy; Seasons; Seawater; Selection, Genetic; Sequence Analysis, DNA; Serine-Threonine Kinase 3; Sewage; Sheep; Sheep, Domestic; Shock, Hemorrhagic; Signal Transduction; Silver; Silymarin; Single Photon Emission Computed Tomography Computed Tomography; Sirolimus; Sirtuin 1; Skin; Skin Neoplasms; Skin Physiological Phenomena; Sleep Initiation and Maintenance Disorders; Social Class; Social Participation; Social Support; Soil; Soil Microbiology; Solutions; Somatomedins; Soot; Specimen Handling; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis; Spinal Fractures; Spirometry; Staphylococcus aureus; STAT1 Transcription Factor; STAT3 Transcription Factor; Streptomyces coelicolor; Stress, Psychological; Stroke; Stroke Volume; Structure-Activity Relationship; Students, Medical; Students, Pharmacy; Substance Abuse Treatment Centers; Sulfur Dioxide; Surface Properties; Surface-Active Agents; Surveys and Questionnaires; Survival Analysis; Survival Rate; Survivin; Sweden; Swine; Swine, Miniature; Sympathetic Nervous System; T-Lymphocytes, Regulatory; Talaromyces; Tandem Mass Spectrometry; tau Proteins; Telemedicine; Telomerase; Telomere; Telomere Homeostasis; Temperature; Terminally Ill; Th1 Cells; Thiamethoxam; Thiazoles; Thiophenes; Thioredoxin Reductase 1; Thrombosis; Thulium; Thyroid Cancer, Papillary; Thyroid Carcinoma, Anaplastic; Thyroid Neoplasms; Time Factors; Titanium; Tomography, Emission-Computed, Single-Photon; Tomography, X-Ray Computed; TOR Serine-Threonine Kinases; Transcription Factor AP-1; Transcription Factors; Transcription, Genetic; Transcriptional Activation; Transcriptome; Transforming Growth Factor beta1; Transistors, Electronic; Translational Research, Biomedical; Transplantation Tolerance; Transplantation, Homologous; Transportation; Treatment Outcome; Tretinoin; Tuberculosis, Multidrug-Resistant; Tuberculosis, Pulmonary; Tubulin Modulators; Tumor Microenvironment; Tumor Necrosis Factor Inhibitors; Tumor Necrosis Factor-alpha; Twins; Ultrasonic Therapy; Ultrasonography; Ultraviolet Rays; United States; Up-Regulation; Uranium; Urethra; Urinary Bladder; Urodynamics; Uromodulin; Uveitis; Vasoconstrictor Agents; Ventricular Function, Left; Vero Cells; Vesicular Transport Proteins; Viral Nonstructural Proteins; Visual Acuity; Vital Capacity; Vitamin D; Vitamin D Deficiency; Vitamin K 2; Vitamins; Volatilization; Voriconazole; Waiting Lists; Waste Disposal, Fluid; Wastewater; Water Pollutants, Chemical; Whole Genome Sequencing; Wine; Wnt Signaling Pathway; Wound Healing; Wounds and Injuries; WW Domains; X-linked Nuclear Protein; X-Ray Diffraction; Xanthines; Xenograft Model Antitumor Assays; YAP-Signaling Proteins; Yogurt; Young Adult; Zebrafish; Zebrafish Proteins; Ziziphus

2016
The histidine brace: nature's copper alternative to haem?
    FEBS letters, 2023, Volume: 597, Issue:4

    Topics: Copper; Heme; Histidine; Oxidation-Reduction

2023

Trials

1 trial(s) available for histidine and heme

ArticleYear
    The Egyptian journal of chest diseases and tuberculosis, 2016, Volume: 65, Issue:1

    Topics: A549 Cells; Acetylmuramyl-Alanyl-Isoglutamine; Acinetobacter baumannii; Acute Lung Injury; Adaptor Proteins, Signal Transducing; Adenine; Adenocarcinoma; Adipogenesis; Administration, Cutaneous; Administration, Ophthalmic; Adolescent; Adsorption; Adult; Aeromonas hydrophila; Aerosols; Aged; Aged, 80 and over; Aging; Agriculture; Air Pollutants; Air Pollution; Airway Remodeling; Alanine Transaminase; Albuminuria; Aldehyde Dehydrogenase 1 Family; Algorithms; AlkB Homolog 2, Alpha-Ketoglutarate-Dependent Dioxygenase; Alzheimer Disease; Amino Acid Sequence; Ammonia; Ammonium Compounds; Anaerobiosis; Anesthetics, Dissociative; Anesthetics, Inhalation; Animals; Anti-Bacterial Agents; Anti-HIV Agents; Anti-Infective Agents; Anti-Inflammatory Agents; Antibiotics, Antineoplastic; Antibodies, Antineutrophil Cytoplasmic; Antibodies, Monoclonal, Humanized; Antifungal Agents; Antigens, Bacterial; Antigens, CD; Antigens, Differentiation, Myelomonocytic; Antimetabolites, Antineoplastic; Antineoplastic Agents; Antineoplastic Combined Chemotherapy Protocols; Antioxidants; Antitubercular Agents; Antiviral Agents; Apolipoproteins E; Apoptosis; Arabidopsis; Arabidopsis Proteins; Arsenic; Arthritis, Rheumatoid; Asthma; Atherosclerosis; ATP-Dependent Proteases; Attitude of Health Personnel; Australia; Austria; Autophagy; Axitinib; Bacteria; Bacterial Outer Membrane Proteins; Bacterial Proteins; Bacterial Toxins; Bacterial Typing Techniques; Bariatric Surgery; Base Composition; Bayes Theorem; Benzoxazoles; Benzylamines; beta Catenin; Betacoronavirus; Betula; Binding Sites; Biological Availability; Biological Oxygen Demand Analysis; Biomarkers; Biomarkers, Tumor; Biopsy; Bioreactors; Biosensing Techniques; Birth Weight; Blindness; Blood Chemical Analysis; Blood Gas Analysis; Blood Glucose; Blood Pressure; Blood Pressure Monitoring, Ambulatory; Blood-Brain Barrier; Blotting, Western; Body Mass Index; Body Weight; Bone and Bones; Bone Density; Bone Resorption; Borates; Brain; Brain Infarction; Brain Injuries, Traumatic; Brain Neoplasms; Breakfast; Breast Milk Expression; Breast Neoplasms; Bronchi; Bronchoalveolar Lavage Fluid; Buffaloes; Cadherins; Calcification, Physiologic; Calcium Compounds; Calcium, Dietary; Cannula; Caprolactam; Carbon; Carbon Dioxide; Carboplatin; Carcinogenesis; Carcinoma, Ductal; Carcinoma, Ehrlich Tumor; Carcinoma, Hepatocellular; Carcinoma, Non-Small-Cell Lung; Carcinoma, Pancreatic Ductal; Carcinoma, Renal Cell; Cardiovascular Diseases; Carps; Carrageenan; Case-Control Studies; Catalysis; Catalytic Domain; Cattle; CD8-Positive T-Lymphocytes; Cell Adhesion; Cell Cycle Proteins; Cell Death; Cell Differentiation; Cell Line; Cell Line, Tumor; Cell Movement; Cell Nucleus; Cell Phone Use; Cell Proliferation; Cell Survival; Cell Transformation, Neoplastic; Cell Transformation, Viral; Cells, Cultured; Cellulose; Chemical Phenomena; Chemoradiotherapy; Child; Child Development; Child, Preschool; China; Chitosan; Chlorocebus aethiops; Cholecalciferol; Chromatography, Liquid; Circadian Clocks; Circadian Rhythm; Circular Dichroism; Cisplatin; Citric Acid; Clinical Competence; Clinical Laboratory Techniques; Clinical Trials, Phase I as Topic; Clinical Trials, Phase II as Topic; Clostridioides difficile; Clostridium Infections; Coculture Techniques; Cohort Studies; Cold Temperature; Colitis; Collagen Type I; Collagen Type I, alpha 1 Chain; Collagen Type XI; Color; Connective Tissue Diseases; Copper; Coronary Angiography; Coronavirus 3C Proteases; Coronavirus Infections; Cost of Illness; Counselors; COVID-19; COVID-19 Testing; Creatine Kinase; Creatinine; Cross-Over Studies; Cross-Sectional Studies; Cryoelectron Microscopy; Cryosurgery; Crystallography, X-Ray; Cues; Cultural Competency; Cultural Diversity; Curriculum; Cyclic AMP Response Element-Binding Protein; Cyclin-Dependent Kinase Inhibitor p21; Cycloparaffins; Cysteine Endopeptidases; Cytokines; Cytoplasm; Cytoprotection; Databases, Factual; Denitrification; Deoxycytidine; Diabetes Complications; Diabetes Mellitus; Diabetes Mellitus, Experimental; Diabetes Mellitus, Type 1; Diabetes Mellitus, Type 2; Diagnosis, Differential; Diatoms; Diet; Diet, High-Fat; Dietary Exposure; Diffusion Magnetic Resonance Imaging; Diketopiperazines; Dipeptidyl Peptidase 4; Dipeptidyl-Peptidase IV Inhibitors; Disease Models, Animal; Disease Progression; Disease-Free Survival; DNA; DNA Damage; DNA Glycosylases; DNA Repair; DNA-Binding Proteins; DNA, Bacterial; DNA, Viral; Docetaxel; Dose Fractionation, Radiation; Dose-Response Relationship, Drug; Down-Regulation; Doxorubicin; Drosophila; Drosophila melanogaster; Drug Carriers; Drug Delivery Systems; Drug Liberation; Drug Repositioning; Drug Resistance, Bacterial; Drug Resistance, Multiple, Bacterial; Drug Resistance, Neoplasm; Drug Screening Assays, Antitumor; Drug Synergism; Drug Therapy, Combination; Edema; Edible Grain; Education, Graduate; Education, Medical, Graduate; Education, Pharmacy; Ehlers-Danlos Syndrome; Electron Transport Complex III; Electron Transport Complex IV; Electronic Nicotine Delivery Systems; Emergency Service, Hospital; Empathy; Emulsions; Endothelial Cells; Endurance Training; Energy Intake; Enterovirus A, Human; Environment; Environmental Monitoring; Enzyme Assays; Enzyme Inhibitors; Epithelial Cells; Epithelial-Mesenchymal Transition; Epoxide Hydrolases; Epoxy Compounds; Erythrocyte Count; Erythrocytes; Escherichia coli; Escherichia coli Infections; Escherichia coli Proteins; Esophageal Neoplasms; Esophageal Squamous Cell Carcinoma; Esophagectomy; Estrogens; Etanercept; Ethiopia; Ethnicity; Ethylenes; Exanthema; Exercise; Exercise Test; Exercise Tolerance; Extracellular Matrix; Extracorporeal Membrane Oxygenation; Eye Infections, Fungal; False Negative Reactions; Fatty Acids; Fecal Microbiota Transplantation; Feces; Female; Femur Neck; Fermentation; Ferritins; Fetal Development; Fibroblast Growth Factor-23; Fibroblast Growth Factors; Fibroblasts; Fibroins; Fish Proteins; Flavanones; Flavonoids; Focus Groups; Follow-Up Studies; Food Handling; Food Supply; Food, Formulated; Forced Expiratory Volume; Forests; Fractures, Bone; Fruit and Vegetable Juices; Fusobacteria; G1 Phase Cell Cycle Checkpoints; G2 Phase Cell Cycle Checkpoints; Gamma Rays; Gastrectomy; Gastrointestinal Microbiome; Gastrointestinal Stromal Tumors; Gefitinib; Gels; Gemcitabine; Gene Amplification; Gene Expression; Gene Expression Regulation; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Neoplastic; Gene Expression Regulation, Plant; Gene Knockdown Techniques; Gene-Environment Interaction; Genotype; Germany; Glioma; Glomerular Filtration Rate; Glucagon; Glucocorticoids; Glycemic Control; Glycerol; Glycogen Synthase Kinase 3 beta; Glycolipids; Glycolysis; Goblet Cells; Gram-Negative Bacterial Infections; Granulocyte Colony-Stimulating Factor; Graphite; Greenhouse Effect; Guanidines; Haemophilus influenzae; HCT116 Cells; Health Knowledge, Attitudes, Practice; Health Personnel; Health Services Accessibility; Health Services Needs and Demand; Health Status Disparities; Healthy Volunteers; Heart Failure; Heart Rate; Heart Transplantation; Heart-Assist Devices; HEK293 Cells; Heme; Heme Oxygenase-1; Hemolysis; Hemorrhage; Hepatitis B; Hepatitis B e Antigens; Hepatitis B Surface Antigens; Hepatitis B virus; Hepatitis B, Chronic; Hepatocytes; Hexoses; High-Throughput Nucleotide Sequencing; Hippo Signaling Pathway; Histamine; Histamine Agonists; Histidine; Histone Deacetylase 2; HIV Infections; HIV Reverse Transcriptase; HIV-1; Homebound Persons; Homeodomain Proteins; Homosexuality, Male; Hospice and Palliative Care Nursing; HSP70 Heat-Shock Proteins; Humans; Hyaluronan Receptors; Hydrogen; Hydrogen Peroxide; Hydrogen-Ion Concentration; Hydrolysis; Hydroxymethylglutaryl-CoA Reductase Inhibitors; Hypoglycemia; Hypoglycemic Agents; Hypoxia; Idiopathic Interstitial Pneumonias; Imaging, Three-Dimensional; Imatinib Mesylate; Immunotherapy; Implementation Science; Incidence; INDEL Mutation; Induced Pluripotent Stem Cells; Industrial Waste; Infant; Infant, Newborn; Inflammation; Inflammation Mediators; Infliximab; Infusions, Intravenous; Inhibitory Concentration 50; Injections; Insecticides; Insulin-Like Growth Factor Binding Protein 5; Insulin-Secreting Cells; Interleukin-1; Interleukin-17; Interleukin-8; Internship and Residency; Intestines; Intracellular Signaling Peptides and Proteins; Ion Transport; Iridaceae; Iridoid Glucosides; Islets of Langerhans Transplantation; Isodon; Isoflurane; Isotopes; Italy; Joint Instability; Ketamine; Kidney; Kidney Failure, Chronic; Kidney Function Tests; Kidney Neoplasms; Kinetics; Klebsiella pneumoniae; Knee Joint; Kruppel-Like Factor 4; Kruppel-Like Transcription Factors; Lactate Dehydrogenase 5; Laparoscopy; Laser Therapy; Lasers, Semiconductor; Lasers, Solid-State; Laurates; Lead; Leukocyte L1 Antigen Complex; Leukocytes, Mononuclear; Light; Lipid Peroxidation; Lipopolysaccharides; Liposomes; Liver; Liver Cirrhosis; Liver Neoplasms; Liver Transplantation; Locomotion; Longitudinal Studies; Lopinavir; Lower Urinary Tract Symptoms; Lubricants; Lung; Lung Diseases, Interstitial; Lung Neoplasms; Lymphocyte Activation; Lymphocytes, Tumor-Infiltrating; Lymphoma, Mantle-Cell; Lysosomes; Macrophages; Male; Manganese Compounds; MAP Kinase Kinase 4; Mass Screening; Maternal Health; Medicine, Chinese Traditional; Melanoma, Experimental; Memantine; Membrane Glycoproteins; Membrane Proteins; Mesenchymal Stem Cell Transplantation; Metal Nanoparticles; Metalloendopeptidases; Metalloporphyrins; Methadone; Methane; Methicillin-Resistant Staphylococcus aureus; Mexico; Mice; Mice, Inbred BALB C; Mice, Inbred C57BL; Mice, Inbred ICR; Mice, Knockout; Mice, Nude; Mice, SCID; Mice, Transgenic; Microarray Analysis; Microbial Sensitivity Tests; Microbiota; Micronutrients; MicroRNAs; Microscopy, Confocal; Microsomes, Liver; Middle Aged; Milk; Milk, Human; Minority Groups; Mitochondria; Mitochondrial Membranes; Mitochondrial Proteins; Models, Animal; Models, Molecular; Molecular Conformation; Molecular Docking Simulation; Molecular Dynamics Simulation; Molecular Epidemiology; Molecular Structure; Molecular Weight; Multilocus Sequence Typing; Multimodal Imaging; Muscle Strength; Muscle, Skeletal; Muscular Diseases; Mutation; Mycobacterium tuberculosis; Myocardial Stunning; Myristates; NAD(P)H Dehydrogenase (Quinone); Nanocomposites; Nanogels; Nanoparticles; Nanotechnology; Naphthalenes; Nasal Cavity; National Health Programs; Necrosis; Needs Assessment; Neoadjuvant Therapy; Neonicotinoids; Neoplasm Invasiveness; Neoplasm Metastasis; Neoplasm Proteins; Neoplasm Recurrence, Local; Neoplasm Staging; Neoplasm Transplantation; Neoplasms; Neoplastic Stem Cells; Netherlands; Neuroblastoma; Neuroprotective Agents; Neutrophils; NF-kappa B; NFATC Transcription Factors; Nicotiana; Nicotine; Nitrates; Nitrification; Nitrites; Nitro Compounds; Nitrogen; Nitrogen Dioxide; North Carolina; Nuclear Magnetic Resonance, Biomolecular; Nuclear Proteins; Nucleic Acid Hybridization; Nucleosomes; Nutrients; Obesity; Obesity, Morbid; Oceans and Seas; Oncogene Protein v-akt; Oncogenes; Oocytes; Open Reading Frames; Osteoclasts; Osteogenesis; Osteoporosis; Osteoporosis, Postmenopausal; Outpatients; Ovarian Neoplasms; Ovariectomy; Overweight; Oxazines; Oxidants; Oxidation-Reduction; Oxidative Stress; Oxides; Oxidoreductases; Oxygen; Oxygen Inhalation Therapy; Oxygenators, Membrane; Ozone; Paclitaxel; Paenibacillus; Pain Measurement; Palliative Care; Pancreatic Neoplasms; Pandemics; Parasympathetic Nervous System; Particulate Matter; Pasteurization; Patient Preference; Patient Satisfaction; Pediatric Obesity; Permeability; Peroxiredoxins; Peroxynitrous Acid; Pharmaceutical Services; Pharmacists; Pharmacy; Phaseolus; Phenotype; Phoeniceae; Phosphates; Phosphatidylinositol 3-Kinases; Phospholipid Transfer Proteins; Phospholipids; Phosphorus; Phosphorylation; Photoperiod; Photosynthesis; Phylogeny; Physical Endurance; Physicians; Pilot Projects; Piperidines; Pituitary Adenylate Cyclase-Activating Polypeptide; Plant Extracts; Plant Leaves; Plant Proteins; Plant Roots; Plaque, Atherosclerotic; Pneumonia; Pneumonia, Viral; Point-of-Care Testing; Polyethylene Glycols; Polymers; Polysorbates; Pore Forming Cytotoxic Proteins; Positron Emission Tomography Computed Tomography; Positron-Emission Tomography; Postprandial Period; Poverty; Pre-Exposure Prophylaxis; Prediabetic State; Predictive Value of Tests; Pregnancy; Pregnancy Trimester, First; Pregnancy, High-Risk; Prenatal Exposure Delayed Effects; Pressure; Prevalence; Primary Graft Dysfunction; Primary Health Care; Professional Role; Professionalism; Prognosis; Progression-Free Survival; Prolactin; Promoter Regions, Genetic; Proof of Concept Study; Proportional Hazards Models; Propylene Glycol; Prospective Studies; Prostate; Protein Binding; Protein Biosynthesis; Protein Isoforms; Protein Kinase Inhibitors; Protein Phosphatase 2; Protein Processing, Post-Translational; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Protein Transport; Proteoglycans; Proteome; Proto-Oncogene Proteins c-akt; Proto-Oncogene Proteins c-myc; Proto-Oncogene Proteins c-ret; Proto-Oncogene Proteins p21(ras); Proton Pumps; Protons; Protoporphyrins; Pseudomonas aeruginosa; Pseudomonas fluorescens; Pulmonary Artery; Pulmonary Disease, Chronic Obstructive; Pulmonary Gas Exchange; Pulmonary Veins; Pyrazoles; Pyridines; Pyrimidines; Qualitative Research; Quinoxalines; Rabbits; Random Allocation; Rats; Rats, Sprague-Dawley; Rats, Wistar; Receptors, Histamine H3; Receptors, Immunologic; Receptors, Transferrin; Recombinant Proteins; Recurrence; Reference Values; Referral and Consultation; Regional Blood Flow; Registries; Regulon; Renal Insufficiency, Chronic; Reperfusion Injury; Repressor Proteins; Reproducibility of Results; Republic of Korea; Research Design; Resistance Training; Respiration, Artificial; Respiratory Distress Syndrome; Respiratory Insufficiency; Resuscitation; Retinal Dehydrogenase; Retreatment; Retrospective Studies; Reverse Transcriptase Inhibitors; Rhinitis, Allergic; Ribosomal Proteins; Ribosomes; Risk Assessment; Risk Factors; Ritonavir; Rivers; RNA Interference; RNA-Seq; RNA, Messenger; RNA, Ribosomal, 16S; RNA, Small Interfering; Rosuvastatin Calcium; Rural Population; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Salivary Ducts; Salivary Gland Neoplasms; San Francisco; SARS-CoV-2; Satiation; Satiety Response; Schools; Schools, Pharmacy; Seasons; Seawater; Selection, Genetic; Sequence Analysis, DNA; Serine-Threonine Kinase 3; Sewage; Sheep; Sheep, Domestic; Shock, Hemorrhagic; Signal Transduction; Silver; Silymarin; Single Photon Emission Computed Tomography Computed Tomography; Sirolimus; Sirtuin 1; Skin; Skin Neoplasms; Skin Physiological Phenomena; Sleep Initiation and Maintenance Disorders; Social Class; Social Participation; Social Support; Soil; Soil Microbiology; Solutions; Somatomedins; Soot; Specimen Handling; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis; Spinal Fractures; Spirometry; Staphylococcus aureus; STAT1 Transcription Factor; STAT3 Transcription Factor; Streptomyces coelicolor; Stress, Psychological; Stroke; Stroke Volume; Structure-Activity Relationship; Students, Medical; Students, Pharmacy; Substance Abuse Treatment Centers; Sulfur Dioxide; Surface Properties; Surface-Active Agents; Surveys and Questionnaires; Survival Analysis; Survival Rate; Survivin; Sweden; Swine; Swine, Miniature; Sympathetic Nervous System; T-Lymphocytes, Regulatory; Talaromyces; Tandem Mass Spectrometry; tau Proteins; Telemedicine; Telomerase; Telomere; Telomere Homeostasis; Temperature; Terminally Ill; Th1 Cells; Thiamethoxam; Thiazoles; Thiophenes; Thioredoxin Reductase 1; Thrombosis; Thulium; Thyroid Cancer, Papillary; Thyroid Carcinoma, Anaplastic; Thyroid Neoplasms; Time Factors; Titanium; Tomography, Emission-Computed, Single-Photon; Tomography, X-Ray Computed; TOR Serine-Threonine Kinases; Transcription Factor AP-1; Transcription Factors; Transcription, Genetic; Transcriptional Activation; Transcriptome; Transforming Growth Factor beta1; Transistors, Electronic; Translational Research, Biomedical; Transplantation Tolerance; Transplantation, Homologous; Transportation; Treatment Outcome; Tretinoin; Tuberculosis, Multidrug-Resistant; Tuberculosis, Pulmonary; Tubulin Modulators; Tumor Microenvironment; Tumor Necrosis Factor Inhibitors; Tumor Necrosis Factor-alpha; Twins; Ultrasonic Therapy; Ultrasonography; Ultraviolet Rays; United States; Up-Regulation; Uranium; Urethra; Urinary Bladder; Urodynamics; Uromodulin; Uveitis; Vasoconstrictor Agents; Ventricular Function, Left; Vero Cells; Vesicular Transport Proteins; Viral Nonstructural Proteins; Visual Acuity; Vital Capacity; Vitamin D; Vitamin D Deficiency; Vitamin K 2; Vitamins; Volatilization; Voriconazole; Waiting Lists; Waste Disposal, Fluid; Wastewater; Water Pollutants, Chemical; Whole Genome Sequencing; Wine; Wnt Signaling Pathway; Wound Healing; Wounds and Injuries; WW Domains; X-linked Nuclear Protein; X-Ray Diffraction; Xanthines; Xenograft Model Antitumor Assays; YAP-Signaling Proteins; Yogurt; Young Adult; Zebrafish; Zebrafish Proteins; Ziziphus

2016

Other Studies

721 other study(ies) available for histidine and heme

ArticleYear
A proton magnetic resonance study of the distal histidine of soybean Leghemoglobin. Effects of nicotinate and other heme ligands.
    The Journal of biological chemistry, 1978, Apr-10, Volume: 253, Issue:7

    Topics: Binding Sites; Glycine max; Heme; Hemeproteins; Histidine; Hydrogen-Ion Concentration; Kinetics; Leghemoglobin; Magnetic Resonance Spectroscopy; Nicotinic Acids; Protein Conformation

1978
Near-heme histidine residues of deoxy- and oxymyoglobins.
    Biochemistry, 1979, Apr-17, Volume: 18, Issue:8

    Topics: Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Myoglobin

1979
Evidence for the existence of a low spin complex in acidic methemoglobin: its structure and formation.
    Biochimica et biophysica acta, 1975, Jun-26, Volume: 393, Issue:2

    Topics: Allosteric Site; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Magnetics; Methemoglobin; Optical Rotation; Spectrum Analysis; Temperature

1975
Mechanism of tertiary structural change in hemoglobin.
    Proceedings of the National Academy of Sciences of the United States of America, 1977, Volume: 74, Issue:3

    Topics: Amino Acid Sequence; Globins; Heme; Hemoglobins; Histidine; Humans; Ligands; Models, Biological; Models, Molecular; Oxyhemoglobins; Protein Conformation; Thermodynamics; Valine

1977
Identification of the haem ligands of cytochrome b562 by X-ray and NMR methods.
    Nature, 1978, Sep-21, Volume: 275, Issue:5677

    Topics: Amino Acid Sequence; Cytochromes; Escherichia coli; Heme; Histidine; Ligands; Magnetic Resonance Spectroscopy; Methionine; Protein Conformation; X-Ray Diffraction

1978
Structure of oxymyoglobin.
    Nature, 1978, May-18, Volume: 273, Issue:5659

    Topics: Animals; Heme; Histidine; Iron; Myoglobin; Oxygen; Protein Conformation; Whales; X-Ray Diffraction

1978
Human serum histidine-rich glycoprotein. I. Interactions with heme, metal ions and organic ligands.
    Biochimica et biophysica acta, 1978, Aug-21, Volume: 535, Issue:2

    Topics: Amino Acids; Carrier Proteins; Cations, Divalent; Chemical Phenomena; Chemistry; Glycoproteins; Heme; Histidine; Humans; Ligands; Macromolecular Substances; Protein Binding; Protein Conformation

1978
Amino-acid sequences of heme-linked, histidine-containing peptides of five peroxidases from horseradish and turnip.
    European journal of biochemistry, 1977, Mar-01, Volume: 73, Issue:2

    Topics: Amino Acid Sequence; Amino Acids; Heme; Histidine; Horseradish Peroxidase; Peptide Fragments; Peroxidases; Plants; Species Specificity; Trypsin

1977
Chemical modification of histidine residues of rabbit hemopexin.
    Archives of biochemistry and biophysics, 1976, Volume: 176, Issue:2

    Topics: Acetates; Animals; Apoproteins; Arginine; Binding Sites; Heme; Hemopexin; Histidine; Kinetics; Lysine; Porphyrins; Protein Binding; Protein Conformation; Rabbits; Spectrophotometry; Spectrophotometry, Ultraviolet

1976
[Structure of nitroso pigments in meats].
    Annales de la nutrition et de l'alimentation, 1976, Volume: 30, Issue:5-6

    Topics: Amino Acids; Ascorbic Acid; Chemical Phenomena; Chemistry; Cysteine; Food Preservation; Heme; Histidine; Meat; Models, Chemical; Nitroso Compounds; Pigments, Biological; Pyrroles

1976
Evolution of the haem-haem interaction in vertebrate haemoglobins - a hypothesis.
    Journal of molecular evolution, 1975, Nov-04, Volume: 6, Issue:3

    Topics: Animals; Biological Evolution; Cyanides; Heme; Hemoglobins; Histidine; Humans; Models, Biological; Mutation; Myoglobin; Oxygen; Protein Conformation; Species Specificity; Vertebrates

1975
An infrared study of NO bonding to heme B and hemoglobin A. Evidence for inositol hexaphosphate induced cleavage of proximal histidine to iron bonds.
    Biochemistry, 1976, Jan-27, Volume: 15, Issue:2

    Topics: Binding Sites; Heme; Hemoglobins; Histidine; Humans; Inositol; Iron; Models, Molecular; Molecular Conformation; Nitric Oxide; Phytic Acid; Protein Binding; Protein Conformation; Spectrophotometry, Infrared

1976
Proton NMR study of coordinated imidazoles in low-spin ferric heme complexes. Assignment of single proton histidine resonance in hemoproteins.
    Biochimica et biophysica acta, 1976, Mar-25, Volume: 428, Issue:1

    Topics: Chemical Phenomena; Chemistry; Cyanides; Cytochromes; Heme; Hemeproteins; Histidine; Imidazoles; Ligands; Magnetic Resonance Spectroscopy; Porphyrins

1976
Determination of the ligands of the low spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis.
    The Journal of biological chemistry, 1992, Jan-25, Volume: 267, Issue:3

    Topics: Amino Acid Sequence; Base Sequence; Dithionite; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Escherichia coli; Genetic Complementation Test; Genotype; Heme; Histidine; Ligands; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Plasmids; Protein Conformation; Recombinant Proteins; Restriction Mapping; Thermodynamics

1992
Definition of the catalytic site of cytochrome c oxidase: specific ligands of heme a and the heme a3-CuB center.
    Proceedings of the National Academy of Sciences of the United States of America, 1992, Jun-01, Volume: 89, Issue:11

    Topics: Amino Acid Sequence; Binding Sites; Copper; Electron Transport Complex IV; Heme; Histidine; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Conformation; Rhodobacter sphaeroides; Spectrum Analysis; Spectrum Analysis, Raman

1992
Proton nuclear Overhauser effect study of the heme active site structure of Coprinus macrorhizus peroxidase.
    Biochimica et biophysica acta, 1992, Jul-13, Volume: 1122, Issue:1

    Topics: Binding Sites; Chemical Phenomena; Chemistry, Physical; Coprinus; Cytochrome-c Peroxidase; Heme; Histidine; Horseradish Peroxidase; Hydroxamic Acids; Magnetic Resonance Spectroscopy; Peroxidase

1992
Site-directed mutants of human myeloperoxidase. A topological approach to the heme-binding site.
    FEBS letters, 1992, May-11, Volume: 302, Issue:2

    Topics: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; CHO Cells; Cricetinae; DNA; Heme; Histidine; Humans; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Peroxidase; Recombinant Proteins; Spectrophotometry; Transfection

1992
Ionization of the heme propionate substituents in pseudomonad cytochromes c-551.
    FEBS letters, 1992, Oct-26, Volume: 311, Issue:3

    Topics: Amino Acid Sequence; Bacterial Proteins; Cytochrome c Group; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Pseudomonas; Pseudomonas aeruginosa; Valine

1992
Modification of the distal histidyl imidazole in myoglobin to N-tetrazole-substituted imidazole and its effects on the heme environmental structure and ligand binding properties.
    Biochemistry, 1992, Sep-15, Volume: 31, Issue:36

    Topics: Animals; Cyanogen Bromide; Ferric Compounds; Heme; Histidine; Ligands; Magnetic Resonance Spectroscopy; Myoglobin; Nitrogen Isotopes; Protein Conformation; Tetrazoles; Whales

1992
Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants.
    The Journal of biological chemistry, 1992, Nov-15, Volume: 267, Issue:32

    Topics: Circular Dichroism; Escherichia coli; Heme; Histidine; Humans; Iron; Mutagenesis, Site-Directed; Myoglobin; Protein Engineering; Recombinant Proteins; Spectrophotometry

1992
Cooperative ligand reorientations in cytochrome c3: a molecular dynamics simulation.
    Biochimica et biophysica acta, 1991, May-23, Volume: 1058, Issue:1

    Topics: Amino Acid Sequence; Computer Simulation; Cytochrome c Group; Desulfovibrio; Heme; Histidine; Imidazoles; Ligands; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Protein Conformation

1991
Assignment of the histidine axial ligands to the cytochrome bH and cytochrome bL components of the bc1 complex from Rhodobacter sphaeroides by site-directed mutagenesis.
    Biochemistry, 1991, Jul-09, Volume: 30, Issue:27

    Topics: Amino Acid Sequence; Base Sequence; Blotting, Western; Codon; Cytochrome b Group; Electron Transport Complex III; Heme; Histidine; Kinetics; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Rhodobacter sphaeroides

1991
Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidase.
    Biochemistry, 1991, Oct-01, Volume: 30, Issue:39

    Topics: Alkenes; Base Sequence; Carbon Monoxide; Cytochrome-c Peroxidase; DNA Mutational Analysis; Ferric Compounds; Ferrous Compounds; Glycine; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Leucine; Ligands; Molecular Sequence Data; Oligonucleotides; Protein Conformation; Recombinant Proteins; Saccharomyces cerevisiae; Spectrophotometry, Infrared; Spectrum Analysis, Raman; Structure-Activity Relationship; Water

1991
Proton nuclear magnetic resonance study of the solution distal histidine orientation in monomeric Chironomus thummi thummi cyanomet hemoglobins. Dynamic stability of the heme pocket as monitored by labile proton exchange.
    Journal of molecular biology, 1991, Oct-05, Volume: 221, Issue:3

    Topics: Animals; Chironomidae; Heme; Histidine; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Methemoglobin; Protein Conformation; Protons; Solutions; Temperature; Thermodynamics; Water

1991
Proton nuclear Overhauser effect study of the heme active site structure of chloroperoxidase.
    Biochemistry, 1992, Feb-18, Volume: 31, Issue:6

    Topics: Arginine; Binding Sites; Chloride Peroxidase; Heme; Histidine; Isoenzymes; Magnetic Resonance Spectroscopy; Mitosporic Fungi; Molecular Structure

1992
The aspirin and heme binding sites of PGG/H synthase.
    Advances in prostaglandin, thromboxane, and leukotriene research, 1991, Volume: 21A

    Topics: Amino Acid Sequence; Animals; Aspirin; Binding Sites; Cyclooxygenase Inhibitors; Heme; Histidine; Humans; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Prostaglandin-Endoperoxide Synthases; Sequence Homology, Nucleic Acid; Serine; Sheep; Species Specificity

1991
Essential histidines of prostaglandin endoperoxide synthase. His-309 is involved in heme binding.
    The Journal of biological chemistry, 1991, Apr-05, Volume: 266, Issue:10

    Topics: Base Sequence; Binding Sites; Blotting, Western; Catalysis; Cell Line; Heme; Histidine; Microsomes; Molecular Sequence Data; Mutagenesis, Site-Directed; Peroxidases; Prostaglandin-Endoperoxide Synthases; Transfection

1991
Site directed mutagenesis of the heme axial ligands of cytochrome b559 affects the stability of the photosystem II complex.
    The EMBO journal, 1991, Volume: 10, Issue:7

    Topics: Amino Acid Sequence; Base Sequence; Cell Membrane; Chloroplasts; Cyanobacteria; Cytochrome b Group; Enzyme Activation; Enzyme Stability; Heme; Histidine; Ligands; Molecular Sequence Data; Multigene Family; Mutagenesis, Site-Directed; Photosynthetic Reaction Center Complex Proteins; Photosystem II Protein Complex; Protein Binding; RNA, Messenger; Transcription, Genetic

1991
Effect of linking allyl and aromatic chains to histidine 170 in horseradish peroxidase.
    Biochimica et biophysica acta, 1991, Aug-30, Volume: 1079, Issue:2

    Topics: Acetophenones; Allyl Compounds; Binding Sites; Diethyl Pyrocarbonate; Heme; Histidine; Horseradish Peroxidase; Kinetics; Peptides; Trypsin

1991
Proton NMR investigation of the reconstitution of equine myoglobin with hemin dicyanide. Evidence for late formation of the proximal His93F8-iron bond.
    FEBS letters, 1991, Sep-23, Volume: 290, Issue:1-2

    Topics: Animals; Apoproteins; Cyanides; Heme; Hemin; Histidine; Horses; In Vitro Techniques; Iron; Kinetics; Magnetic Resonance Spectroscopy; Metmyoglobin; Myoglobin; Swine

1991
Spectroscopic studies of myoglobin at low pH: heme ligation kinetics.
    Biochemistry, 1991, Feb-05, Volume: 30, Issue:5

    Topics: Animals; Heme; Histidine; Hydrogen-Ion Concentration; In Vitro Techniques; Iron; Kinetics; Metmyoglobin; Myoglobin; Photolysis; Spectrum Analysis, Raman; Whales

1991
Characterization by NMR of the heme-myoglobin adduct formed during the reductive metabolism of BrCCl3. Covalent bonding of the proximal histidine to the ring I vinyl group.
    The Journal of biological chemistry, 1991, Feb-15, Volume: 266, Issue:5

    Topics: Heme; Histidine; Hydrocarbons, Brominated; Magnetic Resonance Spectroscopy; Models, Molecular; Myoglobin; Oxidation-Reduction; Spectrophotometry, Ultraviolet; Trihalomethanes

1991
1H NMR study of the solution molecular and electronic structure of Escherichia coli ferricytochrome b562: evidence for S = 1/2 in equilibrium S = 5/2 spin equilibrium for intact His/Met ligation.
    Biochemistry, 1991, Feb-26, Volume: 30, Issue:8

    Topics: Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrogen; Kinetics; Magnetic Resonance Spectroscopy; Methionine; Thermodynamics; X-Ray Diffraction

1991
Role of His residues in Bacillus subtilis cytochrome b558 for haem binding and assembly of succinate: quinone oxidoreductase (complex II).
    Molecular microbiology, 1990, Volume: 4, Issue:6

    Topics: Amino Acid Sequence; Bacillus subtilis; Base Sequence; Codon; Cytochrome b Group; DNA; Electron Transport Complex II; Heme; Histidine; Molecular Sequence Data; Multienzyme Complexes; Mutation; NADPH Oxidases; Oxidoreductases; Protein Conformation; Succinate Dehydrogenase

1990
Cytochrome c'' isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands.
    The Biochemical journal, 1990, Sep-01, Volume: 270, Issue:2

    Topics: Bacteria; Circular Dichroism; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Ferric Compounds; Heme; Histidine; Oxidation-Reduction; Protein Conformation; Protons

1990
Multiple heme pocket subconformations of methemoglobin associated with distal histidine interactions.
    Biochemistry, 1990, Oct-09, Volume: 29, Issue:40

    Topics: Animals; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Humans; Methemoglobin; Protein Conformation; Temperature; Thermodynamics

1990
Low temperature EPR and MCD studies on cytochrome b-558 of the Bacillus subtilis succinate: quinone oxidoreductase indicate bis-histidine coordination of the heme iron.
    Biochimica et biophysica acta, 1990, Nov-15, Volume: 1041, Issue:2

    Topics: Bacillus subtilis; Cell Membrane; Circular Dichroism; Cloning, Molecular; Cytochrome b Group; Electron Spin Resonance Spectroscopy; Electron Transport Complex II; Escherichia coli; Freezing; Heme; Histidine; Iron; Multienzyme Complexes; NADPH Oxidases; Oxidation-Reduction; Oxidoreductases; Protein Conformation; Succinate Dehydrogenase

1990
Molecular structure of flavocytochrome b2 at 2.4 A resolution.
    Journal of molecular biology, 1990, Apr-20, Volume: 212, Issue:4

    Topics: Amino Acid Sequence; Chemical Phenomena; Chemistry, Physical; Computer Graphics; Electron Transport; Flavins; Flavodoxin; Heme; Histidine; Iron; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Molecular Sequence Data; Molecular Structure; Protein Conformation; Substrate Specificity; Sulfhydryl Compounds; X-Ray Diffraction

1990
Rearrangement of the distal pocket accompanying E7 His----Gln substitution in elephant carbonmonoxy- and oxymyoglobin: 1H NMR identification of a new aromatic residue in the heme pocket.
    Biochemistry, 1990, Mar-13, Volume: 29, Issue:10

    Topics: Animals; Binding Sites; Elephants; Glutamine; Heme; Histidine; Kinetics; Magnetic Resonance Spectroscopy; Myoglobin; Phenylalanine; Protein Conformation; Structure-Activity Relationship

1990
Heme methyl hyperfine shift pattern as a probe for determining the orientation of the functionally relevant proximal histidyl imidazole with respect to the heme in hemoproteins.
    FEBS letters, 1990, May-07, Volume: 264, Issue:1

    Topics: Animals; Carbon Isotopes; Heme; Hemeproteins; Histidine; Hydrogen; Imidazoles; Magnetic Resonance Spectroscopy; Metmyoglobin; Muscles; Myoglobin; Protein Conformation; Sharks

1990
Porphyrin-induced photodynamic cross-linking of hepatic heme-binding proteins.
    Life sciences, 1986, Jan-27, Volume: 38, Issue:4

    Topics: Animals; Carrier Proteins; Coproporphyrins; Cytochrome P-450 Enzyme System; Epitopes; Glutathione Transferase; Heme; Heme-Binding Proteins; Hemeproteins; Hemopexin; Histidine; Immunoelectrophoresis; Light; Liver; Photochemistry; Porphyrins; Protoporphyrins; Rats; Temperature; Time Factors; Ultraviolet Rays; Uroporphyrins

1986
Effects of porphyrins on proteins of cytosol and plasma. In vitro photo-oxidation and cross-linking of proteins by naturally occurring and synthetic porphyrins.
    The Journal of laboratory and clinical medicine, 1987, Volume: 110, Issue:4

    Topics: Animals; Blood Proteins; Carrier Proteins; Cytosol; Epitopes; Glutathione Transferase; Heme; Heme-Binding Proteins; Hemeproteins; Histidine; Macromolecular Substances; Oxidation-Reduction; Photochemistry; Porphyrins; Proteins; Rats

1987
Redox properties of the diheme cytochrome c4 from Azotobacter vinelandii and characterisation of the two hemes by NMR, MCD and EPR spectroscopy.
    Biochimica et biophysica acta, 1989, Jan-19, Volume: 994, Issue:1

    Topics: Azotobacter; Cytochrome c Group; Diethyl Pyrocarbonate; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Methionine; Oxidation-Reduction; Spectrophotometry; Spectrum Analysis

1989
Proton magnetic resonance study of the influence of chemical modification, mutation, quaternary state, and ligation state on dynamic stability of the heme pocket in hemoglobin as reflected in the exchange of the proximal histidyl ring labile proton.
    Biochemistry, 1989, Mar-07, Volume: 28, Issue:5

    Topics: Allosteric Site; Catalysis; Deuterium; Energy Transfer; Heme; Hemoglobin A; Histidine; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Mutation; Oxidation-Reduction; Protons

1989
Conformational transition of aquomethemoglobin: intramolecular histidine E7 binding reaction to the heme iron in the temperature range between 220 K and 295 K as seen by EPR and temperature-jump measurements.
    Biochimica et biophysica acta, 1989, Jun-13, Volume: 996, Issue:1-2

    Topics: Animals; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Humans; Hydrogen-Ion Concentration; In Vitro Techniques; Methemoglobin; Motion; Protein Conformation; Temperature; Thermodynamics; Water

1989
Binding of thiocyanate to lactoperoxidase: 1H and 15N nuclear magnetic resonance studies.
    Biochemistry, 1989, May-30, Volume: 28, Issue:11

    Topics: Animals; Binding Sites; Cyanides; Energy Transfer; Heme; Histidine; Hydrogen-Ion Concentration; Iodine; Lactoperoxidase; Magnetic Resonance Spectroscopy; Mathematics; Nitrates; Peroxidases; Protons; Thiocyanates

1989
Axial ligand replacement in horse heart cytochrome c by semisynthesis.
    Proteins, 1989, Volume: 6, Issue:3

    Topics: Animals; Chemical Phenomena; Chemistry; Cytochrome c Group; Heme; Histidine; Horses; Methionine; Myocardium; Protein Conformation; Spectrophotometry, Ultraviolet

1989
Effect of the distal histidine modification (Cyanation) of myoglobin on the ligand binding kinetics and the heme environmental structures.
    Biochemistry, 1989, Sep-19, Volume: 28, Issue:19

    Topics: Animals; Carbon Monoxide; Cyanogen Bromide; Heme; Histidine; Ligands; Male; Myoglobin; Spermatozoa; Thermodynamics; Whales

1989
Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis.
    The Journal of biological chemistry, 1989, May-15, Volume: 264, Issue:14

    Topics: Amino Acid Sequence; Binding Sites; Blotting, Western; Cloning, Molecular; Codon; Cytochrome b Group; Cytochromes; DNA, Bacterial; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Molecular Sequence Data; Mutation; Oxidation-Reduction; Oxidoreductases; Oxygen; Protein Conformation; Structure-Activity Relationship; Ubiquinone; Water

1989
Resonance raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement.
    Biochemistry, 1989, May-30, Volume: 28, Issue:11

    Topics: Animals; Heme; Histidine; Hydrogen-Ion Concentration; Mathematics; Mutation; Myoglobin; Protein Conformation; Spectrum Analysis, Raman; Temperature; Whales

1989
Chemical modification of cytochrome b5, cytochrome c and myoglobin with diethylpyrocarbonate.
    Biochimica et biophysica acta, 1988, May-18, Volume: 954, Issue:2

    Topics: Animals; Cytochrome b Group; Cytochrome c Group; Cytochrome P-450 Enzyme System; Cytochromes b5; Diethyl Pyrocarbonate; Formates; Heme; Histidine; Kinetics; Male; Microsomes, Liver; Myoglobin; NADPH-Ferrihemoprotein Reductase; Rabbits

1988
Cytochrome c peroxidase mutant active site structures probed by resonance Raman and infrared signatures of the CO adducts.
    Biochemistry, 1988, Jul-26, Volume: 27, Issue:15

    Topics: Arginine; Binding Sites; Carbon Monoxide; Cytochrome-c Peroxidase; DNA Mutational Analysis; Heme; Histidine; Hydrogen Bonding; Peroxidases; Protein Conformation; Recombinant Proteins; Saccharomyces cerevisiae; Spectrophotometry, Infrared; Spectrum Analysis, Raman

1988
Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon-13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes.
    Biochemical and biophysical research communications, 1985, Sep-16, Volume: 131, Issue:2

    Topics: Carbon Monoxide; Chloride Peroxidase; Cysteine; Cytochrome-c Peroxidase; Heme; Hemeproteins; Histidine; Horseradish Peroxidase; Imidazoles; Isoenzymes; Lactoperoxidase; Magnetic Resonance Spectroscopy; Myoglobin; Peroxidases

1985
Resonance Raman study on cytochrome c peroxidase and its intermediate. Presence of the Fe(IV) = O bond in compound ES and heme-linked ionization.
    The Journal of biological chemistry, 1986, Aug-25, Volume: 261, Issue:24

    Topics: Computers; Cytochrome-c Peroxidase; Heme; Histidine; Hydrogen-Ion Concentration; Peroxidases; Saccharomyces cerevisiae; Spectrum Analysis, Raman

1986
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c.
    Biophysical journal, 1987, Volume: 52, Issue:1

    Topics: Animals; Cytochrome c Group; Deuterium; Deuterium Oxide; Heme; Histidine; Horses; Magnetic Resonance Spectroscopy; Methionine; Protein Conformation; Species Specificity; Tuna; Water

1987
A nuclear Overhauser effect study of the heme crevice in the resting state and compound I of horseradish peroxidase: evidence for cation radical delocalization to the proximal histidine.
    Biochemistry, 1988, Jul-26, Volume: 27, Issue:15

    Topics: Cations; Heme; Hemeproteins; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Iron; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Peroxidases

1988
The mechanism of peroxidase-mediated cytotoxicity. II. Role of the heme moiety.
    Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.), 1988, Volume: 187, Issue:1

    Topics: Animals; Binding Sites; Erythrocytes; Heme; Hemolysis; Histidine; Hot Temperature; Hydrogen Peroxide; Iodides; Iron; Peroxidases; Porphyrins; Protein Denaturation; Rabbits

1988
Proton NMR studies of human hemoglobin variants modified in the proximal side of beta heme pocket. Implications for the affinity control and cooperative mechanism.
    The Journal of biological chemistry, 1988, Mar-05, Volume: 263, Issue:7

    Topics: Amino Acids; Binding Sites; Heme; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen Bonding; Hydrogen-Ion Concentration; Iron; Magnetic Resonance Spectroscopy; Oxygen; Protein Conformation; Structure-Activity Relationship

1988
Assignment of hyperfine shifted haem methyl carbon resonances in paramagnetic low-spin met-cyano complex of sperm whale myoglobin.
    FEBS letters, 1987, Sep-28, Volume: 222, Issue:1

    Topics: Animals; Heme; Hemeproteins; Histidine; Magnetic Resonance Spectroscopy; Metmyoglobin; Protein Conformation; Whales

1987
Glutathione as a scavenger of free hemin. A mechanism of preventing red cell membrane damage.
    Biochemical pharmacology, 1987, Nov-15, Volume: 36, Issue:22

    Topics: Cyanides; Cytoskeletal Proteins; Erythrocyte Membrane; Glutathione; Heme; Hemin; Hemolysis; Histidine; Humans; Membrane Proteins

1987
Cryogenic stabilization of myoglobin photoproducts.
    The Journal of biological chemistry, 1986, Oct-15, Volume: 261, Issue:29

    Topics: Animals; Drug Stability; Freezing; Heme; Hemoglobins; Histidine; Kinetics; Myoglobin; Photolysis; Protein Conformation; Spectrum Analysis, Raman; Whales

1986
XANES of carboxy and cyanomet-myoglobin. The role of the distal histidine in the bent Fe-C-O configuration.
    European biophysics journal : EBJ, 1986, Volume: 14, Issue:1

    Topics: Biophysical Phenomena; Biophysics; Heme; Hemeproteins; Histidine; Metmyoglobin; Myoglobin; Protein Conformation; Spectrum Analysis; X-Rays

1986
Heme-linked ionizations in horseradish peroxidase detected by Raman difference spectroscopy.
    The Journal of biological chemistry, 1986, Feb-05, Volume: 261, Issue:4

    Topics: Heme; Histidine; Horseradish Peroxidase; Hydrogen-Ion Concentration; Iron; Isoenzymes; Oxidation-Reduction; Peroxidases; Protein Conformation; Spectrum Analysis, Raman

1986
The histidine-rich glycoprotein of serum has a domain rich in histidine, proline, and glycine that binds heme and metals.
    Biochemistry, 1985, Mar-12, Volume: 24, Issue:6

    Topics: Animals; Binding Sites; Circular Dichroism; Glycine; Heme; Histidine; Hydrogen-Ion Concentration; Metals; Molecular Weight; Proline; Proteins; Rabbits

1985
Haem-apoprotein interactions detected by resonance Raman scattering in Mb- and Hb-derivates lacking the saltbridge His146 beta-Asp94 beta.
    European biophysics journal : EBJ, 1985, Volume: 12, Issue:1

    Topics: Animals; Apoproteins; Aspartic Acid; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Myoglobin; Spectrum Analysis, Raman; Structure-Activity Relationship; Whales

1985
Proton nuclear Overhauser effect investigation of the heme pockets in ligated hemoglobin: conformational differences between oxy and carbonmonoxy forms.
    Biochemistry, 1985, Jul-02, Volume: 24, Issue:14

    Topics: Carboxyhemoglobin; Heme; Hemoglobin A; Hemoglobins; Histidine; Humans; Ligands; Macromolecular Substances; Magnetic Resonance Spectroscopy; Oxyhemoglobins; Protein Binding; Protein Conformation; Valine

1985
Low-temperature formation of a distal histidine complex in hemoglobin: a probe for heme pocket flexibility.
    Biochemistry, 1985, Oct-22, Volume: 24, Issue:22

    Topics: Animals; Binding Sites; Freezing; Heme; Hemoglobins; Histidine; Horses; Methemoglobin; Protein Binding; Spectrum Analysis

1985
[Alkylation of histidine radicals of the site of combination of beta-1-seromucoid with hematin].
    Comptes rendus hebdomadaires des seances de l'Academie des sciences. Serie D: Sciences naturelles, 1967, Aug-16, Volume: 265, Issue:7

    Topics: Alkylation; Beta-Globulins; Binding Sites; Heme; Histidine; Humans; Mucoproteins; Protein Binding; Serum Globulins

1967
Electron paramagnetic resonance of nitric oxide cytochrome C.
    Biochemical and biophysical research communications, 1969, May-08, Volume: 35, Issue:3

    Topics: Animals; Chemical Phenomena; Chemistry; Cytochromes; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Methionine; Myocardium; Nitric Oxide; Powders; Radioisotopes

1969
Visible absorption and electron spin resonance spectra of the isolated chains of human hemoglobin. Discussion of chain-mediated heme-heme interaction.
    Biochemistry, 1969, Volume: 8, Issue:7

    Topics: Benzoates; Chemical Phenomena; Chemistry; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Iron; Mercury; Myoglobin; Peptides; Spectrophotometry; Temperature

1969
Purification and properties of cytochromes c of Azotobacter vinelandii.
    Biochimica et biophysica acta, 1969, Aug-05, Volume: 180, Issue:3

    Topics: Amino Acids; Animals; Azotobacter; Cattle; Cell-Free System; Cellulose; Chemical Phenomena; Chemical Precipitation; Chemistry; Chromatography, Gel; Chromatography, Ion Exchange; Cytochromes; Dextrans; Dialysis; Electron Transport; Electron Transport Complex IV; Electrophoresis; Electrophoresis, Disc; Heme; Histidine; Hydrogen-Ion Concentration; Methods; Molecular Weight; Myocardium; Nitrogen Fixation; Species Specificity

1969
An analysis of the electron spin resonance of low spin ferric heme compounds.
    Biophysical journal, 1970, Volume: 10, Issue:2

    Topics: Chemical Phenomena; Chemistry; Cytochromes; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Histidine; Iron; Pyridines

1970
Interaction of hemoglobin with ions. Allosteric effects of the binding of anions.
    Biochimica et biophysica acta, 1971, Apr-27, Volume: 236, Issue:1

    Topics: Adenosine Triphosphate; Adult; Chemical Phenomena; Chemistry; Cobalt; Cyanides; Electron Spin Resonance Spectroscopy; Ferrocyanides; Glycerophosphates; Heme; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Inositol; Ions; Iron; Osmolar Concentration; Oxygen; Phosphates; Polymers; Protein Binding; Ultracentrifugation

1971
Electron paramagnetic resonance studies on the reaction of exogenous ligands with cytochrome c 3 from Desulfovibrio vulgaris.
    Biochimica et biophysica acta, 1971, Jul-25, Volume: 243, Issue:1

    Topics: Ammonia; Azides; Chemical Phenomena; Chemistry; Chlorides; Cyanides; Cytochromes; Desulfovibrio; Electron Spin Resonance Spectroscopy; Fluorides; Helium; Heme; Histidine; Hydroxylamines; Imidazoles; Nitric Oxide; Nitrites; Oxidation-Reduction; Oxygen; Potassium; Protein Binding; Protein Conformation; Sodium; Sulfites; Temperature; Tromethamine

1971
Carbon monoxide bonding in hemeproteins.
    Annals of the New York Academy of Sciences, 1970, Oct-05, Volume: 174, Issue:1

    Topics: Binding Sites; Carbon Monoxide; Cytochromes; Electron Transport Complex IV; Heme; Hemoglobins; Histidine; Infrared Rays; Iron; Ketones; Myoglobin; Oxygen; Protein Binding; Proteins; Spectrum Analysis

1970
Antigen-free medium for cultivation of Haemophilus influenzae, AFH-medium.
    Acta pathologica et microbiologica Scandinavica. Section B: Microbiology and immunology, 1972, Volume: 80, Issue:2

    Topics: Antigens; Antigens, Bacterial; Chromatography, Gel; Culture Media; Densitometry; Glucose; Haemophilus influenzae; Heme; Histidine; Hydrogen-Ion Concentration; Molecular Weight; NAD; Phosphates; Potassium; Sodium Chloride; Spectrophotometry

1972
The conformation of horse heart apocytochrome c.
    The Journal of biological chemistry, 1972, Dec-25, Volume: 247, Issue:24

    Topics: Acetone; Alkylation; Amino Acids; Animals; Apoproteins; Circular Dichroism; Cytochrome c Group; Ferricyanides; Glycols; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Mercaptoethanol; Myocardium; Oxidation-Reduction; Peptides; Protein Binding; Protein Conformation; Silver; Spectrophotometry, Ultraviolet; Sulfates; Tyrosine; Ultracentrifugation; Viscosity

1972
Photo-oxidative modification of the heme ligands in horse heart ferricytochrome c: conformational and functional studies.
    Biochimica et biophysica acta, 1972, Dec-28, Volume: 285, Issue:2

    Topics: Amino Acids; Animals; Circular Dichroism; Cytochrome c Group; Electron Transport; Heme; Histidine; Horses; Kinetics; Membranes; Methionine; Mitochondria, Liver; Myocardium; Oxidation-Reduction; Oxygen Consumption; Photochemistry; Protein Binding; Protein Conformation; Rats; Spectrophotometry; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Sulfoxides

1972
The physical chemistry of hemes and hemopeptides. I. Physiochemical properties and reduction of chlorodeuterohemin in organic solvent.
    Biochimica et biophysica acta, 1973, May-28, Volume: 304, Issue:3

    Topics: Carbon Monoxide; Chlorine; Deuterium; Electron Spin Resonance Spectroscopy; Esters; Heme; Histidine; Imidazoles; Ligands; Magnetic Resonance Spectroscopy; Mathematics; Methanol; Organometallic Compounds; Oxidation-Reduction; Pyridines; Solvents; Spectrophotometry; Spectrophotometry, Infrared; Sulfites

1973
Amino acid sequence of cytochrome c3 from Desulfovibrio vulgaris.
    The Journal of biological chemistry, 1974, Jan-25, Volume: 249, Issue:2

    Topics: Amino Acid Sequence; Amino Acids; Apoproteins; Binding Sites; Chemical Phenomena; Chemistry; Chromatography, Gel; Chromatography, Paper; Chymotrypsin; Cysteine; Cytochrome c Group; Desulfovibrio; Heme; Histidine; Peptide Fragments; Peptides; Thiocyanates; Trypsin

1974
Spectroscopic studies on the conformation of cytochrome c and apocytochrome c.
    The Journal of biological chemistry, 1974, Feb-25, Volume: 249, Issue:4

    Topics: Animals; Apoproteins; Chemical Phenomena; Chemistry; Computers; Cytochrome c Group; Deuterium; Fluorescence; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Myocardium; Osmolar Concentration; Protein Conformation; Protein Denaturation; Protons; Sodium Chloride; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan; Viscosity

1974
The structure of the heme crevice of ferric cytochrome c alkylated at methionine-80.
    The Journal of biological chemistry, 1974, Apr-25, Volume: 249, Issue:8

    Topics: Alkylation; Chemical Phenomena; Chemistry; Cytochrome c Group; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Ligands; Mathematics; Methionine; Protein Binding; Protein Conformation; Spectrophotometry, Ultraviolet

1974
Proton magnetic resonance studies of Desulfovibrio cytochromes c3.
    Biochemistry, 1974, Apr-23, Volume: 13, Issue:9

    Topics: Chemical Phenomena; Chemistry; Cytochrome c Group; Desulfovibrio; Deuterium; Heme; Histidine; Iron; Magnetic Resonance Spectroscopy; Magnetics; Oxidation-Reduction; Protons; Species Specificity; Temperature

1974
The physical chemistry of hemes and hemopeptides. 3. Synthesis and physicochemical properties of cytochrome c-related heme--pentapeptide soluble in organic solvents.
    Biochimica et biophysica acta, 1974, May-24, Volume: 343, Issue:3

    Topics: Binding Sites; Chromatography, Ion Exchange; Cysteine; Cytochrome c Group; Drug Stability; Electron Spin Resonance Spectroscopy; Glycine; Heme; Hemeproteins; Histidine; Iron; Ligands; Oligopeptides; Optical Rotation; Oxidation-Reduction; Protein Binding; Protein Conformation; Solubility; Spectrophotometry; Spectrophotometry, Ultraviolet

1974
Haem ligands of the ferricytochrome c of Ustilago sphaerogena.
    The Biochemical journal, 1974, Volume: 139, Issue:3

    Topics: Acetates; Alkylation; Amino Acid Sequence; Basidiomycota; Bromine; Carboxylic Acids; Cytochrome c Group; Cytochrome Reductases; Electron Transport Complex IV; Heme; Histidine; Imidazoles; Iron; Kinetics; Ligands; Methionine; Methylation; Molecular Conformation; Spectrophotometry

1974
Electrostatic effects in myoglobin. pH and ionic strength variations of ionization equilibria for individual groups in sperm whale ferrimyoglobin.
    Biochemistry, 1974, Jul-02, Volume: 13, Issue:14

    Topics: Amino Acid Sequence; Animals; Cetacea; Chemical Phenomena; Chemistry; Evaluation Studies as Topic; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Mathematics; Models, Chemical; Myoglobin; Osmolar Concentration; Protein Conformation; Protein Denaturation; Valine; Water

1974
Stereochemistry of cooperative effects in hemoglobin.
    Cold Spring Harbor symposia on quantitative biology, 1972, Volume: 36

    Topics: Animals; Arginine; Chemical Phenomena; Chemistry; Crystallization; Diphosphoglyceric Acids; Heme; Hemoglobins; Hemoglobins, Abnormal; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Macromolecular Substances; Methemoglobin; Models, Structural; Oxygen; Protein Binding; Protein Conformation; Valine; X-Ray Diffraction

1972
Translational control of globin synthesis by haemin in Xenopus oocytes.
    Nature: New biology, 1973, Nov-28, Volume: 246, Issue:152

    Topics: Animals; Carbon Radioisotopes; Female; Globins; Heme; Histidine; Iodine Radioisotopes; Lead; Leucine; Ovum; Polyribosomes; Protein Biosynthesis; Reticulocytes; Ribonucleases; RNA, Messenger; Tritium; Xenopus

1973
The nature of the inhibition of -aminolevulinic acid synthetase by hemin.
    Archives of biochemistry and biophysics, 1972, Volume: 148, Issue:1

    Topics: 5-Aminolevulinate Synthetase; Acyltransferases; Azides; Chelating Agents; Cyanides; Feedback; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Rhodobacter sphaeroides; Rhodopseudomonas; Serum Albumin, Bovine; Spectrophotometry

1972
Iron ligands in different forms of ferricytochrome c: the 620-nm band as a probe.
    Archives of biochemistry and biophysics, 1972, Volume: 150, Issue:2

    Topics: 1-Propanol; Animals; Chromatography, Gel; Cytochromes; Ethanol; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Mathematics; Methionine; Myocardium; Osmolar Concentration; Pepsin A; Peptides; Protein Binding; Protein Conformation; Protein Denaturation; Spectrophotometry; Temperature; Thermodynamics; Trypsin; Urea; Water

1972
Immunochemistry of sperm whale myoglobin. XI. Modification of two glutamic acid residues and their role in the antigenic reactivity.
    Immunochemistry, 1972, Volume: 9, Issue:11

    Topics: Amino Acids; Animals; Antigen-Antibody Reactions; Antigens; Apoproteins; Binding Sites, Antibody; Carbodiimides; Cetacea; Electrophoresis, Polyacrylamide Gel; Electrophoresis, Starch Gel; Esters; Glutamates; Glycine; Goats; Heme; Histidine; Immunodiffusion; Myoglobin; Precipitin Tests; Protein Conformation; Rabbits

1972
Effects of anions and ligands on the tertiary structure around ligand binding site in human adult hemoglobin.
    Biochemistry, 1973, Jan-02, Volume: 12, Issue:1

    Topics: Adult; Binding Sites; Carbon Monoxide; Deuterium; Diphosphoglyceric Acids; Heme; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Inositol; Magnetic Resonance Spectroscopy; Oxygen; Phosphates; Potassium Chloride; Protein Binding; Protein Conformation; Sulfates; Tromethamine; Valine

1973
Evidence for the coordination of a histidyl residue to heme. I. Far ultraviolet spectral studies of model complexes.
    Biochimica et biophysica acta, 1973, Jan-25, Volume: 295, Issue:1

    Topics: Animals; Buffers; Catalase; Chemical Phenomena; Chemistry; Cyanides; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Imidazoles; Iron; Lysine; Methemoglobin; Models, Chemical; Myoglobin; Peptides; Peroxidases; Spectrophotometry, Ultraviolet

1973
Functional properties of carboxypeptidase-digested hemoglobins.
    Journal of molecular biology, 1974, Feb-05, Volume: 82, Issue:4

    Topics: Amino Acid Sequence; Carboxyhemoglobin; Carboxypeptidases; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Ligands; Oxyhemoglobins; Phosphates; Photolysis; Protein Binding; Protein Conformation; Time Factors; Tyrosine

1974
Three-dimensional structure of hemoglobin from the polychaete annelid, Glycera dibranchiata, at 2.5 A resolution.
    The Journal of biological chemistry, 1974, Jul-10, Volume: 249, Issue:13

    Topics: Amino Acids; Animals; Annelida; Computers; Crystallization; Crystallography; Electrons; Fourier Analysis; Heme; Hemoglobins; Histidine; Leucine; Models, Structural; Molecular Conformation; Protein Conformation; X-Ray Diffraction

1974
The functional properties of hemoglobin Bethesda ( 2 2 145His ).
    The Journal of biological chemistry, 1972, Jun-10, Volume: 247, Issue:11

    Topics: Amino Acids; Binding Sites; Buffers; Carbon Monoxide; Chemical Phenomena; Chemistry; Heme; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen-Ion Concentration; Inositol; Kinetics; Macromolecular Substances; Mutation; Nitriles; Osmolar Concentration; Oxygen; Peptides; Protein Binding; Protein Conformation; Spectrophotometry; Tyrosine; Ultracentrifugation

1972
Interaction of rose bengal with apo-hemoproteins. An essential histidine residue in cytochrome c peroxidase.
    European journal of biochemistry, 1972, Mar-15, Volume: 26, Issue:1

    Topics: Apoproteins; Binding Sites; Cytochromes; Heme; Hemoglobins; Histidine; Hydrogen Peroxide; Kinetics; Myoglobin; Peroxidases; Photochemistry; Rose Bengal; Spectrophotometry; Tryptophan

1972
Hemin control of globin synthesis: action of an inhibitor formed in the absence of hemin on the reticulocyte cell-free system and its reversal by a ribosomal factor.
    Biochimica et biophysica acta, 1972, Jul-31, Volume: 272, Issue:4

    Topics: Animals; Blood Proteins; Carbon Isotopes; Cell-Free System; Centrifugation, Density Gradient; Chemical Precipitation; Chromatography, DEAE-Cellulose; Chromatography, Ion Exchange; Globins; Heme; Histidine; Hydrogen-Ion Concentration; Isoleucine; Kinetics; Leucine; Potassium Chloride; Rabbits; Reticulocytes; Ribosomes; Trypsin

1972
The structure of hemopeptide 1-65 from cytochrome c.
    Archives of biochemistry and biophysics, 1972, Volume: 148, Issue:1

    Topics: Acetates; Alkylation; Amino Acids; Animals; Bromine; Chemical Phenomena; Chemistry, Physical; Chromatography, Gel; Circular Dichroism; Cyanogen Bromide; Cytochromes; Heme; Histidine; Horses; Myocardium; Peptides; Potassium Iodide; Protein Binding; Protein Conformation; Spectrophotometry; Ultracentrifugation; Ultraviolet Rays; Viscosity

1972
Reaction of 3-amino-1:2:4-triazole with bovine liver catalase and human erythrocyte catalase.
    Archives of biochemistry and biophysics, 1972, Volume: 148, Issue:2

    Topics: Adenosine Monophosphate; Amines; Amino Acids; Animals; Catalase; Cattle; Chemical Phenomena; Chemistry; Erythrocytes; Heme; Histidine; Humans; Hydrogen Peroxide; Liver; Methods; Protein Binding; Rats; Rats, Inbred Strains; Time Factors; Triazoles

1972
High resolution nuclear magnetic resonance spectra of hemoglobin. I. The cyanide complexes of and chains.
    Journal of molecular biology, 1972, Sep-28, Volume: 70, Issue:2

    Topics: Amides; Amino Acids; Chloromercuribenzoates; Chromatography, Gel; Cyanides; Deuterium; Heme; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Peptides; Protons; Temperature

1972
High resolution nuclear resonance spectra of hemoglobin. II. Ligated tetramers.
    Journal of molecular biology, 1972, Sep-28, Volume: 70, Issue:2

    Topics: Buffers; Cyanides; Deuterium; Glycerophosphates; Heme; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Imines; Magnetic Resonance Spectroscopy; Oxygen; Phosphates; Piperazines; Protons; Sulfonic Acids; Tromethamine

1972
Probing the topography of proteins in solution by photosensitized oxidation. The heme environment in horse heart ferrocytochrome c.
    Biochimica et biophysica acta, 1971, Feb-16, Volume: 229, Issue:2

    Topics: Amino Acids; Animals; Chromatography, Gel; Cyanides; Cytochromes; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Light; Methionine; Myocardium; Oxidation-Reduction; Peptides; Photochemistry; Radiation Effects; Tryptophan; Tyrosine

1971
The hemichromogen form of the isolated subunits of hemoglobin.
    Biochimica et biophysica acta, 1971, Aug-27, Volume: 243, Issue:2

    Topics: Binding Sites; Chemical Phenomena; Chemistry; Chloromercuribenzoates; Chromatography, Gel; Circular Dichroism; Complement Fixation Tests; Cyanides; Drug Stability; Ferricyanides; Fluorides; Globins; Heme; Hemoglobins; Histidine; Hot Temperature; Humans; Hydrogen-Ion Concentration; Imidazoles; Immune Sera; Iron; Macromolecular Substances; Oxidation-Reduction; Precipitin Tests; Protein Conformation; Sodium; Spectrophotometry; Sulfhydryl Compounds; Ultracentrifugation; Ultraviolet Rays

1971
Purification and properties of cytochrome c 3 of Desulfovibrio vulgaris, Miyazaki.
    Biochimica et biophysica acta, 1971, Aug-27, Volume: 243, Issue:2

    Topics: Amino Acids; Carbon Monoxide; Chemical Phenomena; Chemistry; Chromatography, Gel; Chromatography, Ion Exchange; Chromatography, Thin Layer; Cytochromes; Dansyl Compounds; Desulfovibrio; Electron Transport; Heme; Histidine; Hydrogen; Iron; Kinetics; Mathematics; Molecular Weight; Oxidation-Reduction; Oxidoreductases; Potentiometry; Species Specificity; Spectrophotometry; Spectrum Analysis; Sulfites; Ultraviolet Rays

1971
The hydrogen ion equilibria of horseradish peroxidase and apoperoxidase.
    The Biochemical journal, 1971, Volume: 124, Issue:3

    Topics: Amino Acids; Binding Sites; Carbohydrates; Chemical Phenomena; Chemistry, Physical; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Molecular Weight; Peroxidases; Potentiometry; Protons; Spectrum Analysis; Tyrosine

1971
An electron paramagnetic resonance study of nitrosylmyoglobin.
    Journal of the American Chemical Society, 1971, Oct-06, Volume: 93, Issue:20

    Topics: Crystallography; Electrons; Heme; Histidine; Imidazoles; Iron; Magnetic Resonance Spectroscopy; Myoglobin; Nitro Compounds; Nitrogen Isotopes; Protein Binding

1971
Rabbit haemoglobin synthesis in frog cells: the translation of reticulocyte 9 s RNA in frog oocytes.
    Journal of molecular biology, 1971, Oct-14, Volume: 61, Issue:1

    Topics: Animals; Anura; Carbon Isotopes; Chromatography; Chromatography, Gel; Chromatography, Ion Exchange; Electrophoresis, Disc; Female; Genetic Code; Heme; Hemoglobins; Histidine; Methylcellulose; Ovum; Peptides; Rabbits; Reticulocytes; RNA, Messenger; Tritium

1971
Alterations in the heme-carbon monoxide bond strength.
    Annals of the New York Academy of Sciences, 1970, Oct-05, Volume: 174, Issue:1

    Topics: Argon; Binding Sites; Carbon Monoxide; Chemical Phenomena; Chemistry; Crystallins; Cyclopropanes; Heme; Histidine; Krypton; Lasers; Methods; Myoglobin; Nitrogen; Photolysis; Xenon

1970
States of amino acid residues in proteins. XIX. Modification of arginine residues in myoglobin.
    Biochimica et biophysica acta, 1969, Nov-11, Volume: 194, Issue:1

    Topics: Acrylates; Aldehydes; Animals; Arginine; Binding Sites; Chemical Phenomena; Chemistry; Chromatography, Gel; Chromatography, Ion Exchange; Cyanides; Dextrans; Electrophoresis; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iodoacetates; Lysine; Methemoglobin; Methods; Methylcellulose; Myocardium; Myoglobin; Spectrophotometry; Time Factors; Ultracentrifugation; Urea

1969
Comparison of the resistance of human and horse ferrihemoglobin ligand derivatives to acid denaturation.
    Biochimica et biophysica acta, 1969, Dec-23, Volume: 194, Issue:2

    Topics: Animals; Azides; Chemical Phenomena; Chemistry; Cyanates; Cyanides; Drug Stability; Fluorides; Formates; Heme; Hemoglobins; Histidine; Horses; Humans; Hydrogen-Ion Concentration; Iron; Kinetics; Light; Protein Denaturation; Rotation; Species Specificity; Spectrophotometry; Temperature; Thiocyanates; Time Factors; Ultraviolet Rays

1969
Infrared studies of azido, cyano, and other derivatives of metmyoglobin, methemoglobin, and hemins.
    Biochemistry, 1970, Jun-09, Volume: 9, Issue:12

    Topics: Azides; Carbon Monoxide; Cyanates; Cyanides; Deuterium; Heme; Hemoglobins; Histidine; Hydrogen; Hydrogen-Ion Concentration; Infrared Rays; Myoglobin; Potassium; Sodium; Spectrophotometry; Thiocyanates

1970
Heme sulfuric anhydrides. I. Synthesis and reactions of mesoheme sulfuric anhydride.
    Biochemistry, 1970, Mar-31, Volume: 9, Issue:7

    Topics: Amino Acids; Anhydrides; Chemical Phenomena; Chemistry; Chromatography, Thin Layer; Heme; Histidine; Methionine; Models, Structural; Spectrophotometry; Sulfuric Acids

1970
Heme sulfuric anhydrides. II. Properties of heme models prepared from mesoheme sulfuric anhydrides.
    Biochemistry, 1970, Mar-31, Volume: 9, Issue:7

    Topics: Anhydrides; Chemical Phenomena; Chemistry; Cytochromes; Dioxins; Heme; Histidine; Imidazoles; Methionine; Models, Chemical; Oxidation-Reduction; Spectrophotometry; Sulfuric Acids

1970
[Principal mechanism of the resonance effect of ultrahigh frequencies on hemoglobin].
    Doklady Akademii nauk SSSR, 1970, Volume: 193, Issue:2

    Topics: Binding Sites; Heme; Hemoglobins; Histidine; Microwaves; Radiation Effects

1970
The role of hemoglobin heme loss in Heinz body formation: studies with a partially heme-deficient hemoglobin and with genetically unstable hemoglobins.
    The Journal of clinical investigation, 1970, Volume: 49, Issue:11

    Topics: Anemia, Hemolytic, Congenital; Binding Sites; Blood Protein Electrophoresis; Carbon Monoxide; Cyanides; Glutathione; Heinz Bodies; Heme; Hemoglobins, Abnormal; Histidine; Hot Temperature; Humans; Methods; Peptides; Protein Binding; Sulfhydryl Compounds

1970
[The oxygen affinity of Chironomus thummi erythrocruorins].
    European journal of biochemistry, 1970, Volume: 15, Issue:1

    Topics: Animals; Blood Proteins; Cetacea; Chemical Phenomena; Chemistry; Chromatography, DEAE-Cellulose; Diptera; Heme; Histidine; Isoleucine; Myoglobin; Oxygen; Phenylalanine; X-Ray Diffraction

1970
H+ titration studies on human hemoglobin.
    Biochimica et biophysica acta, 1970, Nov-17, Volume: 221, Issue:2

    Topics: Arginine; Benzoates; Chemical Phenomena; Chemistry; Globins; Heme; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Iodoacetates; Lysine; Mathematics; Mercury; Organometallic Compounds; Oxygen; Sulfhydryl Compounds

1970
Myoglobin, with particular reference to the myoglobin of Aplysia.
    The Biochemical journal, 1970, Volume: 119, Issue:5

    Topics: Animals; Cetacea; Chemical Phenomena; Chemistry; Heme; Histidine; Mollusca; Myoglobin; Peptides

1970
Kinetics of the reaction of hybrid-heme hemoglobins with carbon monoxide.
    The Journal of biological chemistry, 1970, Aug-25, Volume: 245, Issue:16

    Topics: Binding Sites; Carbon Monoxide; Chemical Phenomena; Chemistry; Deuterium; Heme; Hemoglobins; Histidine; Iron; Methemoglobin

1970
The terminal groups of chlorocruorin.
    Biochimica et biophysica acta, 1971, Mar-23, Volume: 229, Issue:3

    Topics: Alanine; Amino Acid Sequence; Animals; Annelida; Arginine; Carboxypeptidases; Glutamates; Heme; Hemolymph; Histidine; Microscopy, Electron; Molecular Weight; Nitrobenzenes; Peptides; Proteins; Tyrosine

1971
Purification and characterization of cytochrome 553 from the chrysophycean alga Monochrysis lutheri.
    Canadian journal of biochemistry, 1971, Volume: 49, Issue:6

    Topics: Amino Acids; Arginine; Autoanalysis; Chemical Precipitation; Chromatography, Gel; Chromatography, Ion Exchange; Cysteine; Cytochromes; Dialysis; Electron Transport; Electrophoresis, Disc; Eukaryota; Freeze Drying; Heme; Histidine; Iron; Isoelectric Focusing; Methionine; Methods; Molecular Weight; Oxidation-Reduction; Photosynthesis; Proline; Quaternary Ammonium Compounds; Spectrophotometry; Sulfates; Tryptophan; Ultracentrifugation; Ultraviolet Rays

1971
[Variants of the haeme complex: the amino acid residues in positions E7, E11 and F8 of an insect haemoglobin (erythrocruorin)].
    Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 1971, Volume: 352, Issue:5

    Topics: Amino Acid Sequence; Animals; Heme; Hemoglobins; Histidine; Insecta; Valine

1971
The proton-binding behavior of human hemoglobin and its subunits in their native state.
    The Journal of biological chemistry, 1968, Jan-25, Volume: 243, Issue:2

    Topics: Acids; Amines; Benzoates; Binding Sites; Carbon Monoxide; Heme; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Iron; Lysine; Mercury; Peptides; Protons; Spectrophotometry; Sulfhydryl Compounds; Tyrosine; Water

1968
Hemic acid dissociation in whale, seal, and porpoise myoglobins and their alkylated derivatives.
    The Journal of biological chemistry, 1968, Feb-25, Volume: 243, Issue:4

    Topics: Alkylation; Animals; Caniformia; Cetacea; Chemical Phenomena; Chemistry; Dolphins; Heme; Histidine; Hydrogen-Ion Concentration; Lysine; Myoglobin; Physiology, Comparative

1968
Type c ferri- and ferrohemochrome formation between hemin c, amino acids, and peptides.
    The Journal of biological chemistry, 1968, Jun-25, Volume: 243, Issue:12

    Topics: Amino Acids; Ammonia; Arginine; Cytochromes; Detergents; Glycine; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Indoles; Iron; Lysine; Methionine; Peptides; Pigments, Biological; Porphyrins; Protein Binding; Spectrophotometry; Sulfur; Tryptophan

1968
Excretion of delta-aminolevulinic acid in the absence of demonstrable erythropoiesis.
    Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.), 1968, Volume: 128, Issue:1

    Topics: Adolescent; Amino Acids; Aminobutyrates; Ammonia; Anemia, Aplastic; Autoanalysis; Chemistry, Clinical; Child; Child, Preschool; Chromatography, Ion Exchange; Erythropoiesis; Heme; Histidine; Humans; Lead Poisoning; Levulinic Acids; Lysine; Middle Aged; Ornithine; Phenylalanine; Tyrosine

1968
The reversible unfolding of horse heart ferricytochrome c.
    Biochemistry, 1968, Volume: 7, Issue:8

    Topics: Alkylation; Animals; Chemical Phenomena; Chemistry; Cytochromes; Dialysis; Glycols; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Methionine; Myocardium; Spectrum Analysis; Tyrosine; Ultracentrifugation; Urea; Viscosity

1968
Oxygen-equilibrium characteristics of abnormal hemoglobin Hiroshima (alpha-2 beta-2 143 Asp).
    Archives of biochemistry and biophysics, 1968, Sep-20, Volume: 127, Issue:1

    Topics: Aspartic Acid; Chemical Phenomena; Chemistry; Electrophoresis; Genetic Variation; Heme; Hemoglobins; Hemoglobins, Abnormal; Hemolysis; Histidine; Humans; Hydrogen-Ion Concentration; Japan; Molecular Biology; Oxygen; Peptides; Spectrophotometry

1968
Spectral studies of iron coordination in hemeprotein complexes: difference spectroscopy below 250 millimicrons.
    Biophysical journal, 1968, Volume: 8, Issue:6

    Topics: Azides; Catalase; Cyanides; Heme; Histidine; Infrared Rays; Iron; Mathematics; Methemoglobin; Myoglobin; Peroxidases; Proteins; Spectrum Analysis; Ultraviolet Rays

1968
Photodynamic action of porphyrins on amino acids and proteins. I. Selective photooxidation of methionine in Aqueous solution.
    Biochemistry, 1969, Volume: 8, Issue:7

    Topics: Amino Acids; Chemical Phenomena; Chemistry; Chlorophyll; Hematoporphyrins; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Light; Magnesium; Methionine; Micrococcus; Muramidase; Oxidation-Reduction; Porphyrins; Radiation Effects; Spectrophotometry; Time Factors; Tryptophan; Tyrosine; Water

1969
The heme binding group of a microsomal hemoprotein 559.
    Biochimica et biophysica acta, 1969, Volume: 188, Issue:2

    Topics: Chemical Phenomena; Chemistry; Color; Diazonium Compounds; Heme; Histidine; Hydrogen-Ion Concentration; Microsomes; Myocardium; Peptides; Proteins; Retina; Spectrophotometry; Tyrosine

1969
States of amino acid residues in proteins. VI. Heme-linked histidine residues in cytochrome c as determined with diazonium-1-H-tetrazole.
    Archives of biochemistry and biophysics, 1965, Volume: 111, Issue:3

    Topics: Amino Acid Sequence; Animals; Chemical Phenomena; Chemistry; Cytochromes; Endopeptidases; Heme; Histidine; Horses; In Vitro Techniques; Indicators and Reagents; Myocardium; Saccharomyces; Tetrazolium Salts; Trypsin

1965
Oxidation-reduction potentials of heme a hemochromes.
    The Journal of biological chemistry, 1966, Jul-25, Volume: 241, Issue:14

    Topics: Chemical Phenomena; Chemistry, Physical; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Oxidation-Reduction; Pyridines; Spectrophotometry

1966
The stereochemistry of peroxidase catalysis.
    The Journal of biological chemistry, 1980, Sep-10, Volume: 255, Issue:17

    Topics: Amino Acid Sequence; Binding Sites; Cytochrome-c Peroxidase; Heme; Histidine; Iron; Kinetics; Models, Biological; Peroxidases; Protein Binding; Protein Conformation

1980
Identification by nucleotide sequence analysis of a goat pseudoglobin gene.
    Nucleic acids research, 1980, Oct-24, Volume: 8, Issue:20

    Topics: Animals; Base Sequence; Codon; DNA Restriction Enzymes; DNA, Recombinant; Genes; Globins; Goats; Heme; Histidine; Mutation; Serum Globulins

1980
Electron paramagnetic resonance studies of NO-heme-nitrogen base. An interpretation of electron paramagnetic resonance spectra of NO-hemoproteins.
    Biochimica et biophysica acta, 1982, Mar-18, Volume: 702, Issue:1

    Topics: Binding Sites; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Histidine; Iron; Nitric Oxide; Protein Binding

1982
Structure and heme environment of ferrocytochrome c553 from 1H NMR studies.
    The Journal of biological chemistry, 1982, Aug-25, Volume: 257, Issue:16

    Topics: Cyanobacteria; Cytochrome c Group; Heme; Histidine; Magnetic Resonance Spectroscopy; Methionine; Phenylalanine; Protein Conformation; Tryptophan; Tyrosine

1982
Low temperature magnetic circular dichroism spectra and magnetization properties of extracted heme a3+ bis-imidazole. A model of cytochrome a in bovine cytochrome c oxidase.
    Journal of inorganic biochemistry, 1984, Volume: 21, Issue:1

    Topics: Animals; Cattle; Chemical Phenomena; Chemistry, Physical; Circular Dichroism; Cytochrome a Group; Cytochromes; Electron Transport Complex IV; Heme; Histidine; Imidazoles; Models, Biological; Muscles

1984
NMR study of the exchange rates of allosterically responsive labile protons in the heme pockets of hemoglobin A.
    Biophysical journal, 1984, Volume: 46, Issue:1

    Topics: Heme; Hemoglobin A; Histidine; Humans; Macromolecular Substances; Magnetic Resonance Spectroscopy; Protons

1984
Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism.
    Journal of molecular biology, 1983, Dec-25, Volume: 171, Issue:4

    Topics: Allosteric Site; Globins; Heme; Hemoglobins; Histidine; Humans; Hydrogen Bonding; Ligands; Models, Chemical; Models, Molecular; Protein Conformation; X-Rays

1983
Proton nuclear magnetic resonance study of the dynamic stability of the heme pocket of soybean leghemoglobin a. Exchange rates for the labile proton of the proximal histidyl imidazole.
    The Journal of biological chemistry, 1983, Mar-25, Volume: 258, Issue:6

    Topics: Glycine max; Heme; Hemeproteins; Histidine; Hydrogen-Ion Concentration; Kinetics; Leghemoglobin; Magnetic Resonance Spectroscopy

1983
Effect of histidine, cysteine, glutathione or beef on iron absorption in humans.
    The Journal of nutrition, 1984, Volume: 114, Issue:1

    Topics: Absorption; Animals; Cattle; Cysteine; Dose-Response Relationship, Drug; Fabaceae; Female; Glutathione; Heme; Hemoglobins; Histidine; Humans; Iron; Male; Meat; Plants, Medicinal; Zea mays

1984
Subunit heterogeneity in the structure and dynamics of hemoglobin. A transient Raman study.
    FEBS letters, 1983, Jul-11, Volume: 158, Issue:1

    Topics: Heme; Hemoglobins; Histidine; Iron; Ligands; Peptide Fragments; Photochemistry; Protein Binding; Spectrum Analysis, Raman

1983
Differences in Fe(II)-N epsilon(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures.
    Proceedings of the National Academy of Sciences of the United States of America, 1980, Volume: 77, Issue:4

    Topics: Allosteric Regulation; Ferrous Compounds; Heme; Hemoglobin A; Hemoglobins; Hemoglobins, Abnormal; Histidine; Macromolecular Substances; Protein Conformation; Spectrum Analysis, Raman

1980
Resonance Raman detection of structural dynamics at the active site in hemoglobin.
    Proceedings of the National Academy of Sciences of the United States of America, 1982, Volume: 79, Issue:5

    Topics: Heme; Hemoglobins; Histidine; Humans; Motion; Protein Conformation; Spectrum Analysis, Raman; Temperature

1982
Hemoglobins, XLVIIII. The primary structure of a monomeric hemoglobin from the hagfish, Myxine glutinosa L.: evolutionary aspects and comparative studies of the function with special reference to the heme linkage.
    Journal of molecular evolution, 1982, Volume: 18, Issue:2

    Topics: Amino Acid Sequence; Animals; Biological Evolution; Fishes; Glutamine; Hagfishes; Heme; Hemoglobins; Histidine; Humans; Lampreys; Molecular Weight

1982
A proton nuclear magnetic resonance investigation of proximal histidyl residues in human normal and abnormal hemoglobins. A probe for the heme pocket.
    Biophysical journal, 1982, Volume: 39, Issue:1

    Topics: 2,3-Diphosphoglycerate; Binding Sites; Diphosphoglyceric Acids; Heme; Hemoglobin A; Hemoglobins, Abnormal; Histidine; Humans; Macromolecular Substances; Magnetic Resonance Spectroscopy; Phytic Acid; Protein Binding; Protein Conformation

1982
Transient Raman study of hemoglobin: structural dependence of the iron-histidine linkage.
    Science (New York, N.Y.), 1982, Dec-17, Volume: 218, Issue:4578

    Topics: Carboxyhemoglobin; Heme; Hemoglobins; Histidine; Humans; Iron; Motion; Myoglobin; Photolysis; Spectrum Analysis, Raman

1982
Structural implication of the heme-linked ionization of horseradish peroxidase probed by the Fe-histidine stretching Raman line.
    The Journal of biological chemistry, 1981, Apr-25, Volume: 256, Issue:8

    Topics: Heme; Histidine; Horseradish Peroxidase; Iron; Ligands; Peroxidases; Protein Binding; Protein Conformation; Spectrum Analysis, Raman

1981
Interactions of the histidine-rich glycoprotein of serum with metals.
    Biochemistry, 1981, Mar-03, Volume: 20, Issue:5

    Topics: Animals; Binding Sites; Cations, Divalent; Circular Dichroism; Diethyl Pyrocarbonate; Glycoproteins; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Kinetics; Protein Binding; Protein Conformation; Proteins; Rabbits; Spectrometry, Fluorescence; Spectrophotometry

1981
Proton magnetic resonance characterization of the dynamic stability of the heme pocket in myoglobin by the exchange behavior of the labile proton of the proximal histidyl imidazole.
    Biophysical journal, 1981, Volume: 34, Issue:2

    Topics: Animals; Heme; Histidine; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Myoglobin; Protein Conformation; Whales

1981
Structural changes at the heme induced by freezing hemoglobin.
    Science (New York, N.Y.), 1981, Aug-07, Volume: 213, Issue:4508

    Topics: Allosteric Regulation; Freezing; Heme; Hemoglobin A; Histidine; Humans; Motion; Protein Conformation; Spectrum Analysis, Raman; Water

1981
Resonance Raman and absorption spectroscopic detection of distal histidine--fluoride interactions in human methemoglobin fluoride and sperm whale metmyoglobin fluoride: measurements of distal histidine ionization constants.
    Biochemistry, 1981, Jun-09, Volume: 20, Issue:12

    Topics: Animals; Binding Sites; Fluorides; Heme; Hemeproteins; Histidine; Humans; Hydrogen-Ion Concentration; Methemoglobin; Metmyoglobin; Protein Binding; Protein Conformation; Spectrophotometry; Spectrum Analysis, Raman; Whales

1981
Proton nuclear magnetic resonance investigation of the nature of solution conformational equilibria of monomeric insect deoxyhemoglobins.
    Biochemistry, 1981, Jul-21, Volume: 20, Issue:15

    Topics: Animals; Chironomidae; Diptera; Heme; Hemoglobins; Histidine; Larva; Magnetic Resonance Spectroscopy; Protein Conformation; Solutions

1981
Resonance Raman spectroscopy of hemoglobin.
    Methods in enzymology, 1981, Volume: 76

    Topics: Heme; Hemoglobins; Histidine; Humans; Iron; Lasers; Ligands; Mathematics; Protein Conformation; Spectrum Analysis, Raman

1981
Proton nuclear magnetic resonance study of the electronic and molecular structure of the heme crevice in horseradish peroxidase.
    The Journal of biological chemistry, 1980, Jul-25, Volume: 255, Issue:14

    Topics: Heme; Histidine; Horseradish Peroxidase; Magnetic Resonance Spectroscopy; Peroxidases; Protein Binding; Protein Conformation

1980
Isomeric incorporation of the haem into monomeric haemoglobins of Chironomus thummi thummi 3. Comparative study of components, I, III and IV.
    European journal of biochemistry, 1980, Volume: 108, Issue:1

    Topics: Allosteric Regulation; Animals; Carbon Monoxide; Chironomidae; Diptera; Erythrocruorins; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Isomerism; Macromolecular Substances; Magnetic Resonance Spectroscopy; Oxygen

1980
Isomeric incorporation of the haem into monomeric haemoglobins of Chironomus thummi thummi. 1. Isolation of chemically homogeneous haemoglobins. Evidence for the isomerism of the haem in the component III.
    European journal of biochemistry, 1980, Volume: 108, Issue:1

    Topics: Animals; Carbon Monoxide; Chironomidae; Diptera; Erythrocruorins; Heme; Hemoglobins; Histidine; Isomerism; Larva; Macromolecular Substances; Magnetic Resonance Spectroscopy; Protein Conformation

1980
Isomeric incorporation of the Haem into monomeric haemoglobins of Chironomus thummi thummi. 2. The Bohr effect of the component III explained on a molecular basis and functional differences between the two isomeric structures.
    European journal of biochemistry, 1980, Volume: 108, Issue:1

    Topics: Allosteric Regulation; Animals; Carbon Monoxide; Chironomidae; Diptera; Erythrocruorins; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Isomerism; Macromolecular Substances; Magnetic Resonance Spectroscopy; Protein Conformation; Thermodynamics

1980
Conformational changes in the hemoglobin S system as seen by proton binding.
    The Journal of biological chemistry, 1980, Sep-25, Volume: 255, Issue:18

    Topics: Carboxyhemoglobin; Heme; Hemoglobin A; Hemoglobin, Sickle; Histidine; Humans; Hydrogen-Ion Concentration; Macromolecular Substances; Magnetic Resonance Spectroscopy; Mercuribenzoates; Osmolar Concentration; Protein Binding; Protein Conformation

1980
Prokaryotic expression of the heme- and flavin-binding domains of rat neuronal nitric oxide synthase as distinct polypeptides: identification of the heme-binding proximal thiolate ligand as cysteine-415.
    Biochemistry, 1995, Mar-21, Volume: 34, Issue:11

    Topics: Amino Acid Oxidoreductases; Animals; Base Sequence; Cloning, Molecular; Cysteine; DNA Primers; Escherichia coli; Flavins; Heme; Hemeproteins; Histidine; Molecular Sequence Data; Mutagenesis, Site-Directed; Neurons; Nitric Oxide Synthase; Peptides; Rats

1995
Trans effects on cysteine ligation in the proximal His93Cys variant of horse heart myoglobin.
    Biochemistry, 1995, Sep-12, Volume: 34, Issue:36

    Topics: Animals; Circular Dichroism; Cysteine; Cytochrome P-450 Enzyme System; Electrochemistry; Electron Spin Resonance Spectroscopy; Ferric Compounds; Heme; Histidine; Horses; Humans; Magnetic Resonance Spectroscopy; Magnetics; Myocardium; Myoglobin

1995
Determination of haem electronic structure in cytochrome b5 and metcyanomyoglobin.
    European journal of biochemistry, 1995, Sep-01, Volume: 232, Issue:2

    Topics: Animals; Carbon; Cattle; Cytochromes b5; Electrochemistry; Heme; Histidine; Ligands; Magnetic Resonance Spectroscopy; Metmyoglobin; Molecular Structure; Rats; Recombinant Proteins; Whales

1995
Effect of the His175-->Glu mutation on the heme pocket architecture of cytochrome c peroxidase.
    Biochemistry, 1995, Oct-17, Volume: 34, Issue:41

    Topics: Amino Acid Sequence; Binding Sites; Cytochrome-c Peroxidase; Glutamic Acid; Heme; Histidine; Magnetic Resonance Spectroscopy; Models, Molecular; Mutagenesis, Site-Directed; Point Mutation; Recombinant Proteins; Spectrophotometry; Spectrum Analysis, Raman; X-Ray Diffraction

1995
Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli.
    Biochemistry, 1995, Oct-17, Volume: 34, Issue:41

    Topics: Amino Acid Sequence; Base Sequence; Cytochrome b Group; Cytochromes; Dithionite; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Genotype; Heme; Histidine; Leucine; Ligands; Macromolecular Substances; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; NADPH Oxidases; Oligodeoxyribonucleotides; Oxidation-Reduction; Oxidoreductases; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Restriction Mapping; Spectrophotometry

1995
Laser photolysis behavior of ferrous horseradish peroxidase with carbon monoxide and cyanide: effects of mutations in the distal heme pocket.
    Biochemistry, 1995, Nov-14, Volume: 34, Issue:45

    Topics: Arginine; Base Sequence; Carbon Monoxide; Cyanides; Ferrous Compounds; Heme; Histidine; Horseradish Peroxidase; Kinetics; Lasers; Molecular Sequence Data; Mutagenesis, Site-Directed; Photolysis; Recombinant Proteins; Spectrum Analysis

1995
A method of directed random mutagenesis of the yeast chromosome shows that the iso-1-cytochrome c heme ligand His18 is essential.
    Gene, 1995, Oct-16, Volume: 164, Issue:1

    Topics: Base Sequence; Binding Sites; Chromosomes, Fungal; Cytochrome c Group; Cytochromes c; Heme; Histidine; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Saccharomyces cerevisiae Proteins; Selection, Genetic; Spectrophotometry; Structure-Activity Relationship; Transformation, Genetic; Yeasts

1995
Alteration of axial coordination by protein engineering in myoglobin. Bisimidazole ligation in the His64-->Val/Val68-->His double mutant.
    The Journal of biological chemistry, 1995, Jul-07, Volume: 270, Issue:27

    Topics: Animals; Carbon Monoxide; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Heme; Histidine; Humans; Imidazoles; Ligands; Models, Molecular; Mutation; Myoglobin; Protein Engineering; Spectrophotometry; Spectrum Analysis; Swine; Valine; X-Rays

1995
Structure of CuB in the binuclear heme-copper center of the cytochrome aa3-type quinol oxidase from Bacillus subtilis: an ENDOR and EXAFS study.
    Biochemistry, 1995, Aug-15, Volume: 34, Issue:32

    Topics: Bacillus subtilis; Copper; Electron Transport Complex IV; Heme; Histidine; Hydrogen-Ion Concentration; Oxidoreductases; Protein Conformation; Spectrum Analysis

1995
Horseradish peroxidase His-42 --> Ala, His-42 --> Val, and Phe-41 --> Ala mutants. Histidine catalysis and control of substrate access to the heme iron.
    The Journal of biological chemistry, 1995, Aug-18, Volume: 270, Issue:33

    Topics: Alanine; Animals; Catalysis; Cell Line; Heme; Histidine; Horseradish Peroxidase; Imines; Iron; Kinetics; Mutagenesis, Site-Directed; Phenylalanine; Recombinant Proteins; Spectrum Analysis; Spodoptera; Substrate Specificity; Sulfides; Sulfoxides; Valine

1995
Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysis.
    The Journal of biological chemistry, 1995, Sep-15, Volume: 270, Issue:37

    Topics: Amino Acid Sequence; Arginine; Binding Sites; Computer Graphics; Crystallography, X-Ray; Fourier Analysis; Heme; Histidine; Hydrogen-Ion Concentration; Iodides; Mitosporic Fungi; Models, Molecular; Periodic Acid; Peroxidases; Potassium Compounds; Potassium Cyanide

1995
Identification of the histidine residues of hemopexin that coordinate with heme-iron and of a receptor-binding region.
    The Journal of biological chemistry, 1993, Mar-25, Volume: 268, Issue:9

    Topics: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Base Sequence; Chromatography, High Pressure Liquid; DNA; Epitopes; Heme; Hemopexin; Histidine; Humans; Iron; Molecular Sequence Data; Rabbits; Receptors, Cell Surface; Receptors, Peptide; Sequence Homology, Amino Acid; Structure-Activity Relationship

1993
The distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of two distal histidine tautomers.
    Biophysical journal, 1994, Volume: 67, Issue:6

    Topics: Animals; Biophysical Phenomena; Biophysics; Carbon Monoxide; Crystallography, X-Ray; Electrochemistry; Heme; Histidine; Ligands; Models, Molecular; Molecular Structure; Myoglobin; Protein Structure, Tertiary; Spectrophotometry, Infrared; Stereoisomerism; Thermodynamics

1994
Studies of the heme coordination and ligand binding properties of soluble guanylyl cyclase (sGC): characterization of Fe(II)sGC and Fe(II)sGC(CO) by electronic absorption and magnetic circular dichroism spectroscopies and failure of CO to activate the enz
    Biochemistry, 1995, May-02, Volume: 34, Issue:17

    Topics: Animals; Carbon Monoxide; Cattle; Circular Dichroism; Enzyme Activation; Ferrous Compounds; Glycerol; Guanylate Cyclase; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Nitric Oxide

1995
The structure of Ascaris hemoglobin domain I at 2.2 A resolution: molecular features of oxygen avidity.
    Proceedings of the National Academy of Sciences of the United States of America, 1995, May-09, Volume: 92, Issue:10

    Topics: Amino Acid Sequence; Animals; Ascaris; Binding Sites; Crystallization; Crystallography, X-Ray; Heme; Hemoglobins; Histidine; Models, Molecular; Molecular Sequence Data; Myoglobin; Oxygen; Oxyhemoglobins; Protein Structure, Secondary; Recombinant Proteins; Sequence Homology, Amino Acid; Software; Whales

1995
The haem b558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation.
    The Biochemical journal, 1995, Jun-01, Volume: 308 ( Pt 2)

    Topics: Bacterial Proteins; Circular Dichroism; Cytochrome b Group; Cytochromes; Electron Spin Resonance Spectroscopy; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Methionine; NADPH Oxidases; Oxidoreductases; Spectrophotometry, Ultraviolet

1995
Resonance Raman investigation of imidazole and imidazolate complexes of microperoxidase: characterization of the bis(histidine) axial ligation in c-type cytochromes.
    Biochemistry, 1994, Dec-27, Volume: 33, Issue:51

    Topics: Cytochrome c Group; Ferric Compounds; Heme; Hemeproteins; Histidine; Imidazoles; Ligands; Peroxidases; Spectrum Analysis, Raman

1994
Construction of a bisaquo heme enzyme and binding by exogenous ligands.
    Proceedings of the National Academy of Sciences of the United States of America, 1994, Dec-20, Volume: 91, Issue:26

    Topics: Crystallography, X-Ray; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Histidine; Iron; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Recombinant Proteins; Spectrum Analysis; Structure-Activity Relationship

1994
Evidence for sub-picosecond heme doming in hemoglobin and myoglobin: a time-resolved resonance Raman comparison of carbonmonoxy and deoxy species.
    Biochemistry, 1995, Jan-31, Volume: 34, Issue:4

    Topics: Carboxyhemoglobin; Heme; Hemoglobin A; Hemoglobins; Histidine; Humans; Iron; Kinetics; Myoglobin; Photolysis; Spectrum Analysis, Raman; Time Factors

1995
The oxygen sensor protein, FixL, of Rhizobium meliloti. Role of histidine residues in heme binding, phosphorylation, and signal transduction.
    The Journal of biological chemistry, 1995, Mar-10, Volume: 270, Issue:10

    Topics: Bacterial Proteins; Base Sequence; Binding Sites; Heme; Hemeproteins; Histidine; Histidine Kinase; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Oxygen; Phosphorylation; Protein Kinases; Recombinant Proteins; Restriction Mapping; Signal Transduction; Sinorhizobium meliloti; Spectrophotometry

1995
Role of alpha and beta carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly.
    The Journal of biological chemistry, 1994, Mar-18, Volume: 269, Issue:11

    Topics: Amino Acid Sequence; Arginine; Genetic Variation; Glutamates; Glutamic Acid; Heme; Hemoglobin A; Hemoglobins, Abnormal; Histidine; Humans; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; Oxyhemoglobins; Point Mutation; Spectrophotometry; Tyrosine; Valine

1994
Mutation of His-105 in the beta 1 subunit yields a nitric oxide-insensitive form of soluble guanylyl cyclase.
    Proceedings of the National Academy of Sciences of the United States of America, 1994, Mar-29, Volume: 91, Issue:7

    Topics: Amino Acid Sequence; Animals; Cyclic GMP; Enzyme Activation; Glutathione; Guanosine Triphosphate; Guanylate Cyclase; Heme; Histidine; Molecular Sequence Data; Mutation; Nitric Oxide; Nitroprusside; Nitroso Compounds; S-Nitrosoglutathione; Spectrophotometry

1994
Identification of histidine 25 as the heme ligand in human liver heme oxygenase.
    Biochemistry, 1994, Nov-22, Volume: 33, Issue:46

    Topics: Carbon Monoxide; Heme; Heme Oxygenase (Decyclizing); Histidine; Humans; Ligands; Liver; Oxidation-Reduction; Point Mutation; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman

1994
Effect of single-point mutations Phe41-->His and Phe143-->Glu on folding and catalytic properties of recombinant horseradish peroxidase expressed in E. coli.
    FEBS letters, 1994, Nov-14, Volume: 354, Issue:3

    Topics: Base Sequence; Binding Sites; Catalysis; Escherichia coli; Glutamic Acid; Heme; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; Point Mutation; Protein Folding; Recombinant Proteins; Structure-Activity Relationship

1994
Crystal structure of cytochrome c3 from Desulfovibrio desulfuricans Norway at 1.7 A resolution.
    Journal of molecular biology, 1994, Nov-04, Volume: 243, Issue:4

    Topics: Amino Acid Sequence; Computer Simulation; Crystallography, X-Ray; Cytochrome c Group; Desulfovibrio; Heme; Histidine; Hydrogen Bonding; Ligands; Models, Molecular; Molecular Sequence Data; Molecular Weight; Protein Conformation; Protein Structure, Secondary; Solvents; Temperature; Water

1994
Identification of the axial heme ligands of cytochrome b556 in succinate: ubiquinone oxidoreductase from Escherichia coli.
    FEBS letters, 1994, Nov-28, Volume: 355, Issue:2

    Topics: Binding Sites; Circular Dichroism; Cytochrome b Group; Electron Spin Resonance Spectroscopy; Electron Transport Complex II; Escherichia coli; Heme; Histidine; Ligands; Multienzyme Complexes; Oxidoreductases; Succinate Dehydrogenase

1994
Characterization of recombinant horseradish peroxidase C and three site-directed mutants, F41V, F41W, and R38K, by resonance Raman spectroscopy.
    Biochemistry, 1994, Jun-14, Volume: 33, Issue:23

    Topics: Base Sequence; Butylated Hydroxyanisole; DNA; Escherichia coli; Heme; Histidine; Horseradish Peroxidase; Iron; Isoenzymes; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Recombinant Proteins; Spectrum Analysis, Raman

1994
FTIR analysis of the interaction of azide with horse heart myoglobin variants.
    Biochemistry, 1994, Jun-21, Volume: 33, Issue:24

    Topics: Animals; Azides; Binding Sites; Electrochemistry; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Models, Molecular; Molecular Structure; Mutation; Myocardium; Myoglobin; Protein Binding; Recombinant Proteins; Spectrophotometry; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship; Temperature

1994
Active site coordination chemistry of the cytochrome c peroxidase Asp235Ala variant: spectroscopic and functional characterization.
    Biochemistry, 1994, Jun-28, Volume: 33, Issue:25

    Topics: Alanine; Aspartic Acid; Base Sequence; Binding Sites; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Iron; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Recombinant Proteins; Spectrum Analysis; Structure-Activity Relationship; Temperature; Tryptophan

1994
Characterization of mutant Met100Lys of cytochrome c-550 from Thiobacillus versutus with lysine-histidine heme ligation.
    Biochemistry, 1994, Aug-23, Volume: 33, Issue:33

    Topics: Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Lysine; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Mutation; Spectrophotometry; Structure-Activity Relationship; Thiobacillus

1994
Roles of heme iron-coordinating histidine residues of human hemopexin expressed in baculovirus-infected insect cells.
    Proceedings of the National Academy of Sciences of the United States of America, 1994, Aug-30, Volume: 91, Issue:18

    Topics: Animals; Baculoviridae; Base Sequence; Heme; Hemopexin; Histidine; Humans; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Moths; Mutagenesis, Site-Directed; Protein Binding; Recombinant Fusion Proteins; Spectrum Analysis; Structure-Activity Relationship

1994
Spectroscopic characterization of flavocytochrome c-552 from the photosynthetic purple sulfur bacterium Chromatium vinosum.
    Biochimica et biophysica acta, 1994, Mar-08, Volume: 1184, Issue:2-3

    Topics: Chromatium; Circular Dichroism; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Ethylene Glycol; Ethylene Glycols; Heme; Histidine; Methionine; Spectrophotometry, Infrared; Spectrum Analysis

1994
Structural characterization of heme ligation in the His64-->Tyr variant of myoglobin.
    The Journal of biological chemistry, 1994, Apr-29, Volume: 269, Issue:17

    Topics: Animals; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Myocardium; Myoglobin; Protein Conformation; Tyrosine

1994
Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly.
    Biochemistry, 1994, May-31, Volume: 33, Issue:21

    Topics: Animals; Crystallography, X-Ray; Escherichia coli; Glycine; Heme; Histidine; Imidazoles; Ligands; Mutagenesis, Site-Directed; Myoglobin; Protein Conformation; Spectrum Analysis; Whales

1994
EPR studies on the photoproducts of manganese(II) protoporphyrin-IX substituted myoglobin nitrosyl complexes trapped at low temperature: effects of site-specific chemical modification of the distal histidine on ligand-binding structures.
    Biochimica et biophysica acta, 1993, Nov-10, Volume: 1203, Issue:1

    Topics: Cyanates; Electron Spin Resonance Spectroscopy; Heme; Histidine; Myoglobin; Photolysis; Protoporphyrins; Temperature; Tetrazoles

1993
Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli.
    Biochemistry, 1993, Dec-07, Volume: 32, Issue:48

    Topics: Amino Acid Sequence; Bacterial Proteins; Electron Transport Complex IV; Escherichia coli; Genetic Complementation Test; Heme; Histidine; Ligands; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Recombinant Proteins; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship

1993
1H NMR study of the solution molecular and electronic structure of engineered distal myoglobin His64(E7) Val/Val68(E11) His double mutant. Coordination of His64(E11) at the sixth position in both low-spin and high-spin states.
    The Journal of biological chemistry, 1994, Jan-14, Volume: 269, Issue:2

    Topics: Amino Acid Sequence; Heme; Histidine; Humans; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Metmyoglobin; Molecular Sequence Data; Mutagenesis, Site-Directed; Recombinant Proteins; Solutions; Structure-Activity Relationship; Temperature; Valine

1994
Nitrate reductase of Neurospora crassa: the functional role of individual amino acids in the heme domain as examined by site-directed mutagenesis.
    Molecular & general genetics : MGG, 1993, Volume: 240, Issue:2

    Topics: Amino Acid Sequence; Amino Acids; Binding Sites; Blotting, Southern; Enzyme Stability; Heme; Histidine; Molecular Sequence Data; Mutagenesis, Site-Directed; Neurospora crassa; Nitrate Reductase; Nitrate Reductases; Phenotype; Protein Structure, Tertiary; Transformation, Genetic

1993
Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase.
    Biochemistry, 1993, Jan-12, Volume: 32, Issue:1

    Topics: Benzene Derivatives; Binding Sites; Catalase; Chloride Peroxidase; Cysteine; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Heme; Histidine; Humans; Iron; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Myoglobin; Spectrophotometry; Spectrum Analysis, Raman; Tyrosine

1993
Pitfalls in assigning heme axial coordination by EPR. c-Type cytochromes with atypical Met-His ligation.
    FEBS letters, 1993, Feb-15, Volume: 317, Issue:3

    Topics: Bacterial Proteins; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Histidine; Magnetic Resonance Spectroscopy; Methionine; Spectrum Analysis

1993
The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme.
    Biochemistry, 1993, Apr-06, Volume: 32, Issue:13

    Topics: Aspartic Acid; Binding Sites; Crystallography; Cytochrome-c Peroxidase; DNA Mutational Analysis; Electron Spin Resonance Spectroscopy; Ferric Compounds; Free Radicals; Heme; Histidine; Hydrogen Bonding; In Vitro Techniques; Kinetics; Models, Molecular; Oxidation-Reduction; Recombinant Proteins; Structure-Activity Relationship; Tryptophan; X-Ray Diffraction

1993
Effects of charged amino acid mutations on the bimolecular kinetics of reduction of yeast iso-1-ferricytochrome c by bovine ferrocytochrome b5.
    Biochemistry, 1993, Jul-06, Volume: 32, Issue:26

    Topics: Amino Acid Sequence; Animals; Binding Sites; Cattle; Cytochrome c Group; Cytochromes b5; Cytochromes c; Heme; Histidine; Kinetics; Liver; Lysine; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins

1993
Optical activity of hemoproteins in the Soret region. Circular dichroism of the heme undecapeptide of cytochrome c in aqueous solution.
    Biochemistry, 1993, Jul-06, Volume: 32, Issue:26

    Topics: Animals; Circular Dichroism; Cytochrome c Group; Heme; Hemeproteins; Histidine; Horses; Mathematics; Myoglobin; Peroxidases; Protein Conformation; Solutions; Spectrophotometry; Water

1993
Cytochrome c6 from Monoraphidium braunii. A cytochrome with an unusual heme axial coordination.
    European journal of biochemistry, 1993, Aug-15, Volume: 216, Issue:1

    Topics: Amino Acid Sequence; Chlorophyta; Cytochromes; Cytochromes f; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Isoelectric Point; Methionine; Molecular Sequence Data; Molecular Weight; Oxidation-Reduction; Sequence Alignment; Spectrophotometry, Ultraviolet; Spectroscopy, Mossbauer; Surface-Active Agents

1993
A heme c-peptide model system for the resonance Raman study of c-type cytochromes: characterization of the solvent-dependence of peptide-histidine-heme interactions.
    Biochemistry, 1993, Sep-21, Volume: 32, Issue:37

    Topics: Amino Acid Sequence; Animals; Cytochrome c Group; Heme; Histidine; Horses; Models, Molecular; Molecular Sequence Data; Peptides; Porphyrins; Protein Structure, Secondary; Solvents; Spectrum Analysis; Spectrum Analysis, Raman; Structure-Activity Relationship

1993
Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I.
    Biochemistry, 1993, Sep-21, Volume: 32, Issue:37

    Topics: Crystallography; Cytochrome-c Peroxidase; Fungal Proteins; Heme; Histidine; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Recombinant Proteins; Saccharomyces cerevisiae; Spectrum Analysis; Structure-Activity Relationship; X-Ray Diffraction

1993
Substitution of a haem-iron axial ligand in flavocytochrome b2.
    Biochimica et biophysica acta, 1993, Sep-03, Volume: 1202, Issue:1

    Topics: Base Sequence; Cytochromes b5; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Histidine; Iron; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Methionine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Spectrum Analysis

1993
Specific modification of structure and property of myoglobin by the formation of tetrazolylhistidine 64(E7). Reaction of the modified myoglobin with molecular oxygen.
    The Journal of biological chemistry, 1993, Sep-25, Volume: 268, Issue:27

    Topics: Amino Acid Sequence; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Histidine; Humans; Kinetics; Mutagenesis, Site-Directed; Myoglobin; Oxidation-Reduction; Oxygen Consumption; Protein Binding; Spectrophotometry; Tetrazoles; X-Ray Diffraction

1993
Identity of the axial ligand of the high-spin heme in cytochrome oxidase: spectroscopic characterization of mutants in the bo-type oxidase of Escherichia coli and the aa3-type oxidase of Rhodobacter sphaeroides.
    Biochemistry, 1993, Oct-12, Volume: 32, Issue:40

    Topics: Amino Acid Sequence; Binding Sites; Darkness; Electron Transport Complex IV; Escherichia coli; Heme; Histidine; Light; Macromolecular Substances; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Rhodobacter sphaeroides; Spectrophotometry; Spectroscopy, Fourier Transform Infrared

1993
Protein and amino acid oxidation is associated with increased chemiluminescence.
    Archives of biochemistry and biophysics, 1993, Feb-01, Volume: 300, Issue:2

    Topics: Antioxidants; Deferoxamine; Dimethyl Sulfoxide; Ethylamines; Heme; Histidine; Kinetics; Luminescent Measurements; Oxidation-Reduction; Oxygen Consumption; Peroxides; Piperazines; Pyridines; Serum Albumin, Bovine; Superoxide Dismutase; tert-Butylhydroperoxide; Tryptophan; Tyrosine

1993
Heme-heme interactions in a homodimeric cooperative hemoglobin. Evidence from transient Raman scattering.
    The Journal of biological chemistry, 1993, Mar-15, Volume: 268, Issue:8

    Topics: Animals; Bivalvia; Carbon Monoxide; Heme; Hemoglobins; Histidine; Iron; Protein Conformation; Spectrum Analysis, Raman

1993
Domains of rat heme oxygenase-2: the amino terminus and histidine 151 are required for heme oxidation.
    Archives of biochemistry and biophysics, 1993, Volume: 302, Issue:2

    Topics: Amino Acid Sequence; Animals; Base Sequence; Cell Compartmentation; Cloning, Molecular; Escherichia coli; Heme; Heme Oxygenase (Decyclizing); Histidine; Male; Membranes; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Structure, Secondary; Rats; Recombinant Proteins; Structure-Activity Relationship; Testis

1993
Solution structure determination of the heme cavity in the E7 His-->Val cyano-met myoglobin point mutant based on the 1H NMR detected dipolar field of the iron: evidence for contraction of the heme pocket.
    Biochemistry, 1993, Jun-01, Volume: 32, Issue:21

    Topics: Amino Acid Sequence; Animals; Binding Sites; Heme; Histidine; Hydrogen; Magnetic Resonance Spectroscopy; Mathematics; Metmyoglobin; Point Mutation; Protein Structure, Secondary; Valine; Whales

1993
Sequential assignment of proton resonances in the NMR spectrum of Zn-substituted alpha chains from human hemoglobin. Ligand-induced tertiary changes in the heme pocket.
    European journal of biochemistry, 1993, Jun-01, Volume: 214, Issue:2

    Topics: Amino Acid Sequence; Binding Sites; Globins; Heme; Hemoglobins; Histidine; Humans; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Molecular Structure; Protein Conformation; Protein Structure, Secondary; Solutions; Zinc

1993
MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain.
    Biochimica et biophysica acta, 1995, Dec-06, Volume: 1253, Issue:2

    Topics: Amino Acid Sequence; Animals; Apoproteins; Binding Sites; Circular Dichroism; Electron Spin Resonance Spectroscopy; Heme; Hemopexin; Histidine; Hydrogen-Ion Concentration; Ligands; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Peptide Fragments; Rabbits

1995
[Production and catalytic properties of point mutants Phe41--->His and Phe143--->Glu of horseradish peroxidase, expressed in Escherichia coli].
    Biokhimiia (Moscow, Russia), 1995, Volume: 60, Issue:10

    Topics: Amino Acid Sequence; Base Sequence; Catalysis; Cloning, Molecular; DNA, Recombinant; Enzyme Stability; Escherichia coli; Glutamic Acid; Heme; Histidine; Horseradish Peroxidase; Molecular Sequence Data; Oxidation-Reduction; Phenylalanine; Point Mutation

1995
Pentacoordination of the heme iron of Arthromyces ramosus peroxidase shown by a 1.8 A resolution crystallographic study at pH 4.5.
    FEBS letters, 1996, Jan-15, Volume: 378, Issue:3

    Topics: Crystallography, X-Ray; Cytochrome-c Peroxidase; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Iron; Mitosporic Fungi; Models, Molecular; Peroxidase; Peroxidases; Protein Conformation; Spectrophotometry; Water

1996
EPR study of NO complex of bd-type ubiquinol oxidase from Escherichia coli.
    The Journal of biological chemistry, 1996, Apr-19, Volume: 271, Issue:16

    Topics: Binding Sites; Cytochrome a Group; Cytochrome b Group; Cytochrome d Group; Cytochromes; Cytochromes a1; Electron Spin Resonance Spectroscopy; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Kinetics; Ligands; Nitric Oxide; Oxidoreductases

1996
Endothelial nitric-oxide synthase. Expression in Escherichia coli, spectroscopic characterization, and role of tetrahydrobiopterin in dimer formation.
    The Journal of biological chemistry, 1996, May-10, Volume: 271, Issue:19

    Topics: Animals; Arginine; Biopterins; Cattle; Chromatography, Affinity; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Endothelium, Vascular; Heme; Histidine; Kinetics; Macromolecular Substances; Molecular Weight; Nitric Oxide Synthase; Protein Denaturation; Recombinant Proteins; Restriction Mapping; Sequence Tagged Sites; Spectrophotometry; Substrate Specificity

1996
Crystal structures of CO-, deoxy- and met-myoglobins at various pH values.
    Journal of molecular biology, 1996, Mar-08, Volume: 256, Issue:4

    Topics: Animals; Anisotropy; Carbon Monoxide; Computer Graphics; Crystallization; Crystallography, X-Ray; Heme; Histidine; Hydrogen-Ion Concentration; Metmyoglobin; Models, Molecular; Myoglobin; Protein Conformation; Protein Structure, Tertiary; Whales

1996
Rescue of the catalytic activity of an H42A mutant of horseradish peroxidase by exogenous imidazoles.
    The Journal of biological chemistry, 1996, Jun-21, Volume: 271, Issue:25

    Topics: Binding Sites; Catalysis; Cloning, Molecular; Cyanides; Escherichia coli; Guaiacol; Heme; Histidine; Horseradish Peroxidase; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Point Mutation; Recombinant Proteins; Sequence Tagged Sites; Spectrophotometry

1996
Global mapping of structural solutions provided by the extended X-ray absorption fine structure ab initio code FEFF 6.01: structure of the cryogenic photoproduct of the myoglobin-carbon monoxide complex.
    Biochemistry, 1996, Jul-16, Volume: 35, Issue:28

    Topics: Animals; Carbon Monoxide; Computer Simulation; Crystallography, X-Ray; Heme; Histidine; Horses; Iron; Muscle, Skeletal; Myoglobin; Photolysis; Software; Spectrophotometry; Spectrum Analysis, Raman; Temperature

1996
Evidence for a proximal histidine interaction in the structure of cytochromes c in solution: a resonance Raman study.
    Biochemistry, 1996, Jul-16, Volume: 35, Issue:28

    Topics: Amino Acid Sequence; Binding Sites; Cytochrome c Group; Heme; Histidine; Hydrogen Bonding; Molecular Sequence Data; Oxidation-Reduction; Rhodobacter sphaeroides; Rhodospirillum; Spectrum Analysis, Raman

1996
Assignment of the hyperfine-shifted 1H-NMR signals of the heme in the oxygen sensor FixL from Rhizobium meliloti.
    Chemistry & biology, 1996, Volume: 3, Issue:7

    Topics: Bacterial Proteins; Biosensing Techniques; Heme; Hemeproteins; Histidine; Histidine Kinase; Ligands; Magnetic Resonance Spectroscopy; Molecular Structure; Oxygen; Protons; Sinorhizobium meliloti

1996
Histidine 131, not histidine 43, of the Bradyrhizobium japonicum FixN protein is exposed towards the periplasm and essential for the function of the cbb3-type cytochrome oxidase.
    FEBS letters, 1996, Oct-07, Volume: 394, Issue:3

    Topics: Bacterial Proteins; Cell Polarity; Heme; Histidine; Ligands; Membrane Proteins; Mutagenesis, Site-Directed; Mutation; Oxidoreductases; Protein Conformation; Rhizobiaceae

1996
Resonance Raman spectroscopy of the integral quinol oxidase complex of Sulfolobus acidocaldarius.
    Biochemistry, 1996, Oct-01, Volume: 35, Issue:39

    Topics: Animals; Cattle; Electron Transport Complex IV; Heme; Histidine; Oxidation-Reduction; Oxidoreductases; Spectrophotometry; Spectrum Analysis, Raman; Structure-Activity Relationship; Sulfolobus acidocaldarius

1996
Preparation and reactions of myoglobin mutants bearing both proximal cysteine ligand and hydrophobic distal cavity: protein models for the active site of P-450.
    Biochemistry, 1996, Oct-08, Volume: 35, Issue:40

    Topics: Acetophenones; Aniline Compounds; Benzene Derivatives; Binding Sites; Cysteine; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Histidine; Humans; Kinetics; Magnetic Resonance Spectroscopy; Models, Chemical; Mutagenesis, Site-Directed; Myoglobin; Protein Conformation; Recombinant Proteins; Spectrophotometry, Ultraviolet; Sulfoxides

1996
The distal glutamic acid as an acid-base catalyst in the distal site of horseradish peroxidase.
    Biochemical and biophysical research communications, 1996, Oct-14, Volume: 227, Issue:2

    Topics: Amino Acid Sequence; Binding Sites; Chloride Peroxidase; Glutamic Acid; Guaiacol; Heme; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Oxidation-Reduction; Polymerase Chain Reaction; Recombinant Proteins; Spectrophotometry

1996
A new EPR signal from cytochrome oxidase--evidence for conformational flexibility at the CuB site?
    Biochemical Society transactions, 1996, Volume: 24, Issue:3

    Topics: Animals; Binding Sites; Copper; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Heme; Histidine; Molecular Structure; Oxidation-Reduction; Protein Conformation

1996
H-NMR study of temperature-induced structure alteration at the active site of horse heart cytochrome c.
    Journal of biochemistry, 1996, Volume: 119, Issue:1

    Topics: Animals; Binding Sites; Cytochrome c Group; Heme; Histidine; Horses; Imidazoles; Magnetic Resonance Spectroscopy; Models, Molecular; Myocardium; Protons; Temperature

1996
The Asp245-->Asn mutant of Coprinus cinereus peroxidase. Characterization by 1H-NMR spectroscopy and comparison with the wild-type enzyme.
    Biochemistry, 1996, Nov-12, Volume: 35, Issue:45

    Topics: Arginine; Coprinus; Cyanides; Fluorides; Fungal Proteins; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Peroxidases; Point Mutation

1996
Photolysis of the carbon monoxide complex of myoglobin: nanosecond time-resolved crystallography.
    Science (New York, N.Y.), 1996, Dec-06, Volume: 274, Issue:5293

    Topics: Carbon Monoxide; Computer Simulation; Crystallography, X-Ray; Fourier Analysis; Globins; Heme; Histidine; Iron; Ligands; Myoglobin; Photolysis; Temperature; Time Factors

1996
Triplet state magnetic resonance and fluorescence spectroscopy of metal-substituted hemoglobins.
    Biophysical journal, 1997, Volume: 72, Issue:1

    Topics: Animals; Binding Sites; Cattle; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Macromolecular Substances; Magnesium; Magnetic Resonance Spectroscopy; Models, Structural; Models, Theoretical; Protein Conformation; Protoporphyrins; Spectrometry, Fluorescence; Zinc

1997
Theoretical study of the electrostatic and steric effects on the spectroscopic characteristics of the metal-ligand unit of heme proteins. 2. C-O vibrational frequencies, 17O isotropic chemical shifts, and nuclear quadrupole coupling constants.
    Biophysical journal, 1997, Volume: 72, Issue:2 Pt 1

    Topics: Carbon Monoxide; Heme; Hemeproteins; Hemoglobins; Histidine; Iron; Ligands; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Structure; Myoglobin; Oxygen; Oxygen Isotopes; Porphyrins; Protein Conformation

1997
1H-NMR study of inter-segmental hydrogen bonds in sperm whale and horse apomyoglobins.
    European journal of biochemistry, 1997, Jan-15, Volume: 243, Issue:1-2

    Topics: Animals; Apoproteins; Aspartic Acid; Guanidine; Guanidines; Heme; Histidine; Horses; Hydrogen Bonding; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Myoglobin; Protein Conformation; Protein Denaturation; Temperature; Whales

1997
Notomastus lobatus chloroperoxidase and Amphitrite ornata dehaloperoxidase both contain histidine as their proximal heme iron ligand.
    Biochemistry, 1997, Feb-25, Volume: 36, Issue:8

    Topics: Animals; Binding Sites; Chloride Peroxidase; Heme; Hemoglobins; Histidine; Iron; Ligands; Peroxidases; Polychaeta

1997
CbiX: a novel metal-binding protein involved in sirohaem biosynthesis in Bacillus megaterium.
    Biochemical Society transactions, 1997, Volume: 25, Issue:1

    Topics: Amino Acid Sequence; Bacillus megaterium; Binding Sites; Carrier Proteins; Cloning, Molecular; Escherichia coli; Heme; Histidine; Metals; Molecular Sequence Data; Operon; Recombinant Proteins; Sequence Homology, Amino Acid; Vitamin B 12

1997
The effects of imidazole binding on the conformation of cytochrome c.
    Biochimica et biophysica acta, 1997, Apr-04, Volume: 1338, Issue:2

    Topics: Cytochrome c Group; Heme; Histidine; Hydrogen Bonding; Imidazoles; Protein Conformation

1997
A 4-term energy level scheme for the high-spin ferrous hemoproteins: evidence for the 5E eta, and 5B2 terms as the ground multiplets in hemoproteins with a histidine and a cysteine protein-derived heme ligand, respectively.
    Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 1997, Volume: 53A, Issue:3

    Topics: Animals; Chloride Peroxidase; Circular Dichroism; Computer Simulation; Cysteine; Cytochrome P-450 Enzyme System; Heme; Histidine; Horseradish Peroxidase; Imidazoles; In Vitro Techniques; Magnetic Resonance Spectroscopy; Models, Chemical; Myoglobin; Spectroscopy, Mossbauer; Temperature; Thermodynamics

1997
One-step purification of histidine-tagged cytochrome bo3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase.
    Biochimica et biophysica acta, 1997, Jun-20, Volume: 1340, Issue:1

    Topics: Benzoquinones; Binding Sites; Chromatography, Affinity; Cytochrome b Group; Cytochromes; Detergents; DNA Restriction Enzymes; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Glucosides; Heme; Histidine; Hydrogen-Ion Concentration; Nickel; Octoxynol; Polymerase Chain Reaction; Protein Engineering; Sucrose

1997
Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state.
    Journal of molecular biology, 1997, Aug-15, Volume: 271, Issue:2

    Topics: Binding Sites; Heme; Hemoglobin A; Hemoglobins; Histidine; Humans; Iron; Macromolecular Substances; Models, Molecular; Oxyhemoglobins; Porphyrins; Protein Conformation

1997
Bound water in the proton translocation mechanism of the haem-copper oxidases.
    FEBS letters, 1997, Sep-08, Volume: 414, Issue:2

    Topics: Amino Acid Sequence; Binding Sites; Cloning, Molecular; Conserved Sequence; Copper; Cytochrome b Group; Cytochromes; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Ion Channels; Ligands; Models, Chemical; Models, Molecular; Models, Statistical; Oxidation-Reduction; Protein Conformation; Protons; Water

1997
Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A.
    The Journal of biological chemistry, 1997, Oct-10, Volume: 272, Issue:41

    Topics: Cold Temperature; Conserved Sequence; Cytochrome b Group; Dimerization; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Histidine; Mutagenesis, Site-Directed; Nitrate Reductase; Nitrate Reductases; Potentiometry; Protein Structure, Secondary; Spectrophotometry, Atomic

1997
Reaction of variant sperm-whale myoglobins with hydrogen peroxide: the effects of mutating a histidine residue in the haem distal pocket.
    The Biochemical journal, 1997, Aug-15, Volume: 326 ( Pt 1)

    Topics: Amino Acid Sequence; Animals; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen Bonding; Hydrogen Peroxide; Kinetics; Mass Spectrometry; Mutagenesis, Site-Directed; Myoglobin; Whales

1997
Pressure effects on the proximal heme pocket in myoglobin probed by Raman and near-infrared absorption spectroscopy.
    Biophysical journal, 1997, Volume: 73, Issue:5

    Topics: Animals; Carbon Monoxide; Heme; Histidine; Horses; Iron; Ligands; Myoglobin; Pressure; Protein Conformation; Spectrophotometry, Infrared; Spectrum Analysis, Raman; Temperature

1997
Molecular genetic identification of a pathway for heme binding to cytochrome b6.
    The Journal of biological chemistry, 1997, Dec-19, Volume: 272, Issue:51

    Topics: Cyclohexanecarboxylic Acids; Cytochrome b Group; Cytochrome b6f Complex; Heme; Histidine; Mutagenesis, Site-Directed; Phenotype; Protein Binding; Protein Denaturation; Pyrroles; Tetrapyrroles; Transformation, Genetic

1997
Identification of histidine 45 as the axial heme iron ligand of heme oxygenase-2.
    The Journal of biological chemistry, 1998, Feb-20, Volume: 273, Issue:8

    Topics: Electron Spin Resonance Spectroscopy; Heme; Heme Oxygenase (Decyclizing); Histidine; Humans; Ligands; Mutagenesis, Site-Directed; Recombinant Proteins

1998
Alpha-subunit oxidation in T-state crystals of a sebacyl cross-linked human hemoglobin with unusual autoxidation properties.
    Biophysical chemistry, 1998, Jan-01, Volume: 70, Issue:1

    Topics: Circular Dichroism; Cross-Linking Reagents; Crystallography, X-Ray; Decanoic Acids; Dicarboxylic Acids; Heme; Hemoglobins; Histidine; Humans; Kinetics; Models, Molecular; Oxidation-Reduction; Protein Conformation; Spectrophotometry

1998
Cytochrome c folding traps are not due solely to histidine-heme ligation: direct demonstration of a role for N-terminal amino group-heme ligation.
    Journal of molecular biology, 1998, Feb-06, Volume: 275, Issue:5

    Topics: Cytochrome c Group; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Protein Denaturation; Protein Folding

1998
Mutation of the distal arginine in Coprinus cinereus peroxidase--structural implications.
    European journal of biochemistry, 1998, Feb-01, Volume: 251, Issue:3

    Topics: Amino Acid Sequence; Amino Acid Substitution; Arginine; Binding Sites; Coprinus; Crystallography, X-Ray; Fluorides; Heme; Histidine; Iron; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Peroxidases; Protein Conformation; Recombinant Proteins; Spectrophotometry; Spectrum Analysis, Raman

1998
Localization of histidine residues responsible for heme axial ligation in cytochrome b556 of complex II (succinate:ubiquinone oxidoreductase) in Escherichia coli.
    Biochemistry, 1998, Mar-24, Volume: 37, Issue:12

    Topics: Aerobiosis; Amino Acid Sequence; Amino Acid Substitution; Chromatography, Agarose; Chromatography, High Pressure Liquid; Cytochrome b Group; Electron Transport Complex II; Escherichia coli; Heme; Histidine; Membrane Proteins; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; Oxidoreductases; Succinate Dehydrogenase

1998
Identification of histidine 105 in the beta1 subunit of soluble guanylate cyclase as the heme proximal ligand.
    Biochemistry, 1998, Mar-31, Volume: 37, Issue:13

    Topics: Alanine; Escherichia coli; Guanylate Cyclase; Heme; Histidine; Imidazoles; Ligands; Mutagenesis, Site-Directed; Solubility; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman

1998
The apolar distal histidine mutant (His69-->Val) of the homodimeric Scapharca hemoglobin is in an R-like conformation.
    Biochemistry, 1998, Apr-21, Volume: 37, Issue:16

    Topics: Amino Acid Substitution; Animals; Bivalvia; Carbon Monoxide; Circular Dichroism; Dimerization; Heme; Hemoglobins; Histidine; Ligands; Mutagenesis, Insertional; Protein Binding; Protein Conformation; Spectrophotometry; Spectrum Analysis, Raman; Valine

1998
Transmembrane heme delivery systems.
    Proceedings of the National Academy of Sciences of the United States of America, 1998, Apr-28, Volume: 95, Issue:9

    Topics: Amino Acid Sequence; ATP-Binding Cassette Transporters; Bacterial Proteins; Biological Transport; Cell Membrane; Chloroplasts; Heme; Hemeproteins; Histidine; Membrane Proteins; Molecular Sequence Data; Nuclear Proteins; Plant Proteins; Proteins; Protozoan Proteins; Recombinant Proteins; Sequence Alignment; Structure-Activity Relationship; Tryptophan

1998
Influence of proximal side mutations on the molecular and electronic structure of cyanomet myoglobin: an 1H NMR study.
    Biochemistry, 1998, May-12, Volume: 37, Issue:19

    Topics: Animals; Binding Sites; Carbon Monoxide; Energy Transfer; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Male; Metmyoglobin; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Protons; Spermatozoa; Whales

1998
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.
    Biochemistry, 1998, May-12, Volume: 37, Issue:19

    Topics: Acids; Animals; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Kinetics; Male; Mutagenesis, Site-Directed; Myoglobin; Protein Folding; Spectrophotometry; Spermatozoa; Whales

1998
The cbb3-type cytochrome c oxidase from Rhodobacter sphaeroides, a proton-pumping heme-copper oxidase.
    Biochimica et biophysica acta, 1998, Jul-20, Volume: 1365, Issue:3

    Topics: Amino Acid Sequence; Base Sequence; Cell Membrane; Cloning, Molecular; Copper; Electron Transport Complex IV; Genes, Bacterial; Genetic Complementation Test; Heme; Histidine; Molecular Sequence Data; Multigene Family; Mutation; Open Reading Frames; Oxidoreductases; Proton Pumps; Restriction Mapping; Rhodobacter sphaeroides; Sequence Analysis, DNA

1998
Prototype of a heme chaperone essential for cytochrome c maturation.
    Science (New York, N.Y.), 1998, Aug-21, Volume: 281, Issue:5380

    Topics: Amino Acid Sequence; Apoproteins; Bacterial Proteins; Binding Sites; Cytochrome c Group; Cytochromes c; Escherichia coli; Heme; Histidine; Mass Spectrometry; Membrane Proteins; Molecular Chaperones; Recombinant Fusion Proteins

1998
Functional implications of the proximal hydrogen-bonding network in myoglobin: a resonance Raman and kinetic study of Leu89, Ser92, His97, and F-helix swap mutants.
    Biochemistry, 1998, Sep-01, Volume: 37, Issue:35

    Topics: Animals; Heme; Histidine; Humans; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Leucine; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Phenylalanine; Photolysis; Propionates; Protein Structure, Secondary; Spectrum Analysis, Raman; Whales

1998
Ionic strength-dependent physicochemical factors in cytochrome c3 regulating the electron transfer rate.
    Biophysical journal, 1998, Volume: 75, Issue:3

    Topics: Biophysical Phenomena; Biophysics; Chemical Phenomena; Chemistry, Physical; Cytochrome c Group; Desulfovibrio vulgaris; Electron Transport; Heme; Histidine; Kinetics; Magnetic Resonance Spectroscopy; Osmolar Concentration; Oxidation-Reduction; Static Electricity

1998
Conversion of mitochondrial cytochrome b5 into a species capable of performing the efficient coupled oxidation of heme.
    Biochemistry, 1998, Sep-22, Volume: 37, Issue:38

    Topics: Cytochromes b5; Electrochemistry; Electron Spin Resonance Spectroscopy; Heme; Heme Oxygenase (Decyclizing); Histidine; Magnetic Resonance Spectroscopy; Mass Spectrometry; Methionine; Mitochondria; Mutagenesis, Site-Directed; NADP; Oxidation-Reduction

1998
Heme speciation in alkaline ferric FixL and possible tyrosine involvement in the signal transduction pathway for regulation of nitrogen fixation.
    Biochemistry, 1998, Sep-29, Volume: 37, Issue:39

    Topics: Bacterial Proteins; Ferric Compounds; Heme; Hemeproteins; Histidine; Histidine Kinase; Hydrogen Bonding; Hydrogen-Ion Concentration; Ligands; Nitrogen Fixation; Peptide Fragments; Phosphotransferases; Signal Transduction; Sinorhizobium meliloti; Spectrophotometry, Ultraviolet; Tyrosine

1998
Structural and functional roles of heme binding module in globin proteins: identification of the segment regulating the heme binding structure.
    Journal of molecular biology, 1998, Volume: 283, Issue:1

    Topics: Amino Acid Sequence; Binding Sites; Circular Dichroism; Escherichia coli; Globins; Heme; Histidine; Humans; Molecular Sequence Data; Myoglobin; Nuclear Magnetic Resonance, Biomolecular; Oxygen; Recombinant Fusion Proteins; Spectrum Analysis; Spectrum Analysis, Raman; Structure-Activity Relationship

1998
Mutation at histidine 338 of gp91(phox) depletes FAD and affects expression of cytochrome b558 of the human NADPH oxidase.
    The Journal of biological chemistry, 1998, Oct-23, Volume: 273, Issue:43

    Topics: Amino Acid Sequence; Binding Sites; Biological Transport; Child, Preschool; Cytochrome b Group; Cytosol; Ferredoxin-NADP Reductase; Flavin-Adenine Dinucleotide; Genetic Linkage; Granulomatous Disease, Chronic; Heme; Histidine; Humans; Male; Membrane Glycoproteins; Membrane Transport Proteins; Molecular Sequence Data; Mutation; NADPH Dehydrogenase; NADPH Oxidase 2; NADPH Oxidases; Neutrophils; Phosphoproteins; Sequence Homology, Amino Acid; Sex Chromosome Aberrations; Superoxides; X Chromosome

1998
Resonance raman characterization of the heme domain of soluble guanylate cyclase.
    Biochemistry, 1998, Nov-17, Volume: 37, Issue:46

    Topics: Animals; Carbon Monoxide; Ferrous Compounds; Glycine; Guanylate Cyclase; Heme; Histidine; Imidazoles; Lung; Nitric Oxide; Peptide Fragments; Protein Structure, Tertiary; Rats; Solubility; Spectrum Analysis, Raman

1998
Functionalized de novo designed proteins: mechanism of proton coupling to oxidation/reduction in heme protein maquettes.
    Biochemistry, 1998, Nov-24, Volume: 37, Issue:47

    Topics: Amino Acid Sequence; Amino Acid Substitution; Circular Dichroism; Electron Transport Complex III; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Molecular Sequence Data; Oxidation-Reduction; Propionates; Protein Binding; Protein Engineering; Protein Structure, Secondary; Protons; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman

1998
Characterization of soybean seed coat peroxidase: resonance Raman evidence for a structure-based classification of plant peroxidases.
    Biospectroscopy, 1998, Volume: 4, Issue:6

    Topics: Arginine; Ferric Compounds; Ferrous Compounds; Glycine max; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Molecular Structure; Peroxidases; Seeds; Sodium Fluoride; Spectrophotometry; Spectrum Analysis, Raman; Temperature

1998
Solution 1H NMR investigation of the heme cavity and substrate binding site in cyanide-inhibited horseradish peroxidase.
    Biochemistry, 1999, Jan-19, Volume: 38, Issue:3

    Topics: Benzoates; Binding Sites; Cyanides; Enzyme Inhibitors; Heme; Histidine; Horseradish Peroxidase; Hydroxamic Acids; Macromolecular Substances; Nuclear Magnetic Resonance, Biomolecular; Solutions; Substrate Specificity

1999
Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide.
    The Journal of biological chemistry, 1999, Jan-29, Volume: 274, Issue:5

    Topics: Animals; Azides; Crystallography, X-Ray; Cyanides; Ferric Compounds; Heme; Histidine; Hydrogen Peroxide; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Myoglobin; Spectrophotometry, Atomic; Whales

1999
Hydroxide rather than histidine is coordinated to the heme in five-coordinate ferric Scapharca inaequivalvis hemoglobin.
    The Journal of biological chemistry, 1999, Jan-29, Volume: 274, Issue:5

    Topics: Animals; Bivalvia; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Hydroxides; Oxidation-Reduction; Spectrum Analysis, Raman

1999
The heme environment in barley hemoglobin.
    The Journal of biological chemistry, 1999, Feb-12, Volume: 274, Issue:7

    Topics: Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Ligands; Plant Proteins; Spectrum Analysis, Raman

1999
Identification of two important heme site residues (cysteine 75 and histidine 77) in CooA, the CO-sensing transcription factor of Rhodospirillum rubrum.
    Biochemistry, 1999, Mar-02, Volume: 38, Issue:9

    Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Carbon Monoxide; Cysteine; Escherichia coli; Ferric Compounds; Ferrous Compounds; Heme; Hemeproteins; Histidine; Ligands; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Rhodospirillum rubrum; Trans-Activators

1999
EPR characterization of axial bond in metal center of native and cobalt-substituted guanylate cyclase.
    The Journal of biological chemistry, 1999, Mar-19, Volume: 274, Issue:12

    Topics: Animals; Cattle; Cobalt; Electron Spin Resonance Spectroscopy; Guanylate Cyclase; Heme; Histidine; Iron; Kinetics; Nitric Oxide; Nitrites; Nitrogen; Spectrum Analysis, Raman

1999
Replacement of the proximal histidine iron ligand by a cysteine or tyrosine converts heme oxygenase to an oxidase.
    Biochemistry, 1999, Mar-23, Volume: 38, Issue:12

    Topics: Amino Acid Substitution; Catalysis; Cysteine; Electron Transport; Ferric Compounds; Ferrous Compounds; Heme; Heme Oxygenase (Decyclizing); Histidine; Humans; Iron; Ligands; Mutagenesis; Oxidation-Reduction; Oxidoreductases; Peroxides; Spectrum Analysis, Raman; Tyrosine

1999
Molecular dynamics of human methemoglobin: the transmission of conformational information between subunits in an alpha beta dimer.
    Biophysical journal, 1999, Volume: 76, Issue:4

    Topics: Binding Sites; Biophysical Phenomena; Biophysics; Dimerization; Heme; Histidine; Humans; Hydrogen Bonding; Iron; Ligands; Methemoglobin; Models, Molecular; Protein Conformation; Protein Structure, Secondary; Static Electricity; Thermodynamics

1999
A steric mechanism for inhibition of CO binding to heme proteins.
    Science (New York, N.Y.), 1999, Apr-16, Volume: 284, Issue:5413

    Topics: Animals; Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Heme; Histidine; Hydrogen Bonding; Iron; Ligands; Metmyoglobin; Models, Molecular; Myoglobin; Nitrogen; Protein Conformation; Protein Structure, Secondary; Temperature; Valine

1999
Assignment of the heme axial ligand(s) for the ferric myoglobin (H93G) and heme oxygenase (H25A) cavity mutants as oxygen donors using magnetic circular dichroism.
    Biochemistry, 1999, Jun-08, Volume: 38, Issue:23

    Topics: Alanine; Animals; Circular Dichroism; Electron Transport; Glycine; Heme; Heme Oxygenase (Decyclizing); Histidine; Humans; Hydrogen-Ion Concentration; Iron; Ligands; Mutagenesis, Site-Directed; Myoglobin; Oxygen; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Titrimetry; Whales

1999
Substitution of the sixth axial ligand of Rhodobacter capsulatus cytochrome c1 heme yields novel cytochrome c1 variants with unusual properties.
    Biochemistry, 1999, Jun-22, Volume: 38, Issue:25

    Topics: Amino Acid Substitution; Binding Sites; Cytochromes c1; Electron Transport Complex III; Heme; Histidine; Ligands; Lysine; Methionine; Mutagenesis, Site-Directed; NADH Dehydrogenase; Oxidation-Reduction; Rhodobacter capsulatus; Spectrophotometry

1999
A study of vibrational relaxation of B-state carbon monoxide in the heme pocket of photolyzed carboxymyoglobin.
    Biophysical journal, 1999, Volume: 77, Issue:1

    Topics: Animals; Carbon Monoxide; Computer Simulation; Heme; Histidine; Myoglobin; Static Electricity; Whales

1999
Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
    Biochemistry, 1999, Jul-13, Volume: 38, Issue:28

    Topics: Arginine; Aspartic Acid; Binding Sites; Cyanides; Cytochrome-c Peroxidase; Glutamic Acid; Glycine; Heme; Histidine; Leucine; Molecular Mimicry; Nuclear Magnetic Resonance, Biomolecular; Peroxidases; Protein Engineering; Protons; Spectrophotometry; Valine

1999
Mutation of the five conserved histidines in the endothelial nitric-oxide synthase hemoprotein domain. No evidence for a non-heme metal requirement for catalysis.
    The Journal of biological chemistry, 1999, Jul-30, Volume: 274, Issue:31

    Topics: Amino Acid Substitution; Animals; Binding Sites; Calmodulin; Catalysis; Cattle; Conserved Sequence; Edetic Acid; Heme; Hemeproteins; Histidine; Humans; Iron; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Nitric Oxide Synthase; Nitric Oxide Synthase Type III; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Recombinant Proteins; Zinc

1999
UV resonance Raman studies of alpha-nitrosyl hemoglobin derivatives: relation between the alpha 1-beta 2 subunit interface interactions and the Fe-histidine bonding of alpha heme.
    Biochemistry, 1999, Jul-27, Volume: 38, Issue:30

    Topics: Carboxyhemoglobin; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Histidine; Humans; Hydrogen Bonding; Hydrogen-Ion Concentration; Iron; Models, Molecular; Phytic Acid; Protein Conformation; Spectrum Analysis, Raman; Tryptophan; Tyrosine; Ultraviolet Rays

1999
Connection between the taxonomic substates and protonation of histidines 64 and 97 in carbonmonoxy myoglobin.
    Biophysical journal, 1999, Volume: 77, Issue:2

    Topics: Animals; Binding Sites; Biophysical Phenomena; Biophysics; Heme; Histidine; Hydrogen-Ion Concentration; Models, Chemical; Myoglobin; Point Mutation; Protein Conformation; Protons; Spectroscopy, Fourier Transform Infrared; Static Electricity; Thermodynamics; Whales

1999
Iron coordination structures of oxygen sensor FixL characterized by Fe K-edge extended x-ray absorption fine structure and resonance raman spectroscopy.
    The Journal of biological chemistry, 1999, Aug-13, Volume: 274, Issue:33

    Topics: Bacterial Proteins; Fluorides; Heme; Hemeproteins; Histidine; Histidine Kinase; Imidazoles; Iron; Ligands; Oxygen; Protein Kinases; Spectrum Analysis; Spectrum Analysis, Raman; X-Rays

1999
The source of heterogeneity in the heme vicinity of ferricytochrome c.
    Biophysical chemistry, 1999, Jun-28, Volume: 79, Issue:3

    Topics: Animals; Computer Simulation; Cytochrome c Group; Drug Stability; Heme; Histidine; Horses; Magnetic Resonance Spectroscopy; Point Mutation; Protein Conformation; Rats; Recombinant Proteins; Thermodynamics

1999
Engineering cytochrome c peroxidase into cytochrome P450: a proximal effect on heme-thiolate ligation.
    Biochemistry, 1999, Aug-24, Volume: 38, Issue:34

    Topics: Aspartic Acid; Circular Dichroism; Cysteine; Cytochrome c Group; Cytochrome P-450 Enzyme System; Cytochrome-c Peroxidase; Cytochromes c; Electron Spin Resonance Spectroscopy; Escherichia coli; Ferric Compounds; Heme; Histidine; Imidazoles; Leucine; Ligands; Mutagenesis, Site-Directed; Protein Engineering; Spectrophotometry, Ultraviolet

1999
Crystal structure of human heme oxygenase-1.
    Nature structural biology, 1999, Volume: 6, Issue:9

    Topics: Binding Sites; Crystallography, X-Ray; Glycine; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Histidine; Humans; Iron; Ligands; Membrane Proteins; Models, Molecular; Molecular Sequence Data; Oxygen; Peptide Fragments; Pliability; Protein Conformation; Protein Folding; Protein Structure, Secondary; Solvents; Static Electricity; Substrate Specificity

1999
Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli.
    The Journal of biological chemistry, 1999, Sep-24, Volume: 274, Issue:39

    Topics: Amino Acid Sequence; Amino Acid Substitution; Base Sequence; Catalase; Crystallography, X-Ray; Cysteine; Escherichia coli; Genetic Variation; Glutamic Acid; Heme; Histidine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Conformation; Recombinant Proteins; Restriction Mapping

1999
Use of heme-protein complexes by the Yersinia enterocolitica HemR receptor: histidine residues are essential for receptor function.
    Journal of bacteriology, 1999, Volume: 181, Issue:19

    Topics: Amino Acid Sequence; Bacterial Outer Membrane Proteins; Bacterial Proteins; Binding Sites; Carrier Proteins; Escherichia coli Proteins; Heme; Hemeproteins; Hemoglobins; Histidine; Iron; Molecular Sequence Data; Receptors, Cell Surface; Receptors, Virus; Sequence Homology, Amino Acid; Yersinia enterocolitica

1999
Crystal structures of myoglobin-ligand complexes at near-atomic resolution.
    Biophysical journal, 1999, Volume: 77, Issue:4

    Topics: Animals; Anisotropy; Binding Sites; Carbon Monoxide; Crystallization; Crystallography, X-Ray; Electrons; Heme; Histidine; Hydrogen Bonding; Ligands; Metmyoglobin; Models, Molecular; Myoglobin; Oxygen; Protein Conformation; Protons; Water; Whales

1999
Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue.
    Proceedings of the National Academy of Sciences of the United States of America, 1999, Oct-26, Volume: 96, Issue:22

    Topics: Amino Acid Substitution; Chloride Peroxidase; Cysteine; Epoxy Compounds; Escherichia coli; Genetic Vectors; Heme; Histidine; Mutagenesis, Site-Directed

1999
Heme methyl 1H chemical shifts as structural parameters in some low-spin ferriheme proteins.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 1999, Volume: 4, Issue:4

    Topics: Animals; Cattle; Cytochrome c Group; Cytochromes b5; Heme; Histidine; Iron; Ligands; Magnetic Resonance Spectroscopy; Metalloproteins; Models, Molecular; Myoglobin; Protein Conformation

1999
Coupled oxidation of heme covalently attached to cytochrome b562 yields a novel biliprotein.
    Biochemistry, 1999, Dec-21, Volume: 38, Issue:51

    Topics: Arginine; Bacterial Proteins; Biliverdine; Cloning, Molecular; Cysteine; Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrolysis; Methionine; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Pyrroles; Tetrapyrroles

1999
Spectroscopic characterization of the heme-binding sites in Plasmodium falciparum histidine-rich protein 2.
    Biochemistry, 1999, Dec-21, Volume: 38, Issue:51

    Topics: Animals; Binding Sites; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Ferric Compounds; Ferrous Compounds; Heme; Histidine; Plasmodium falciparum; Proteins; Protozoan Proteins; Spectrophotometry; Spectrum Analysis, Raman

1999
The Rhodobacter sphaeroides ECF sigma factor, sigma(E), and the target promoters cycA P3 and rpoE P1.
    Journal of molecular biology, 1999, Nov-26, Volume: 294, Issue:2

    Topics: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Cytochrome c Group; Cytoplasm; DNA Mutational Analysis; Drug Resistance, Microbial; Gene Expression Regulation, Bacterial; Heme; Hemin; Histidine; Molecular Sequence Data; Point Mutation; Promoter Regions, Genetic; Regulatory Sequences, Nucleic Acid; Rhodobacter sphaeroides; Sigma Factor; Transcription Factors; Transcription, Genetic

1999
The N-terminal region of the heme-regulated eIF2alpha kinase is an autonomous heme binding domain.
    European journal of biochemistry, 2000, Volume: 267, Issue:2

    Topics: Amino Acid Sequence; Animals; beta-Galactosidase; Binding Sites; Circular Dichroism; eIF-2 Kinase; Heme; Histidine; Models, Molecular; Molecular Sequence Data; Mutation; Protein Conformation; Rabbits; Recombinant Fusion Proteins; Sequence Homology, Amino Acid

2000
Measuring denatured state energetics: deviations from random coil behavior and implications for the folding of iso-1-cytochrome c.
    Journal of molecular biology, 2000, Feb-11, Volume: 296, Issue:1

    Topics: Binding, Competitive; Biopolymers; Circular Dichroism; Cytochrome c Group; Cytochromes c; Enzyme Stability; Genetic Variation; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Models, Chemical; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics; Titrimetry

2000
Resonance Raman study of multihemic c-type cytochromes from Desulfuromonas acetoxidans.
    European journal of biochemistry, 2000, Volume: 267, Issue:4

    Topics: Ascorbic Acid; Circular Dichroism; Cytochrome c Group; Deltaproteobacteria; Ferric Compounds; Ferrous Compounds; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Molecular Weight; Oxidation-Reduction; Protein Conformation; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Sulfur-Reducing Bacteria; Titrimetry

2000
Cytochrome cM from synechocystis 6803. Detection in cells, expression in Escherichia coli, purification and physical characterization.
    European journal of biochemistry, 2000, Volume: 267, Issue:4

    Topics: Amino Acid Sequence; Bacterial Proteins; Blotting, Western; Cyanobacteria; Cytochrome c Group; Escherichia coli; Heme; Histidine; Isoelectric Point; Methionine; Molecular Weight; Oxidation-Reduction; Recombinant Fusion Proteins; Sequence Deletion; Solubility; Spectrum Analysis; Titrimetry

2000
Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans. Evidence from FTIR difference spectroscopy and site-directed mutagenesis.
    Biochemistry, 2000, Feb-15, Volume: 39, Issue:6

    Topics: Amino Acid Substitution; Arginine; Electron Transport Complex IV; Heme; Histidine; Hydrogen Bonding; Mutagenesis, Site-Directed; Oxidation-Reduction; Paracoccus denitrificans; Propionates; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Tryptophan; Tyrosine

2000
Investigations of the myoglobin cavity mutant H93G with unnatural imidazole proximal ligands as a modular peroxide O-O bond cleavage model system.
    Biochemistry, 2000, Feb-15, Volume: 39, Issue:6

    Topics: Animals; Glycine; Heme; Histidine; Hydrogen Peroxide; Hydrogen-Ion Concentration; Hydrolysis; Imidazoles; Iron; Ligands; Models, Chemical; Mutagenesis, Site-Directed; Myoglobin; Oxygen; Sodium Nitrite; Whales

2000
Engineering His(E7) affects the control of heme reactivity in Aplysia limacina myoglobin.
    Biochemical and biophysical research communications, 2000, Mar-05, Volume: 269, Issue:1

    Topics: Animals; Aplysia; Azides; Binding Sites; Crystallography, X-Ray; Heme; Histidine; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Protein Binding; Protein Conformation; Protein Engineering; Static Electricity; Whales

2000
Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a.
    Biochemistry, 2000, Mar-21, Volume: 39, Issue:11

    Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Cattle; Electron Transport Complex IV; Enzyme Activation; Glutamine; Heme; Histidine; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Proton Pumps; Rhodobacter sphaeroides; Spectrum Analysis, Raman; Tyrosine

2000
Proximal and distal effects on the coordination chemistry of ferric Scapharca homodimeric hemoglobin as revealed by heme pocket mutants.
    Biochemistry, 2000, Mar-28, Volume: 39, Issue:12

    Topics: Amino Acid Substitution; Animals; Bivalvia; Dimerization; Ferric Compounds; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Leucine; Phenylalanine; Point Mutation; Spectrophotometry; Spectrum Analysis, Raman; Ultracentrifugation; Valine

2000
Proton electron nuclear double resonance from nitrosyl horse heart myoglobin: the role of His-E7 and Val-E11.
    Biophysical journal, 2000, Volume: 78, Issue:4

    Topics: Animals; Biophysical Phenomena; Biophysics; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Models, Molecular; Myocardium; Myoglobin; Protein Conformation; Protons; Valine

2000
Histidine 20, the crucial proximal axial heme ligand of bacterial heme oxygenase Hmu O from Corynebacterium diphtheriae.
    The Journal of biological chemistry, 2000, Jun-09, Volume: 275, Issue:23

    Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Ascorbic Acid; Bacterial Proteins; Base Sequence; Corynebacterium diphtheriae; Electron Spin Resonance Spectroscopy; Heme; Heme Oxygenase (Decyclizing); Histidine; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Spectrophotometry; Spectrum Analysis, Raman

2000
Cytochrome cd(1) from Paracoccus pantotrophus exhibits kinetically gated, conformationally dependent, highly cooperative two-electron redox behavior.
    Biochemistry, 2000, Apr-18, Volume: 39, Issue:15

    Topics: Allosteric Regulation; Allosteric Site; Apoenzymes; Cytochrome c Group; Cytochromes; Dimerization; Electrons; Heme; Histidine; Holoenzymes; Kinetics; Ligands; Methionine; Nitrite Reductases; Oxidation-Reduction; Paracoccus; Protein Conformation; Spectrum Analysis; Temperature; Titrimetry

2000
Identification of the proximal ligand His-20 in heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Oxidative cleavage of the heme macrocycle does not require the proximal histidine.
    The Journal of biological chemistry, 2000, Apr-21, Volume: 275, Issue:16

    Topics: Bacterial Proteins; Biliverdine; Carbon Monoxide; Catalytic Domain; Chromatography, High Pressure Liquid; Corynebacterium diphtheriae; Electrophoresis, Polyacrylamide Gel; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Histidine; Humans; Hydroxylation; Ligands; Membrane Proteins; Models, Chemical; Mutagenesis, Site-Directed; Oxidation-Reduction; Spectrophotometry, Atomic; Spectrum Analysis, Raman; Structure-Activity Relationship

2000
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization.
    Journal of molecular biology, 2000, May-19, Volume: 298, Issue:5

    Topics: Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cytochrome c Group; Cytochromes c; Enzyme Stability; Fluorescence; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Proline; Protein Conformation; Protein Denaturation; Protein Folding; Protein Renaturation; Saccharomyces cerevisiae; Sequence Alignment; Thermodynamics

2000
Formation of two types of low-spin heme in horseradish peroxidase isoenzyme A2 at low temperature.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2000, Volume: 5, Issue:2

    Topics: Arginine; Cold Temperature; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horseradish Peroxidase; Hydrogen Bonding; Hydrogen-Ion Concentration; Isoenzymes; Protein Conformation; Spectrophotometry, Infrared

2000
Substitution of tyrosine for the proximal histidine ligand to the heme of prostaglandin endoperoxide synthase 2: implications for the mechanism of cyclooxygenase activation and catalysis.
    Biochemistry, 2000, May-09, Volume: 39, Issue:18

    Topics: Animals; Arachidonic Acid; Binding Sites; Cyclooxygenase 2; Electron Transport; Enzyme Activation; Heme; Histidine; Iron; Isoenzymes; Kinetics; Mutation; Oxidation-Reduction; Oxygen Consumption; Peroxidases; Peroxides; Prostaglandin H2; Prostaglandin-Endoperoxide Synthases; Prostaglandins H; Spectrophotometry; Tyrosine

2000
Functions of fluctuation in the heme-binding loops of cytochrome b5 revealed in the process of heme incorporation.
    Biochemistry, 2000, May-23, Volume: 39, Issue:20

    Topics: Animals; Carrier Proteins; Circular Dichroism; Cytochromes b5; Heme; Heme-Binding Proteins; Hemeproteins; Histidine; Kinetics; Leucine; Models, Chemical; Mutagenesis, Site-Directed; Protein Binding; Protein Folding; Protein Structure, Secondary; Rats; Spectrophotometry, Ultraviolet; Spectrum Analysis; Structure-Activity Relationship

2000
Peroxidase activity in prostaglandin endoperoxide H synthase-1 occurs with a neutral histidine proximal heme ligand.
    Biochemistry, 2000, Jun-06, Volume: 39, Issue:22

    Topics: Animals; Crystallography, X-Ray; Cyclooxygenase 1; Heme; Histidine; Hydrogen Bonding; Iron; Isoenzymes; Models, Molecular; Mutagenesis, Site-Directed; Peroxidases; Prostaglandin-Endoperoxide Synthases; Sheep; Spectrophotometry; Spectrum Analysis, Raman; Water

2000
The hydrogenase cytochrome b heme ligands of Azotobacter vinelandii are required for full H(2) oxidation capability.
    Journal of bacteriology, 2000, Volume: 182, Issue:12

    Topics: Amino Acid Sequence; Amino Acid Substitution; Azotobacter vinelandii; Cytochrome b Group; Dimerization; Heme; Histidine; Hydrogen; Hydrogenase; Imidazoles; Ligands; Methylene Blue; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Plasmids

2000
Identification and characterization of a novel cytochrome c(3) from Shewanella frigidimarina that is involved in Fe(III) respiration.
    The Biochemical journal, 2000, Jul-01, Volume: 349, Issue:Pt 1

    Topics: Amino Acid Sequence; Base Sequence; Cytochrome c Group; Cytochromes; DNA Primers; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Ions; Iron; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Plasmids; Polymerase Chain Reaction; Protein Structure, Tertiary; Respiration; Sequence Homology, Amino Acid; Shewanella; Spectrophotometry; Succinate Dehydrogenase; Time Factors

2000
Structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC6803 reveal a unique distal heme pocket.
    European journal of biochemistry, 2000, Volume: 267, Issue:15

    Topics: Amino Acid Sequence; Cloning, Molecular; Cyanobacteria; Heme; Hemoglobins; Histidine; Iron; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitrogen; Oxygen; Plasmids; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrophotometry; Spectrum Analysis, Raman

2000
Obtaining ligand geometries from paramagnetic shifts in low-spin haem proteins.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2000, Volume: 5, Issue:3

    Topics: Cyanides; Heme; Hemeproteins; Histidine; Ligands; Methionine; Models, Theoretical; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation

2000
Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin.
    Biophysical journal, 2000, Volume: 79, Issue:2

    Topics: Binding Sites; Carboxyhemoglobin; Cloning, Molecular; Escherichia coli; Genes, Synthetic; Heme; Hemoglobins; Histidine; Humans; Isotope Labeling; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Recombinant Proteins

2000
Spectroscopic comparison of the heme active sites in WT KatG and its S315T mutant.
    Biochemistry, 2000, Aug-15, Volume: 39, Issue:32

    Topics: Bacterial Proteins; Binding Sites; Electron Spin Resonance Spectroscopy; Ferric Compounds; Ferrous Compounds; Heme; Hemeproteins; Histidine; Ligands; Mutation; Mycobacterium tuberculosis; Peroxidases; Recombinant Proteins; Serine; Spectrum Analysis, Raman; Threonine

2000
Mapping the pathways for O2 entry into and exit from myoglobin.
    The Journal of biological chemistry, 2001, Feb-16, Volume: 276, Issue:7

    Topics: Animals; Binding Sites; Heme; Histidine; Kinetics; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Oxygen; Protein Binding; Water; Whales

2001
Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy.
    Biochemistry, 2000, Oct-24, Volume: 39, Issue:42

    Topics: Bacterial Proteins; Carbon Monoxide; Escherichia coli; Escherichia coli Proteins; Fimbriae Proteins; Heme; Histidine; Imidazoles; Iron; Ligands; Mutagenesis, Site-Directed; Myoglobin; Photolysis; Spectrum Analysis, Raman; Tyrosine

2000
Proximal ligand control of heme iron coordination structure and reactivity with hydrogen peroxide: investigations of the myoglobin cavity mutant H93G with unnatural oxygen donor proximal ligands.
    Journal of inorganic biochemistry, 2000, Aug-31, Volume: 81, Issue:3

    Topics: Animals; Benzoates; Binding Sites; Escherichia coli; Heme; Histidine; Hydrogen Peroxide; Hydrogen-Ion Concentration; Iron; Ligands; Models, Molecular; Mutation; Myoglobin; Oxygen; Phenol; Protein Binding; Protein Conformation; Spectrophotometry; Time Factors; Tyrosine; Ultraviolet Rays; Whales

2000
Heme structure of hemoglobin M Iwate [alpha 87(F8)His-->Tyr]: a UV and visible resonance Raman study.
    Biochemistry, 2000, Oct-31, Volume: 39, Issue:43

    Topics: Amino Acid Substitution; Dithionite; Heme; Hemoglobin A; Hemoglobin M; Hemoglobins; Histidine; Humans; Methemoglobin; Oxidation-Reduction; Peptide Fragments; Reducing Agents; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Tyrosine

2000
pH dependence of formation of a partially unfolded state of a Lys 73 --> His variant of iso-1-cytochrome c: implications for the alkaline conformational transition of cytochrome c.
    Biochemistry, 2000, Nov-07, Volume: 39, Issue:44

    Topics: Amino Acid Substitution; Cytochrome c Group; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Lysine; Models, Chemical; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Folding; Saccharomyces cerevisiae; Titrimetry

2000
Roles of Ile209 and Ile210 on the heme pocket structure and regulation of histidine kinase activity of oxygen sensor FixL from Rhizobium meliloti.
    Biochemistry, 2000, Nov-14, Volume: 39, Issue:45

    Topics: Bacterial Proteins; Carbon Monoxide; Enzyme Activation; Ferric Compounds; Heme; Hemeproteins; Histidine; Histidine Kinase; Isoleucine; Mutagenesis, Site-Directed; Oxygen; Phosphorylation; Protein Binding; Protein Conformation; Protein Kinases; Sinorhizobium meliloti; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Tryptophan

2000
Changing the heme ligation in flavocytochrome b2: substitution of histidine-66 by cysteine.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2000, Volume: 5, Issue:5

    Topics: Amino Acid Substitution; Circular Dichroism; Cysteine; Electron Spin Resonance Spectroscopy; Flavin Mononucleotide; Heme; Histidine; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Mutation; Oxidation-Reduction; Protein Binding; Saccharomyces cerevisiae; Spectrophotometry; Spectrum Analysis, Raman

2000
Redox properties and coordination structure of the heme in the co-sensing transcriptional activator CooA.
    The Journal of biological chemistry, 2001, Mar-09, Volume: 276, Issue:10

    Topics: Alanine; Bacterial Proteins; Cysteine; Electrochemistry; Escherichia coli Proteins; Fimbriae Proteins; Heme; Histidine; Iron; Ligands; Models, Chemical; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxygen; Spectrum Analysis, Raman; Transcriptional Activation

2001
Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structure.
    Biochemistry, 2001, Feb-06, Volume: 40, Issue:5

    Topics: Amino Acid Substitution; Binding Sites; Computer Simulation; Crystallography, X-Ray; Cytochrome-c Peroxidase; Escherichia coli; Glycine; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Ligands; Models, Molecular; Phosphates; Protein Binding; Protein Conformation; Structure-Activity Relationship; Temperature

2001
Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 2. Effects on heme coordination and function.
    Biochemistry, 2001, Feb-06, Volume: 40, Issue:5

    Topics: Amino Acid Substitution; Binding Sites; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Escherichia coli; Ferrous Compounds; Free Radicals; Glycine; Heme; Histidine; Imidazoles; Ligands; Nitric Oxide; Protein Binding; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman

2001
NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: identification of the haem-specific axial ligands and order of oxidation.
    FEBS letters, 2001, Jan-26, Volume: 489, Issue:1

    Topics: Amino Acid Sequence; Cytochrome c Group; Heme; Histidine; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Sequence Homology, Amino Acid; Shewanella; Thermodynamics

2001
Structural and dynamic perturbations induced by heme binding in cytochrome b5.
    Biochemistry, 2001, Apr-17, Volume: 40, Issue:15

    Topics: Alanine; Amino Acid Substitution; Animals; Apoproteins; Carbon Monoxide; Crystallography, X-Ray; Cytochrome b Group; Cytochromes b; Cytochromes b5; Heme; Histidine; Macromolecular Substances; Methylamines; Nuclear Magnetic Resonance, Biomolecular; Oxidants; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Rats; Thermodynamics

2001
Interaction of apo-cytochrome b5 with cytochromes P4503A4 and P45017A: relevance of heme transfer reactions.
    Biochemistry, 2001, Apr-24, Volume: 40, Issue:16

    Topics: Alanine; Animals; Apoproteins; Aryl Hydrocarbon Hydroxylases; Catalysis; Chromatography, Affinity; Cytochrome b Group; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme System; Cytochromes b; Electron Transport; Enzymes, Immobilized; Heme; Histidine; Holoenzymes; Horses; Humans; Kinetics; Mixed Function Oxygenases; Molecular Weight; Mutagenesis, Site-Directed; Myoglobin; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Rats; Recombinant Proteins; Spectrophotometry; Steroid 17-alpha-Hydroxylase; Steroid Hydroxylases

2001
A photolysis-triggered heme ligand switch in H93G myoglobin.
    Biochemistry, 2001, May-01, Volume: 40, Issue:17

    Topics: Animals; Carbon Monoxide; Ferrous Compounds; Glycine; Heme; Histidine; Iron; Lasers; Ligands; Metmyoglobin; Mutagenesis, Insertional; Myoglobin; Photolysis; Protein Binding; Spectrum Analysis, Raman; Thermodynamics; Whales

2001
Solution structure of Methylophilus methylotrophus cytochrome c": insights into the structural basis of haem-ligand detachment.
    Journal of molecular biology, 2001, Apr-27, Volume: 308, Issue:2

    Topics: Amino Acid Sequence; Binding Sites; Cysteine; Cytochrome c Group; Disulfides; Heme; Histidine; Ligands; Methylophilus methylotrophus; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation

2001
Water penetration and binding to ferric myoglobin.
    Biochemistry, 2001, May-15, Volume: 40, Issue:19

    Topics: Amino Acid Substitution; Animals; Binding Sites; Heme; Histidine; Horses; Hydrogen Bonding; Kinetics; Leucine; Ligands; Metmyoglobin; Models, Chemical; Nitric Oxide; Water

2001
Binding of ferric heme by the recombinant globin from the cyanobacterium Synechocystis sp. PCC 6803.
    Biochemistry, 2001, May-29, Volume: 40, Issue:21

    Topics: Amino Acid Sequence; Cyanobacteria; Ferric Compounds; Globins; Heme; Histidine; Iron; Kinetics; Ligands; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Conformation; Protons; Recombinant Proteins; Thermodynamics; Truncated Hemoglobins

2001
High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2001, Volume: 6, Issue:4

    Topics: Amino Acid Motifs; Amino Acid Sequence; Crystallography, X-Ray; Cytochrome c Group; Heme; Histidine; Models, Molecular; Molecular Sequence Data; Nitrosomonas; Oxidation-Reduction; Phenylalanine; Protein Conformation; Protein Folding

2001
Heme histidine ligands within gp91(phox) modulate proton conduction by the phagocyte NADPH oxidase.
    The Journal of biological chemistry, 2001, Aug-10, Volume: 276, Issue:32

    Topics: Animals; Blotting, Western; Cell Line; COS Cells; Electrons; Heme; Histidine; Humans; Hydrogen; Hydrogen-Ion Concentration; Ions; Kinetics; Ligands; Membrane Glycoproteins; Microscopy, Fluorescence; Models, Biological; Mutagenesis, Site-Directed; NADPH Oxidase 2; NADPH Oxidases; Patch-Clamp Techniques; Phagocytes; Phagocytosis; Protein Binding; Protons; Spectrophotometry; Time Factors; Transfection; Zinc

2001
Site-directed mutagenesis of the heme axial ligands in the hemoflavoenzyme cellobiose dehydrogenase.
    Archives of biochemistry and biophysics, 2001, Jun-15, Volume: 390, Issue:2

    Topics: Amino Acid Substitution; Carbohydrate Dehydrogenases; Catalysis; Cellulose; Heme; Histidine; Ligands; Methionine; Molecular Weight; Mutagenesis, Site-Directed; Phanerochaete

2001
Heme-ligating histidines in flavocytochrome b(558): identification of specific histidines in gp91(phox).
    The Journal of biological chemistry, 2001, Aug-17, Volume: 276, Issue:33

    Topics: Amino Acid Sequence; Animals; COS Cells; Cytochrome b Group; Dimerization; Heme; Histidine; Humans; Membrane Glycoproteins; Molecular Sequence Data; NADPH Oxidase 2; NADPH Oxidases; Structure-Activity Relationship

2001
Influence of the heme pocket conformation on the structure and vibrations of the Fe-CO bond in myoglobin: a QM/MM density functional study.
    Biophysical journal, 2001, Volume: 81, Issue:1

    Topics: Carbon Monoxide; Computer Simulation; Heme; Histidine; Iron; Ligands; Models, Molecular; Myoglobin; Protein Conformation; Thermodynamics; Vibration

2001
Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique.
    Journal of the American Chemical Society, 2001, Jul-11, Volume: 123, Issue:27

    Topics: Animals; Bacterial Proteins; Cytochrome c Group; Guanidine; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Protein Folding

2001
Analysis of the principal g-tensors in single crystals of ferrimyoglobin complexes.
    Biochimica et biophysica acta, 1971, Nov-19, Volume: 251, Issue:2

    Topics: Animals; Electron Spin Resonance Spectroscopy; Heme; Histidine; Imidazoles; Metmyoglobin; Models, Molecular; Muscle, Skeletal; Potassium Cyanide; Sodium Azide; Thiocyanates; Whales

1971
Structure--function relationships of rat hepatic tryptophan 2,3-dioxygenase: identification of the putative heme-ligating histidine residues.
    Archives of biochemistry and biophysics, 2001, Aug-01, Volume: 392, Issue:1

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Base Sequence; Binding Sites; Cytosol; DNA Primers; Evolution, Molecular; Heme; Histidine; Humans; Ligands; Liver; Molecular Sequence Data; Mutagenesis, Site-Directed; Rats; Sequence Homology, Amino Acid; Structure-Activity Relationship; Tryptophan Oxygenase

2001
The peroxidase activity of cytochrome c-550 from Paracoccus versutus.
    European journal of biochemistry, 2001, Volume: 268, Issue:15

    Topics: Amino Acids; Catalysis; Cytochrome c Group; Dose-Response Relationship, Drug; Enzyme Activation; Guaiacol; Heme; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Oxidation-Reduction; Paracoccus; Peroxidase; Protein Binding; Superoxide Dismutase; Superoxides; Time Factors

2001
Inhibition of the neutrophil NADPH oxidase and associated H+ channel by diethyl pyrocarbonate (DEPC), a histidine-modifying agent: evidence for at least two target sites.
    The Biochemical journal, 2001, Sep-01, Volume: 358, Issue:Pt 2

    Topics: Cytochrome b Group; Diethyl Pyrocarbonate; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Indicators and Reagents; Ion Channels; Ion Transport; NADPH Oxidases; Neutrophils; Oxidation-Reduction; Protons; Subcellular Fractions; Superoxides; Tetrazolium Salts

2001
Hydrophobic modulation of heme properties in heme protein maquettes.
    Biochemistry, 2001, Sep-04, Volume: 40, Issue:35

    Topics: Amino Acid Sequence; Circular Dichroism; Heme; Hemeproteins; Histidine; Molecular Sequence Data; Molecular Weight; Protein Conformation; Spectrophotometry, Ultraviolet; Thermodynamics; Water

2001
Denatured state thermodynamics: residual structure, chain stiffness and scaling factors.
    Journal of molecular biology, 2001, Aug-31, Volume: 311, Issue:5

    Topics: Acetylation; Circular Dichroism; Cytochrome c Group; Cytochromes c; Enzyme Stability; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Mutation; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae Proteins; Serine Endopeptidases; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Thermodynamics; Titrimetry; Yeasts

2001
Factors determining the special redox properties of photosynthetic cytochrome b559.
    European journal of biochemistry, 2001, Volume: 268, Issue:18

    Topics: Cytochrome b Group; Heme; Histidine; Hydrogen-Ion Concentration; Intracellular Membranes; Ligands; Oxidation-Reduction; Phosphorylcholine; Photosynthetic Reaction Center Complex Proteins; Photosystem II Protein Complex; Pisum sativum; Protons; Spinacia oleracea

2001
Domain swing upon His to Ala mutation in nitrite reductase of Pseudomonas aeruginosa.
    Journal of molecular biology, 2001, Sep-21, Volume: 312, Issue:3

    Topics: Alanine; Amino Acid Substitution; Binding Sites; Crystallization; Crystallography, X-Ray; Dimerization; Heme; Histidine; Models, Molecular; Mutation; Nitric Oxide; Nitrite Reductases; Pliability; Protein Structure, Quaternary; Protein Structure, Tertiary; Pseudomonas aeruginosa; Spectrophotometry; Static Electricity

2001
Covalent linkage of prosthetic heme to CYP4 family P450 enzymes.
    Biochemistry, 2001, Oct-30, Volume: 40, Issue:43

    Topics: Amino Acid Sequence; Animals; Aryl Hydrocarbon Hydroxylases; Baculoviridae; Benzidines; Binding Sites; Catalytic Domain; Chromatography; Chromatography, High Pressure Liquid; Cytochrome P-450 CYP4A; Cytochrome P-450 Enzyme System; Cytochrome P450 Family 4; Electrophoresis, Polyacrylamide Gel; Gas Chromatography-Mass Spectrometry; Heme; Histidine; Humans; Hydrogen Bonding; Hydrogen Peroxide; Mixed Function Oxygenases; Molecular Sequence Data; Protein Binding; Protein Isoforms; Rabbits; Sequence Homology, Amino Acid; Spectrophotometry; Ultraviolet Rays

2001
Factors that determine the unusually low reduction potential of cytochrome c550 in cyanobacterial photosystem II.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2001, Volume: 6, Issue:7

    Topics: Cyanobacteria; Cytochrome c Group; Electrochemistry; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Heme; Histidine; Oxidation-Reduction; Photosynthetic Reaction Center Complex Proteins; Photosystem II Protein Complex; Recombinant Proteins; Spectrum Analysis, Raman

2001
A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c.
    The Journal of biological chemistry, 2002, Mar-08, Volume: 277, Issue:10

    Topics: Amino Acid Motifs; Amino Acid Sequence; Apoproteins; Bacterial Outer Membrane Proteins; Cytochrome c Group; Cytochromes c; DNA Primers; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Lyases; Models, Biological; Molecular Sequence Data; Mutation; Periplasm; Plasmids; Point Mutation; Precipitin Tests; Protein Binding; Protein Structure, Tertiary; Protein Transport; Tryptophan

2002
Site-directed mutagenesis reveals the essentiality of the conserved residues in the putative diiron active site of the trypanosome alternative oxidase.
    The Journal of biological chemistry, 2002, Mar-08, Volume: 277, Issue:10

    Topics: Amino Acid Motifs; Animals; Binding Sites; Cell Division; Escherichia coli; Genetic Complementation Test; Glutamine; Heme; Histidine; Immunoblotting; Iron; Models, Genetic; Mutagenesis, Site-Directed; Mutation; Oxidoreductases; Plasmids; Protein Binding; Protein Structure, Tertiary; Trypanosoma brucei brucei

2002
Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferrocytochrome C.
    Biochemistry, 2002, Jan-29, Volume: 41, Issue:4

    Topics: Animals; Cytochrome c Group; Fishes; Heme; Histidine; Horses; Kinetics; Protein Binding; Protein Denaturation; Spectrum Analysis

2002
The role of the cross-link His-Tyr in the functional properties of the binuclear center in cytochrome c oxidase.
    The Journal of biological chemistry, 2002, Apr-19, Volume: 277, Issue:16

    Topics: Binding Sites; Carbon Dioxide; Catalysis; Catalytic Domain; Electron Transport Complex IV; Heme; Histidine; Ligands; Mutation; Oxygen; Paracoccus denitrificans; Spectrum Analysis, Raman; Tyrosine

2002
Mutants of the CuA site in cytochrome c oxidase of Rhodobacter sphaeroides: I. Spectral and functional properties.
    Biochemistry, 2002, Feb-19, Volume: 41, Issue:7

    Topics: Amino Acid Substitution; Asparagine; Cell Membrane; Copper; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Glycine; Heme; Histidine; Iron; Kinetics; Leucine; Manganese; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Structure, Secondary; Proton Pumps; Rhodobacter sphaeroides; Spectrometry, Fluorescence; Spectrophotometry; Spectroscopy, Fourier Transform Infrared

2002
Studies of the reduction and protonation behavior of tetraheme cytochromes using atomic detail.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2002, Volume: 7, Issue:1-2

    Topics: Computer Simulation; Cytochrome c Group; Electrons; Enzyme Stability; Heme; Histidine; Models, Molecular; Monte Carlo Method; Oxidation-Reduction; Propionates; Proteobacteria; Protons; Static Electricity; Thermodynamics

2002
Histidine pK(a) shifts and changes of tautomeric states induced by the binding of gallium-protoporphyrin IX in the hemophore HasA(SM).
    Protein science : a publication of the Protein Society, 2002, Volume: 11, Issue:4

    Topics: Bacterial Proteins; Binding Sites; Carrier Proteins; Crystallography, X-Ray; Escherichia coli; Gallium; Heme; Histidine; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Membrane Proteins; Models, Molecular; Protein Binding; Protein Conformation; Protoporphyrins

2002
Crystal structures of deoxy- and carbonmonoxyhemoglobin F1 from the hagfish Eptatretus burgeri.
    The Journal of biological chemistry, 2002, Jun-14, Volume: 277, Issue:24

    Topics: Amino Acid Sequence; Animals; Carboxyhemoglobin; Crystallography, X-Ray; Dimerization; DNA, Complementary; Electrons; Genetic Linkage; Hagfishes; Heme; Hemoglobins; Histidine; Humans; Ligands; Models, Molecular; Models, Statistical; Molecular Sequence Data; Oxygen; Protein Binding

2002
Chemical shift-based constraints for solution structure determination of paramagnetic low-spin heme proteins with bis-His and His-CN axial ligands: the cases of oxidized cytochrome b(5) and Met80Ala cyano-cytochrome c.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2002, Volume: 7, Issue:4-5

    Topics: Alanine; Cyanides; Cytochrome c Group; Cytochromes b5; Heme; Histidine; Ligands; Methionine; Models, Molecular; Molecular Structure; Mutation; Oxidation-Reduction; Yeasts

2002
Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein.
    Biochemistry, 2002, Jun-04, Volume: 41, Issue:22

    Topics: Amino Acid Sequence; Cloning, Molecular; Cyanobacteria; Escherichia coli; Hemoglobins; Histidine; Inclusion Bodies; Magnetic Resonance Spectroscopy; Mass Spectrometry; Molecular Sequence Data; Protoporphyrins; Recombinant Proteins; Truncated Hemoglobins

2002
The carbon monoxide derivative of human hemoglobin carrying the double mutation LeuB10-->Tyr and HisE7-->Gln on alpha and beta chains probed by infrared spectroscopy.
    Archives of biochemistry and biophysics, 2002, Jun-01, Volume: 402, Issue:1

    Topics: Amino Acid Substitution; Carbon Monoxide; Carboxyhemoglobin; Glutamine; Heme; Hemoglobin A; Histidine; Humans; Hydrogen Bonding; Iron; Kinetics; Leucine; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship; Tyrosine

2002
Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli.
    The Journal of biological chemistry, 2002, Sep-06, Volume: 277, Issue:36

    Topics: Carbon Monoxide; Carrier Proteins; Cloning, Molecular; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Methionine; Mutation; Oxygen; Phosphoric Diester Hydrolases; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Spectrum Analysis, Raman; Time Factors

2002
Novel histidine-heme covalent linkage in a hemoglobin.
    Journal of the American Chemical Society, 2002, Jul-24, Volume: 124, Issue:29

    Topics: Apoproteins; Cyanobacteria; Heme; Hemoglobins; Histidine; Mass Spectrometry; Nuclear Magnetic Resonance, Biomolecular; Recombinant Proteins

2002
Identification of two domains and distal histidine ligands to the four haems in the bacterial c-type cytochrome NapC; the prototype connector between quinol/quinone and periplasmic oxido-reductases.
    The Biochemical journal, 2002, Dec-01, Volume: 368, Issue:Pt 2

    Topics: Amino Acid Sequence; Bacterial Proteins; Benzoquinones; Binding Sites; Cytochrome c Group; Escherichia coli; Genetic Complementation Test; Heme; Histidine; Hydroquinones; Iron; Ligands; Molecular Sequence Data; Mutagenesis; Nitrate Reductase; Nitrate Reductases; Oxidoreductases; Paracoccus; Periplasm; Periplasmic Proteins; Protein Structure, Tertiary; Sequence Homology, Amino Acid

2002
Crystal structures of unligated and CN-ligated Glycera dibranchiata monomer ferric hemoglobin components III and IV.
    Proteins, 2002, Oct-01, Volume: 49, Issue:1

    Topics: Amino Acid Sequence; Animals; Crystallography, X-Ray; Cyanides; Heme; Hemoglobins; Histidine; Kinetics; Ligands; Methemoglobin; Models, Molecular; Molecular Sequence Data; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Polychaeta; Protein Binding; Sequence Homology, Amino Acid; Temperature

2002
Influence of the distal his in imparting imidazolate character to the proximal his in heme peroxidase: (1)h NMR spectroscopic study of cyanide-inhibited his42-->ala horseradish peroxidase.
    Journal of the American Chemical Society, 2002, Sep-18, Volume: 124, Issue:37

    Topics: Alanine; Cyanides; Enzyme Inhibitors; Heme; Histidine; Horseradish Peroxidase; Hydrogen Bonding; Imidazoles; Nuclear Magnetic Resonance, Biomolecular; Peroxidases; Protein Conformation

2002
Probing the role of active site histidine residues in the catalytic activity of lacrimal gland peroxidase.
    Molecular and cellular biochemistry, 2002, Volume: 237, Issue:1-2

    Topics: Animals; Binding Sites; Catalysis; Circular Dichroism; Diethyl Pyrocarbonate; Dose-Response Relationship, Drug; Heme; Histidine; Hydrogen-Ion Concentration; Hydroxylamine; Kinetics; Lacrimal Apparatus; Models, Chemical; Peroxidase; Protein Binding; Protein Structure, Secondary; Sheep; Substrate Specificity; Temperature; Time Factors; Ultraviolet Rays

2002
Ligand binding properties and structural studies of recombinant and chemically modified hemoglobins altered at beta 93 cysteine.
    Biochemistry, 2002, Oct-01, Volume: 41, Issue:39

    Topics: 2,3-Diphosphoglycerate; Allosteric Regulation; Amino Acid Substitution; Cysteine; Globins; Heme; Hemoglobin A; Hemoglobins; Histidine; Humans; Ligands; Methemoglobin; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Oxygen; Phytic Acid; Protein Subunits; Recombinant Proteins; Structure-Activity Relationship; Thermodynamics

2002
Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein.
    The Journal of biological chemistry, 2003, Jan-24, Volume: 278, Issue:4

    Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Biological Transport; Chlamydomonas; Chloroplasts; Conserved Sequence; Cytochrome c Group; Electrophoresis, Polyacrylamide Gel; Heme; Histidine; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nuclear Proteins; Phenotype; Protozoan Proteins; Recombinant Fusion Proteins; Time Factors; Tryptophan

2003
NMR structure of the heme chaperone CcmE reveals a novel functional motif.
    Structure (London, England : 1993), 2002, Volume: 10, Issue:11

    Topics: Amino Acid Motifs; Amino Acid Sequence; Bacterial Outer Membrane Proteins; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Magnetic Resonance Spectroscopy; Models, Biological; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrophotometry

2002
NO-induced activation mechanism of the heme-regulated eIF2alpha kinase.
    Journal of the American Chemical Society, 2002, Nov-20, Volume: 124, Issue:46

    Topics: Carbon Monoxide; eIF-2 Kinase; Electron Spin Resonance Spectroscopy; Enzyme Activation; Heme; Histidine; Nitric Oxide; Protein Conformation; Protein Structure, Tertiary; Spectrum Analysis, Raman

2002
Oxidation of heme to beta- and delta-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme.
    Journal of the American Chemical Society, 2002, Dec-18, Volume: 124, Issue:50

    Topics: Biliverdine; Catalysis; Heme; Heme Oxygenase (Decyclizing); Histidine; Isomerism; Models, Molecular; Mutagenesis; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Polymerase Chain Reaction; Protein Conformation; Pseudomonas aeruginosa; Spectrum Analysis, Raman

2002
Distal heme pocket regulation of ligand binding and stability in soybean leghemoglobin.
    Proteins, 2003, Feb-01, Volume: 50, Issue:2

    Topics: Amino Acids; Animals; Binding Sites; Carbon Monoxide; Cyanides; Glycine max; Heme; Histidine; Leghemoglobin; Ligands; Models, Molecular; Mutation; Myoglobin; Oxygen; Protein Conformation; Soybean Proteins; Thermodynamics; Water; Whales

2003
Assignment of heme resonances and determination of the electronic structures of high- and low-spin nitrophorin 2 by 1H and 13C NMR spectroscopy: an explanation of the order of heme methyl resonances in high-spin ferriheme proteins.
    Biochemistry, 2003, Jan-28, Volume: 42, Issue:3

    Topics: Animals; Carbon Isotopes; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Hemin; Histidine; Imidazoles; Insect Proteins; Ligands; Macromolecular Substances; Nuclear Magnetic Resonance, Biomolecular; Protons; Recombinant Proteins; Rhodnius; Salivary Proteins and Peptides; Thermodynamics

2003
Expression and characterization of cyanobacterium heme oxygenase, a key enzyme in the phycobilin synthesis. Properties of the heme complex of recombinant active enzyme.
    European journal of biochemistry, 2003, Volume: 270, Issue:4

    Topics: Amino Acid Sequence; Animals; Ascorbic Acid; Biliverdine; Catalysis; Cyanobacteria; Electron Spin Resonance Spectroscopy; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Hemin; Histidine; Molecular Sequence Data; NADPH-Ferrihemoprotein Reductase; Phycobilins; Phycocyanin; Pyrroles; Rats; Sequence Homology, Amino Acid; Tetrapyrroles

2003
1H NMR structure of the heme pocket of HNO-myoglobin.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2003, Volume: 8, Issue:3

    Topics: Animals; Binding Sites; Carbon Monoxide; Heme; Histidine; Horses; Models, Molecular; Muscle, Skeletal; Myoglobin; Nitrogen Oxides; Nuclear Magnetic Resonance, Biomolecular; Protons

2003
Effect of pH on the iso-1-cytochrome c denatured state: changing constraints due to heme ligation.
    Biochemistry, 2003, Feb-25, Volume: 42, Issue:7

    Topics: Acetylation; Amino Acid Substitution; Binding, Competitive; Cytochrome c Group; Cytochromes c; Genetic Variation; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Lysine; Mutagenesis, Site-Directed; Protein Conformation; Protein Denaturation; Protein Structure, Tertiary; Saccharomyces cerevisiae Proteins; Spectrometry, Fluorescence; Tryptophan

2003
Modulation of the NO trans effect in heme proteins: implications for the activation of soluble guanylate cyclase.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2003, Volume: 8, Issue:6

    Topics: Binding Sites; Enzyme Activation; Guanylate Cyclase; Heme; Hemeproteins; Histidine; Humans; Hydrogen Bonding; Imidazoles; Models, Chemical; Nitric Oxide; Solubility

2003
Interaction of heme with variants of the heme chaperone CcmE carrying active site mutations and a cleavable N-terminal His tag.
    The Journal of biological chemistry, 2003, Jun-06, Volume: 278, Issue:23

    Topics: Apoproteins; Bacterial Outer Membrane Proteins; Binding Sites; Cytochrome c Group; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Binding

2003
Proton NMR study of chemically modified horse heart ferricytochrome c confirms the presence of histidine and lysine-ligated conformers in 30% acetonitrile solution.
    Journal of inorganic biochemistry, 2003, Apr-01, Volume: 94, Issue:4

    Topics: Acetonitriles; Animals; Cytochrome c Group; Guanidines; Heme; Histidine; Horses; Ligands; Lysine; Mitochondria, Heart; Nuclear Magnetic Resonance, Biomolecular; Organoplatinum Compounds; Protein Conformation; Protons; Solutions

2003
A novel heme and peroxide-dependent tryptophan-tyrosine cross-link in a mutant of cytochrome c peroxidase.
    Journal of molecular biology, 2003, Apr-18, Volume: 328, Issue:1

    Topics: Amino Acid Substitution; Cross-Linking Reagents; Crystallography, X-Ray; Cytochrome-c Peroxidase; Heme; Histidine; Imaging, Three-Dimensional; Models, Molecular; Mutation; Peroxides; Porphyrins; Protein Conformation; Protein Folding; Saccharomyces cerevisiae; Tryptophan; Tyrosine; Zinc

2003
Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase.
    The Journal of biological chemistry, 2003, Aug-08, Volume: 278, Issue:32

    Topics: Alanine; Amino Acid Sequence; Animals; Aspartic Acid; Blotting, Western; Catalysis; Cell Division; Circular Dichroism; Cytokines; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Heme; Histidine; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Interferon-gamma; Kinetics; Ligands; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Plasmids; Protein Binding; Protein Conformation; Rats; Sequence Homology, Amino Acid; Tryptophan; Tryptophan Oxygenase; Ultraviolet Rays; Up-Regulation

2003
Proton conduction through full-length gp91phox requires histidine 115.
    Protoplasma, 2003, Volume: 221, Issue:1-2

    Topics: Animals; Arachidonic Acid; CHO Cells; Cricetinae; Gene Expression; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Iron; Ligands; Membrane Glycoproteins; Mutagenesis, Site-Directed; NADPH Oxidase 2; NADPH Oxidases; Protein Structure, Tertiary; Protons

2003
The solution structure of the oxidized bovine microsomal cytochrome b(5) mutant V61H.
    Biochemical and biophysical research communications, 2003, Aug-01, Volume: 307, Issue:3

    Topics: Amino Acid Sequence; Animals; Binding Sites; Cattle; Cytochromes b5; Heme; Histidine; Hydrophobic and Hydrophilic Interactions; Ligands; Microsomes; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mutation; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Structure, Secondary; Protons

2003
A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin.
    Biochemistry, 2003, Sep-02, Volume: 42, Issue:34

    Topics: Animals; Crystallography, X-Ray; Dimerization; Ferric Compounds; Heme; Hemeproteins; Histidine; Horses; Hydrogen Bonding; Hydrogen-Ion Concentration; Ligands; Methemoglobin; Models, Molecular; Protein Structure, Quaternary; Protein Structure, Tertiary; Protein Subunits; Static Electricity; Water

2003
Significance of beta116 His (G18) at alpha1beta1 contact sites for alphabeta assembly and autoxidation of hemoglobin.
    Biochemistry, 2003, Sep-02, Volume: 42, Issue:34

    Topics: Amino Acid Substitution; Binding Sites; Chromatography, Gel; Circular Dichroism; Fetal Hemoglobin; Heme; Hemoglobin A; Hemoglobins; Histidine; Humans; Kinetics; Molecular Weight; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Oxygen; Protein Structure, Quaternary; Recombinant Proteins

2003
Histidine 386 and its role in cyclooxygenase and peroxidase catalysis by prostaglandin-endoperoxide H synthases.
    The Journal of biological chemistry, 2003, Nov-14, Volume: 278, Issue:46

    Topics: Animals; Binding Sites; Catalysis; COS Cells; Crystallography, X-Ray; Cyclooxygenase 1; Eicosanoids; Heme; Histidine; Isoenzymes; Ligands; Linoleic Acid; Microsomes; Models, Chemical; Mutation; Oxygen; Peroxidase; Plasmids; Prostaglandin-Endoperoxide Synthases; Prostaglandins; Protein Binding; Protein Structure, Tertiary; Sheep; Time Factors; Transfection; Tyrosine; Ultraviolet Rays

2003
Temperature, pH, and solvent isotope dependent properties of the active sites of resting-state and cyanide-ligated recombinant cytochrome c peroxidase (H52L) revealed by proton hyperfine resonance spectra.
    Biochemistry, 2003, Sep-16, Volume: 42, Issue:36

    Topics: Amino Acid Substitution; Binding Sites; Cyanides; Cytochrome-c Peroxidase; Heme; Histidine; Hydrogen-Ion Concentration; Leucine; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Protons; Recombinant Proteins; Saccharomyces cerevisiae Proteins; Solvents; Temperature

2003
Preparation of heme-free soluble guanylate cyclase.
    Protein expression and purification, 2003, Volume: 31, Issue:1

    Topics: Benzoates; Chromatography, Ion Exchange; Cyclic GMP; Enzyme Activation; Enzyme Activators; Guanosine Triphosphate; Guanylate Cyclase; Heme; Hemeproteins; Histidine; Indazoles; Nitroprusside; Polysorbates; Proteins; Protoporphyrins; Spectrophotometry; Zinc

2003
Peroxidase activities of hemoproteins. V. Hematin complexes with heterogeneous liganes.
    Archives of biochemistry and biophysics, 1963, Volume: 102

    Topics: Acetates; Alcohols; Amides; Ethanol; Guanidines; Heme; Hemeproteins; Hemin; Histidine; Humans; Methanol; Oxidation-Reduction; Oxidoreductases; Peroxidase; Peroxidases; Pilocarpine; Pyridines

1963
ABSORPTION SPECTRA OF HEMATIN COMPLEXES WITH POLYHISTIDINE AND COPOLY-(HISTIDINE, GLUTAMIC ACID).
    Archives of biochemistry and biophysics, 1963, Volume: 103

    Topics: Animals; Cytochromes; Glutamates; Glutamic Acid; Heme; Hemin; Histidine; Horses; Methemoglobin; Peptides; Research; Spectrophotometry

1963
[EFFECTS OF HYDROCYANIC ACID AND HYDROGEN SULFIDE AND POSSIBILITIES FOR TREATMENT OF POISONING].
    Japanese journal of pharmacology, 1964, Volume: 14

    Topics: Animals; Antidotes; Blood Pressure; Blood Pressure Determination; Central Nervous System Stimulants; Cobalt; Edetic Acid; Epinephrine; Guinea Pigs; Heme; Histidine; Hydrogen Cyanide; Hydrogen Sulfide; Lobeline; Methemoglobin; Nitrites; Oxygen; Pentylenetetrazole; Poisoning; Rats; Research; Sulfides; Thiocyanates; Thiosulfates; Toxicology; Vagotomy

1964
[On organic catalysts. 67. The catalytic activation of hemin by histidine derivatives and histidine peptides].
    Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 1962, May-04, Volume: 327

    Topics: Catalase; Catalysis; Heme; Hemin; Histidine; Peptides

1962
Ligand delivery by haem carrier proteins: the binding of Serratia marcescens haemophore to its outer membrane receptor is mediated by two distinct peptide regions.
    Molecular microbiology, 2003, Volume: 50, Issue:1

    Topics: Bacterial Proteins; Binding, Competitive; Carrier Proteins; DNA Mutational Analysis; Genes, Bacterial; Heme; Histidine; Ligands; Membrane Proteins; Models, Molecular; Mutagenesis, Insertional; Mutagenesis, Site-Directed; Mutation, Missense; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors, Cell Surface; Serratia marcescens; Tyrosine

2003
Solvent dependent and independent motions of CO-horseradish peroxidase examined by infrared spectroscopy and molecular dynamics calculations.
    Biophysical chemistry, 2003, Oct-01, Volume: 106, Issue:1

    Topics: Arginine; Binding Sites; Carbon Monoxide; Heme; Histidine; Horseradish Peroxidase; Hydrogen-Ion Concentration; Hydroxamic Acids; Models, Molecular; Movement; Solvents; Spectrophotometry, Infrared; Temperature

2003
Dynamic features of a heme delivery system for cytochrome C maturation.
    The Journal of biological chemistry, 2003, Dec-26, Volume: 278, Issue:52

    Topics: Alanine; Amino Acid Motifs; Bacterial Outer Membrane Proteins; Bacterial Proteins; Cell Division; Cytochromes c; Cytoplasm; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Genotype; Heme; Hemeproteins; Histidine; Membrane Proteins; Models, Biological; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Periplasm; Phenotype; Plasmids; Precipitin Tests; Protein Binding; Subcellular Fractions; Tryptophan

2003
Reversal of cyanide inhibition of cytochrome c oxidase by the auxiliary substrate nitric oxide: an endogenous antidote to cyanide poisoning?
    The Journal of biological chemistry, 2003, Dec-26, Volume: 278, Issue:52

    Topics: Animals; Brain; Catalysis; Cattle; Copper; Cyanides; Cytochromes c; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Electrons; Heme; Histidine; Iron; Kinetics; Magnetics; Mitochondria; Models, Chemical; Myocardium; Nitric Oxide; Oxygen; Potassium Cyanide; Spectrophotometry

2003
Engineering peroxidase activity in myoglobin: the haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine.
    The Biochemical journal, 2004, Feb-01, Volume: 377, Issue:Pt 3

    Topics: Animals; Crystallography, X-Ray; Enzyme Activation; Ferric Compounds; Ferrous Compounds; Heme; Hemin; Histidine; Kinetics; Mutagenesis, Site-Directed; Myoglobin; Nuclear Magnetic Resonance, Biomolecular; Peroxidases; Protein Engineering; Whales

2004
Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina.
    Biochemistry, 2003, Nov-18, Volume: 42, Issue:45

    Topics: Alanine; Crystallization; Crystallography, X-Ray; Cytochrome c Group; Deuterium Oxide; Electron Transport; Flavin-Adenine Dinucleotide; Heme; Histidine; Kinetics; Ligands; Methionine; Molecular Weight; Mutagenesis, Site-Directed; Potentiometry; Shewanella; Solubility; Solvents; Succinate Dehydrogenase

2003
Effects of site-directed mutations on heme reduction in Escherichia coli nitrate reductase A by menaquinol: a stopped-flow study.
    Biochemistry, 2003, Dec-09, Volume: 42, Issue:48

    Topics: Arginine; Electron Transport; Escherichia coli Proteins; Heme; Histidine; Hydroxyquinolines; Mutagenesis, Site-Directed; Naphthols; Nitrate Reductase; Nitrate Reductases; Nitrates; Oxidation-Reduction; Polyenes; Spectrometry, Fluorescence; Terpenes; Tyrosine; Vitamin K

2003
1H NMR studies of the effect of mutation at Valine45 on heme microenvironment of cytochrome b5.
    Biochimie, 2003, Volume: 85, Issue:10

    Topics: Animals; Cattle; Cytochromes b5; Enzyme Stability; Glutamine; Heme; Histidine; Imidazoles; Ligands; Magnetic Resonance Spectroscopy; Microsomes; Molecular Structure; Mutation; Protein Conformation; Temperature; Tyrosine; Valine

2003
Residues in the distal heme pocket of neuroglobin. Implications for the multiple ligand binding steps.
    The Journal of biological chemistry, 2004, Feb-13, Volume: 279, Issue:7

    Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Carbon Monoxide; Cloning, Molecular; DNA; Electrophoresis, Polyacrylamide Gel; Globins; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Kinetics; Ligands; Lysine; Models, Chemical; Molecular Sequence Data; Mutation; Myoglobin; Nerve Tissue Proteins; Neuroglobin; Protein Binding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Spectrophotometry; Spectrum Analysis, Raman; Time Factors

2004
The 2.0 A resolution crystal structure of prostaglandin H2 synthase-1: structural insights into an unusual peroxidase.
    Journal of molecular biology, 2004, Jan-09, Volume: 335, Issue:2

    Topics: Animals; Binding Sites; Crystallization; Crystallography, X-Ray; Cyclooxygenase Inhibitors; Epidermal Growth Factor; Flurbiprofen; Glycerol; Heme; Histidine; Hydrogen Bonding; Isoenzymes; Lipid Bilayers; Male; Membrane Proteins; Models, Molecular; Peroxidases; Prostaglandin-Endoperoxide Synthases; Protein Conformation; Seminal Vesicles; Sheep

2004
Identification of crucial histidines for heme binding in the N-terminal domain of the heme-regulated eIF2alpha kinase.
    The Journal of biological chemistry, 2004, Feb-20, Volume: 279, Issue:8

    Topics: Amino Acid Sequence; Animals; Circular Dichroism; eIF-2 Kinase; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Histidine; Humans; Ligands; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Spectrophotometry; Spectrum Analysis, Raman; Ultraviolet Rays

2004
Crystallographic analysis of the interaction of nitric oxide with quaternary-T human hemoglobin.
    Biochemistry, 2004, Jan-13, Volume: 43, Issue:1

    Topics: Anaerobiosis; Crystallization; Crystallography, X-Ray; Cysteine; Heme; Hemoglobins; Histidine; Humans; Iron; Ligands; Nitric Oxide; Protein Conformation; Protein Structure, Quaternary; Protein Structure, Tertiary; Protein Subunits; Sulfhydryl Compounds

2004
Hybridization of modified-heme reconstitution and distal histidine mutation to functionalize sperm whale myoglobin.
    Journal of the American Chemical Society, 2004, Jan-21, Volume: 126, Issue:2

    Topics: Animals; Heme; Histidine; Kinetics; Mutation; Myoglobin; Peroxidase; Whales

2004
Characterization of the heme-histidine cross-link in cyanobacterial hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2004, Volume: 9, Issue:2

    Topics: Acids; Amino Acid Substitution; Cross-Linking Reagents; Cyanobacteria; Electrons; Heme; Hemoglobins; Histidine; Hot Temperature; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Models, Molecular; Plasmids; Protein Conformation; Protein Denaturation

2004
Hydrophobic effect of trityrosine on heme ligand exchange during folding of cytochrome c.
    Biochemical and biophysical research communications, 2004, Feb-06, Volume: 314, Issue:2

    Topics: Amino Acids; Animals; Cytochromes c; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Peptides; Protein Folding; Spectrophotometry; Spectrum Analysis, Raman; Tyrosine

2004
Formation and spectroscopic characterization of the dioxygen adduct of a heme-Cu complex possessing a cross-linked tyrosine-histidine mimic: modeling the active site of cytochrome c oxidase.
    Chemical communications (Cambridge, England), 2004, Jan-07, Issue:1

    Topics: Binding Sites; Copper; Electron Transport Complex IV; Heme; Histidine; Imidazoles; Molecular Mimicry; Molecular Structure; Oxygen; Phenols; Porphyrins; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Tyrosine

2004
How O2 binds to heme: reasons for rapid binding and spin inversion.
    The Journal of biological chemistry, 2004, Apr-09, Volume: 279, Issue:15

    Topics: Electrons; Heme; Histidine; Hydrogen; Hydrogen Peroxide; Iron; Ligands; Models, Chemical; Models, Molecular; Molecular Conformation; Oxygen; Porphyrins; Protein Binding; Software; Time Factors

2004
A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide.
    Biochemistry, 2004, Feb-17, Volume: 43, Issue:6

    Topics: Animals; Binding Sites; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Stability; Ferric Compounds; Glycine; Heme; Hemeproteins; Histidine; Horses; Imidazoles; Iron; Ligands; Mercaptoethanol; Methionine; Peptide Fragments; Peptides; Protein Structure, Secondary; Spectrum Analysis, Raman; Structure-Activity Relationship

2004
An EPR, ESEEM, structural NMR, and DFT study of a synthetic model for the covalently ring-linked tyrosine-histidine structure in the heme-copper oxidases.
    Journal of the American Chemical Society, 2004, Mar-03, Volume: 126, Issue:8

    Topics: Computer Simulation; Cross-Linking Reagents; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Fourier Analysis; Heme; Histidine; Models, Chemical; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Oxidoreductases; Tyrosine

2004
The distinct heme coordination environments and heme-binding stabilities of His39Ser and His39Cys mutants of cytochrome b5.
    Protein engineering, 2003, Volume: 16, Issue:12

    Topics: Animals; Cattle; Cysteine; Cytochromes b5; Electrophoresis, Polyacrylamide Gel; Heme; Histidine; Mass Spectrometry; Mutation; Protein Denaturation; Serine; Temperature

2003
The occurrence of two types of hemopexin-like protein in medaka and differences in their affinity to heme.
    The Journal of experimental biology, 2004, Volume: 207, Issue:Pt 8

    Topics: Amino Acid Sequence; Animals; Chromatography, Affinity; DNA, Complementary; Escherichia coli; Genetic Vectors; Heme; Histidine; Immunoblotting; Liver; Molecular Sequence Data; Oryzias; Phylogeny; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Sequence Alignment; Sequence Analysis, DNA; Temperature

2004
Structure of a cDNA for Ciona Cytochrome b(5) and the ubiquitous expression of mRNA in embryonic tissues.
    Journal of biochemistry, 2004, Volume: 135, Issue:2

    Topics: Amino Acid Sequence; Animals; Base Sequence; Ciona intestinalis; Cloning, Molecular; Cytochromes b5; DNA, Complementary; Gene Expression; Heme; Histidine; Humans; Molecular Sequence Data; NAD; Nucleic Acid Conformation; Nucleic Acid Hybridization; Oxidoreductases; Recombinant Proteins; RNA, Messenger

2004
The HP-1 maquette: from an apoprotein structure to a structured hemoprotein designed to promote redox-coupled proton exchange.
    Proceedings of the National Academy of Sciences of the United States of America, 2004, Apr-13, Volume: 101, Issue:15

    Topics: Amino Acid Sequence; Amino Acid Substitution; Apoproteins; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Histidine; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Engineering; Protein Structure, Quaternary; Protein Structure, Secondary; Protons; Spectrophotometry, Ultraviolet

2004
Conformational properties of the iso-1-cytochrome C denatured state: dependence on guanidine hydrochloride concentration.
    Journal of molecular biology, 2004, May-21, Volume: 339, Issue:1

    Topics: Cytochromes c; Guanidine; Heme; Histidine; Isoenzymes; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins

2004
Paracoccus pantotrophus NapC can reductively activate cytochrome cd1 nitrite reductase.
    FEBS letters, 2004, May-07, Volume: 565, Issue:1-3

    Topics: Catalysis; Cytochromes; Cytochromes c; Electron Transport Complex IV; Enzyme Activation; Heme; Histidine; Kinetics; Ligands; Nitrite Reductases; Oxygen; Paracoccus pantotrophus; Spectrophotometry; Time Factors; Tyrosine

2004
A model for the misfolded bis-His intermediate of cytochrome c: the 1-56 N-fragment.
    Journal of inorganic biochemistry, 2004, Volume: 98, Issue:6

    Topics: Animals; Cytochromes c; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Models, Molecular; Myocardium; Peptides; Protein Denaturation; Protein Folding; Protein Structure, Tertiary

2004
Proximal and distal influences on ligand binding kinetics in microperoxidase and heme model compounds.
    Biochemistry, 2004, Jun-08, Volume: 43, Issue:22

    Topics: Animals; Carbon Monoxide; Heart; Heme; Histidine; Horses; Imidazoles; Kinetics; Ligands; Models, Molecular; Myoglobin; Peroxidases; Photolysis; Protein Binding; Protein Conformation; Protoporphyrins; Spectrum Analysis, Raman; Time Factors

2004
Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants.
    Journal of the American Chemical Society, 2004, Jun-09, Volume: 126, Issue:22

    Topics: Animals; Catalysis; Chromatography, High Pressure Liquid; Globins; Heme; Histidine; Hydrogen-Ion Concentration; Isomerism; Kinetics; Metmyoglobin; Mutation; Nitrates; Nitrogen; Peroxynitrous Acid; Tyrosine; Whales

2004
Heme structures of five variants of hemoglobin M probed by resonance Raman spectroscopy.
    Biochemistry, 2004, Jul-06, Volume: 43, Issue:26

    Topics: Carbon; Glutamic Acid; Heme; Hemoglobin M; Hemoglobins; Hemoglobins, Abnormal; Histidine; Ions; Models, Chemical; Mutation; Oxygen; Spectrum Analysis, Raman; Tyrosine

2004
Design and synthesis of de novo cytochromes c.
    Biochemistry, 2004, Aug-03, Volume: 43, Issue:30

    Topics: Amino Acid Sequence; Animals; Cattle; Cytochromes b; Cytochromes c; Genes, Synthetic; Helix-Loop-Helix Motifs; Heme; Histidine; Methionine; Molecular Sequence Data; Oxidation-Reduction; Peptides; Protein Binding; Protein Engineering; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Sulfides

2004
Structural basis for the mechanism of Ca(2+) activation of the di-heme cytochrome c peroxidase from Pseudomonas nautica 617.
    Structure (London, England : 1993), 2004, Volume: 12, Issue:6

    Topics: Amino Acid Sequence; Binding Sites; Calcium; Catalysis; Crystallography, X-Ray; Cytochrome-c Peroxidase; Dimerization; Electron Transport; Electrons; Enzyme Activation; Heme; Histidine; Hydrogen Peroxide; Hydrogen-Ion Concentration; Models, Chemical; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Protein Conformation; Protein Structure, Tertiary; Pseudomonas; Sequence Homology, Amino Acid; Spectrophotometry; Water

2004
Roles of noncoordinated aromatic residues in redox regulation of cytochrome c3 from Desulfovibrio vulgaris Miyazaki F.
    Biochemistry, 2004, Aug-31, Volume: 43, Issue:34

    Topics: Amino Acid Sequence; Amino Acid Substitution; Amino Acids, Aromatic; Cytochrome c Group; Desulfovibrio vulgaris; Electrochemistry; Heme; Histidine; Leucine; Molecular Sequence Data; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Phenylalanine; Tyrosine

2004
Investigations of photolysis and rebinding kinetics in myoglobin using proximal ligand replacements.
    Biochemistry, 2004, Aug-31, Volume: 43, Issue:34

    Topics: Amino Acid Substitution; Animals; Bromine; Carbon Monoxide; Glycine; Heme; Histidine; Imidazoles; Kinetics; Ligands; Models, Chemical; Myoglobin; Photolysis; Protein Binding; Pyridines; Spectrophotometry; Spectrum Analysis, Raman; Whales

2004
Optimised expression and purification of recombinant human indoleamine 2,3-dioxygenase.
    Protein expression and purification, 2004, Volume: 37, Issue:2

    Topics: Aminolevulinic Acid; Biochemistry; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Heme; Histidine; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Iron; Isopropyl Thiogalactoside; Kynurenine; Plasmids; Protoporphyrins; Recombinant Proteins; Temperature; Time Factors; Tryptophan; Tryptophan Oxygenase

2004
Bis-histidyl hexacoordination in hemoglobins facilitates heme reduction kinetics.
    Journal of the American Chemical Society, 2004, Sep-29, Volume: 126, Issue:38

    Topics: Animals; Bacterial Proteins; Cyanobacteria; Heme; Hemoglobins; Histidine; Horses; Humans; Kinetics; Ligands; Models, Molecular; Oxidation-Reduction; Plant Proteins; Structure-Activity Relationship; Whales

2004
Effect of axial coordination on the kinetics of assembly and folding of the two halves of horse heart cytochrome C.
    The Journal of biological chemistry, 2004, Dec-17, Volume: 279, Issue:51

    Topics: Animals; Circular Dichroism; Cytochromes; Cytochromes c; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Models, Molecular; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Protons; Spectrophotometry; Time Factors; Ultraviolet Rays

2004
Cytochrome c550 in the cyanobacterium Thermosynechococcus elongatus: study of redox mutants.
    The Journal of biological chemistry, 2004, Dec-17, Volume: 279, Issue:51

    Topics: Calcium; Chlorine; Cloning, Molecular; Cyanobacteria; Cysteine; Cytochrome c Group; DNA; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hot Temperature; Ligands; Methionine; Models, Genetic; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Oxygen; Plasmids; Point Mutation; Polymerase Chain Reaction; Synechocystis; Temperature; Thylakoids; Time Factors

2004
Cyanide binding to hexacoordinate cyanobacterial hemoglobins: hydrogen-bonding network and heme pocket rearrangement in ferric H117A Synechocystis hemoglobin.
    Biochemistry, 2004, Oct-05, Volume: 43, Issue:39

    Topics: Alanine; Bacterial Proteins; Binding Sites; Cyanobacteria; Heme; Hemeproteins; Hemoglobins; Histidine; Hot Temperature; Hydrogen Bonding; Imidazoles; Iron; Mutagenesis, Site-Directed; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Potassium Cyanide; Protein Binding; Protein Denaturation; Recombinant Proteins; Truncated Hemoglobins

2004
Role of Tyr-288 at the dioxygen reduction site of cytochrome bo studied by stable isotope labeling and resonance raman spectroscopy.
    The Journal of biological chemistry, 2004, Dec-17, Volume: 279, Issue:51

    Topics: Carbon Monoxide; Catalysis; Copper; Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrogen; Ions; Kinetics; Metals; Models, Chemical; Models, Molecular; Nitrites; Oxygen; Quinone Reductases; Spectrophotometry; Spectrum Analysis, Raman; Temperature; Tyrosine

2004
The interaction of covalently bound heme with the cytochrome c maturation protein CcmE.
    The Journal of biological chemistry, 2004, Dec-10, Volume: 279, Issue:50

    Topics: Bacterial Outer Membrane Proteins; Base Sequence; Binding Sites; Cytochromes c; DNA, Bacterial; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Ligands; Protein Binding; Spectrum Analysis, Raman; Tyrosine

2004
Steric effects of isoleucine 107 on heme reorientation reaction in human myoglobin.
    Biochemical and biophysical research communications, 2004, Nov-19, Volume: 324, Issue:3

    Topics: Biochemistry; Heme; Hemin; Histidine; Humans; Isoleucine; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Structure; Myoglobin; Phenylalanine; Proteins; Spectrophotometry; Spectrum Analysis, Raman; Stereoisomerism; X-Rays

2004
NO activation of guanylyl cyclase.
    The EMBO journal, 2004, Nov-10, Volume: 23, Issue:22

    Topics: Catalysis; Cyclic GMP; Diphosphates; Enzyme Activation; Ferrous Compounds; Guanylate Cyclase; Heme; Histidine; Ligands; Magnesium; Models, Chemical; Nitric Oxide; Protein Binding; Signal Transduction; Spectrophotometry, Ultraviolet

2004
In situ effects of mutations of the extrinsic cytochrome c550 of photosystem II in Synechocystis sp. PCC6803.
    Biochemistry, 2004, Nov-09, Volume: 43, Issue:44

    Topics: Amino Acid Substitution; Calcium; Cytochrome c Group; Fluorometry; Heme; Histidine; Ligands; Methionine; Mutagenesis, Site-Directed; Oxygen; Photolysis; Photosystem II Protein Complex; Polarography; Synechocystis; Thylakoids

2004
SOUL in mouse eyes is a new hexameric heme-binding protein with characteristic optical absorption, resonance Raman spectral, and heme-binding properties.
    Biochemistry, 2004, Nov-09, Volume: 43, Issue:44

    Topics: Amino Acid Sequence; Animals; Carrier Proteins; Circular Dichroism; Cloning, Molecular; Eye Proteins; Heme; Heme-Binding Proteins; Hemeproteins; Hemin; Histidine; Ligands; Mice; Mice, Inbred C57BL; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid; Spectrophotometry; Spectrum Analysis, Raman

2004
Molecular modeling and small angle X-ray scattering studies of Hoplosternum littorale cathodic haemoglobin.
    Biochemical and biophysical research communications, 2004, Dec-10, Volume: 325, Issue:2

    Topics: Amino Acid Sequence; Animals; Catfishes; Heme; Hemoglobins; Histidine; Models, Molecular; Oxygen; Protein Structure, Quaternary; Sequence Homology, Amino Acid; X-Ray Diffraction

2004
Protein microarray system for detecting protein-protein interactions using an anti-His-tag antibody and fluorescence scanning: effects of the heme redox state on protein-protein interactions of heme-regulated phosphodiesterase from Escherichia coli.
    Analytical chemistry, 2004, Nov-15, Volume: 76, Issue:22

    Topics: Antibodies; Escherichia coli; Fluorescence; Heme; Histidine; Oxidation-Reduction; Phosphoric Diester Hydrolases; Protein Array Analysis; Proteins

2004
The heme iron coordination of unfolded ferric and ferrous cytochrome c in neutral and acidic urea solutions. Spectroscopic and electrochemical studies.
    Biochimica et biophysica acta, 2004, Dec-01, Volume: 1703, Issue:1

    Topics: Animals; Circular Dichroism; Cytochrome c Group; Electrochemistry; Ferric Compounds; Ferrous Compounds; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Kinetics; Oxidation-Reduction; Protein Denaturation; Solutions; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Urea; Water

2004
Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein.
    The Journal of biological chemistry, 2005, Mar-04, Volume: 280, Issue:9

    Topics: Alanine; Amino Acid Motifs; Bacterial Proteins; Binding Sites; Bradyrhizobium; Ferrochelatase; Glutathione Transferase; Heme; Histidine; Iron; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Oxygen; Protein Structure, Tertiary; Recombinant Fusion Proteins; Recombinant Proteins; Time Factors; Transcription Factors

2005
Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A.
    The Journal of biological chemistry, 2005, Apr-15, Volume: 280, Issue:15

    Topics: Binding Sites; Cell Membrane; Crystallography, X-Ray; Dose-Response Relationship, Drug; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Histidine; Hydroxyquinolines; Kinetics; Lysine; Models, Chemical; Models, Molecular; Mutation; Naphthols; Nitrate Reductase; Nitrate Reductases; Oxidoreductases; Oxygen; Pentachlorophenol; Plasmids; Protein Binding; Protons; Terpenes; Ubiquinone

2005
Abolition of oxygenase function, retention of NADPH oxidase activity, and emergence of peroxidase activity upon replacement of the axial cysteine-436 ligand by histidine in cytochrome P450 2B4.
    Archives of biochemistry and biophysics, 2005, Feb-01, Volume: 434, Issue:1

    Topics: Amino Acid Substitution; Aryl Hydrocarbon Hydroxylases; Base Sequence; Catalytic Domain; Chromatography, High Pressure Liquid; Cysteine; Cytochrome P450 Family 2; DNA, Complementary; Escherichia coli; Heme; Histidine; Hydrogen Peroxide; In Vitro Techniques; Ligands; Molecular Weight; Mutagenesis, Site-Directed; Recombinant Proteins; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry

2005
Effects of metal ions in the CuB center on the redox properties of heme in heme-copper oxidases: spectroelectrochemical studies of an engineered heme-copper center in myoglobin.
    Biochemistry, 2005, Feb-01, Volume: 44, Issue:4

    Topics: Amine Oxidase (Copper-Containing); Animals; Cations, Divalent; Cattle; Copper; Electron Transport; Electron Transport Complex IV; Heme; Histidine; Leucine; Myoglobin; Oxidation-Reduction; Phenylalanine; Potentiometry; Protein Engineering; Spectrophotometry, Ultraviolet; Whales; Zinc

2005
Functional characterization and purification of a Saccharomyces cerevisiae ADP/ATP carrier-iso 1 cytochrome c fusion protein.
    Protein expression and purification, 2005, Volume: 40, Issue:2

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Atractyloside; Chromatography; Cloning, Molecular; Crystallization; Cytochromes c; Escherichia coli; Genetic Engineering; Heme; Histidine; Kinetics; Mitochondrial ADP, ATP Translocases; Molecular Probes; Recombinant Fusion Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins

2005
Purification and characterization of bovine adrenal cytochrome b561 expressed in insect and yeast cell systems.
    Protein expression and purification, 2005, Volume: 40, Issue:2

    Topics: Adrenal Glands; Animals; Baculoviridae; Cattle; Chromatography; Cloning, Molecular; Cytochrome b Group; Genetic Vectors; Heme; Histidine; Insecta; Kinetics; Pichia; Recombinant Proteins; Spectrum Analysis; Yeasts

2005
Unusual heme-histidine bond in the active site of a chaperone.
    Journal of the American Chemical Society, 2005, Mar-23, Volume: 127, Issue:11

    Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Heme; Hemeproteins; Histidine; Molecular Chaperones; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

2005
CO-dependent activity-controlling mechanism of heme-containing CO-sensor protein, neuronal PAS domain protein 2.
    The Journal of biological chemistry, 2005, Jun-03, Volume: 280, Issue:22

    Topics: Amino Acid Sequence; Animals; Basic Helix-Loop-Helix Transcription Factors; Carbon Monoxide; Cysteine; Cytochrome c Group; Dimerization; DNA; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Iron; Ligands; Liver; Mice; Mice, Inbred C57BL; Models, Chemical; Molecular Sequence Data; Mutation; Nerve Tissue Proteins; Neurons; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protons; Sequence Homology, Amino Acid; Signal Transduction; Spectrum Analysis, Raman; Time Factors; Transcription Factors

2005
The histidine of the c-type cytochrome CXXCH haem-binding motif is essential for haem attachment by the Escherichia coli cytochrome c maturation (Ccm) apparatus.
    The Biochemical journal, 2005, Jul-15, Volume: 389, Issue:Pt 2

    Topics: Amino Acid Substitution; Arginine; Binding Sites; Cytochrome b Group; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Lysine; Mutation; Protein Binding

2005
Molecular dynamics simulation of sperm whale myoglobin: effects of mutations and trapped CO on the structure and dynamics of cavities.
    Biophysical journal, 2005, Volume: 89, Issue:1

    Topics: Animals; Biophysics; Carbon Monoxide; Crystallography, X-Ray; Heme; Histidine; Iron; Ligands; Light; Models, Molecular; Models, Statistical; Molecular Conformation; Mutation; Myoglobin; Oxygen; Photolysis; Protein Binding; Protein Conformation; Protein Structure, Secondary; Solvents; Whales

2005
Redox-dependent structural changes in an engineered heme-copper center in myoglobin: insights into chloride binding to CuB in heme copper oxidases.
    Biochemistry, 2005, May-03, Volume: 44, Issue:17

    Topics: Amino Acid Substitution; Animals; Binding Sites; Copper; Electrolysis; Electron Spin Resonance Spectroscopy; Ferric Compounds; Heme; Histidine; Hydroxides; Leucine; Myoglobin; Oxidation-Reduction; Phenylalanine; Potassium Chloride; Potentiometry; Spectrophotometry, Ultraviolet; Whales

2005
Electrochemical and spectroscopic investigations of immobilized de novo designed heme proteins on metal electrodes.
    Chemphyschem : a European journal of chemical physics and physical chemistry, 2005, Volume: 6, Issue:5

    Topics: Biophysics; Chromatography, Gel; Circular Dichroism; Electrochemistry; Electrodes; Heme; Hemeproteins; Histidine; Hydrogen-Ion Concentration; Lysine; Mass Spectrometry; Metals; Models, Chemical; Molecular Conformation; Oxidation-Reduction; Protein Structure, Tertiary; Proteins; Spectrophotometry; Spectrum Analysis, Raman; Static Electricity; Thermodynamics; Time Factors

2005
Y25S variant of Paracoccus pantotrophus cytochrome cd1 provides insight into anion binding by d1 heme and a rare example of a critical difference between solution and crystal structures.
    The Journal of biological chemistry, 2005, Jul-15, Volume: 280, Issue:28

    Topics: Anions; Binding Sites; Crystallography, X-Ray; Cytochrome c Group; Cytochromes; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Mutation; Nitric Oxide; Nitrite Reductases; Nitrites; Oxygen; Paracoccus pantotrophus; Potassium Cyanide; Protein Binding; Spectrophotometry; Temperature; Tyrosine; Ultraviolet Rays

2005
Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin.
    The Journal of biological chemistry, 2005, Jul-22, Volume: 280, Issue:29

    Topics: Alkanesulfonic Acids; Animals; Binding Sites; Crystallography, X-Ray; Cyclohexylamines; Drosophila Proteins; Heme; Hemoglobins; Histidine; Ligands; Oxygen; Protein Conformation; Spectrum Analysis

2005
Structural and dynamic properties of Synechocystis sp. PCC 6803 Hb revealed by reconstitution with Zn-protoporphyrin IX.
    Journal of inorganic biochemistry, 2005, Volume: 99, Issue:8

    Topics: Crystallography, X-Ray; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Models, Molecular; Protein Structure, Tertiary; Protoporphyrins; Synechocystis; Temperature

2005
ENDOR investigation of the liganding environment of mixed-spin ferric cytochrome c'.
    Journal of the American Chemical Society, 2005, Jul-06, Volume: 127, Issue:26

    Topics: Binding Sites; Coumarins; Cytochromes c'; Electron Spin Resonance Spectroscopy; Ferric Compounds; Heme; Histidine; Hydrogen; Hydrogen Bonding; Iron; Ligands; Nitrogen; Phenylalanine; Protons; Rhodobacter sphaeroides

2005
Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2.
    Molecular cell, 2005, Jul-22, Volume: 19, Issue:2

    Topics: Amino Acid Motifs; Cell Line, Tumor; Cysteine; Heme; Histidine; Humans; Iron; Iron Regulatory Protein 2; Ubiquitin

2005
High pressure enhances hexacoordination in neuroglobin and other globins.
    The Journal of biological chemistry, 2005, Nov-04, Volume: 280, Issue:44

    Topics: Animals; Binding Sites; Globins; Heart; Heme; Hemoglobins; Histidine; Horses; Humans; Iron; Kinetics; Ligands; Models, Molecular; Myoglobin; Nerve Tissue Proteins; Neuroglobin; Oxygen; Photolysis; Pressure; Protein Binding; Protein Conformation; Solanum lycopersicum

2005
Axial ligation and polypeptide matrix effects on the reduction potential of heme proteins probed on their cyanide adducts.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2005, Volume: 10, Issue:6

    Topics: Cyanides; Cytochromes c; Electrochemistry; Heme; Hemeproteins; Histidine; Oxidation-Reduction; Peptides; Peroxidases; Plant Proteins; Plants; Thermodynamics; Ultraviolet Rays

2005
Expression of Nox genes in rat organs, mouse oocytes, and sea urchin eggs.
    DNA sequence : the journal of DNA sequencing and mapping, 2005, Volume: 16, Issue:2

    Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Base Sequence; DNA Primers; DNA, Complementary; Female; Gene Expression Regulation; Heme; Histidine; Membrane Glycoproteins; Membrane Proteins; Mice; Molecular Sequence Data; NADH, NADPH Oxidoreductases; NADPH Oxidase 1; NADPH Oxidase 2; NADPH Oxidase 4; NADPH Oxidase 5; NADPH Oxidases; Oocytes; Phylogeny; Rats; RNA; Sea Urchins; Software; Species Specificity; Superoxides; Tissue Distribution

2005
The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities.
    The Journal of biological chemistry, 2005, Nov-18, Volume: 280, Issue:46

    Topics: Animals; Binding Sites; Carbon Monoxide; Glycerol; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Models, Chemical; Models, Molecular; Molecular Conformation; Mutation; Myocardium; Myoglobin; Phase Transition; Protein Binding; Protein Conformation; Recombination, Genetic; Sperm Whale; Stereoisomerism; Temperature; Time Factors; Xenon

2005
Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin.
    Biochemistry, 2005, Oct-11, Volume: 44, Issue:40

    Topics: Carbon Monoxide; Crystallography; Cytoglobin; Globins; Heme; Histidine; Humans; Iron; Ligands; Light; Models, Chemical; Mutation; Nerve Tissue Proteins; Neuroglobin; Nitric Oxide; Photolysis; Protein Binding; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman

2005
A GAF domain in the hypoxia/NO-inducible Mycobacterium tuberculosis DosS protein binds haem.
    Journal of molecular biology, 2005, Nov-11, Volume: 353, Issue:5

    Topics: Amino Acid Sequence; Bacterial Proteins; Cloning, Molecular; Heme; Histidine; Hypoxia; Molecular Sequence Data; Mycobacterium tuberculosis; Nitric Oxide; Oxygen; Protamine Kinase; Protein Structure, Tertiary; Sequence Alignment

2005
Redox and spectroscopic properties of human indoleamine 2,3-dioxygenase and a His303Ala variant: implications for catalysis.
    Biochemistry, 2005, Nov-01, Volume: 44, Issue:43

    Topics: Alanine; Binding Sites; Catalysis; Ferric Compounds; Ferrous Compounds; Genetic Variation; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Indoleamine-Pyrrole 2,3,-Dioxygenase; Ligands; Oxidation-Reduction; Spectrophotometry; Temperature

2005
Detection of the His-heme Fe2+-NO species in the reduction of NO to N2O by ba3-oxidase from thermus thermophilus.
    Journal of the American Chemical Society, 2005, Nov-02, Volume: 127, Issue:43

    Topics: Binding Sites; Copper; Cytochrome b Group; Electron Transport Complex IV; Ferrous Compounds; Heme; Histidine; Ligands; Nitrate Reductase; Nitrogen Oxides; Nitrous Oxide; Oxidation-Reduction; Protons; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Thermus thermophilus

2005
Heme A synthase enzyme functions dissected by mutagenesis of Bacillus subtilis CtaA.
    Journal of bacteriology, 2005, Volume: 187, Issue:24

    Topics: Amino Acid Substitution; Bacillus subtilis; Bacterial Proteins; Chromatography, Affinity; Chromatography, High Pressure Liquid; Cytochrome b Group; DNA Mutational Analysis; Gene Expression; Gene Order; Genes, Bacterial; Heme; Histidine; Membrane Proteins; Models, Biological; Protein Binding; Sequence Deletion; Spectrum Analysis

2005
pH-dependent redox and CO binding properties of chelated protoheme-L-histidine and protoheme-glycyl-L-histidine complexes.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2006, Volume: 11, Issue:2

    Topics: Carbon Monoxide; Chelating Agents; Dipeptides; Heme; Histidine; Hydrogen-Ion Concentration; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Thermodynamics

2006
Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex--a membrane-bound redox complex involved in the sulfate respiratory pathway.
    Biochemistry, 2006, Jan-10, Volume: 45, Issue:1

    Topics: Bacterial Proteins; Catalysis; Cysteine; Cytochrome c Group; Desulfovibrio desulfuricans; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Genomics; Heme; Histidine; Iron-Sulfur Proteins; Membranes; Methionine; Oxidation-Reduction; Respiratory System; Spectrophotometry, Ultraviolet; Sulfates

2006
Characterization of heme environment and mechanism of peroxide bond cleavage in human prostacyclin synthase.
    Biochimica et biophysica acta, 2005, Dec-30, Volume: 1738, Issue:1-3

    Topics: Amino Acid Sequence; Binding Sites; Circular Dichroism; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Heme; Histidine; Humans; Hydrophobic and Hydrophilic Interactions; Intramolecular Oxidoreductases; Kinetics; Ligands; Linoleic Acids; Molecular Sequence Data; Peroxides; Protein Engineering; Recombinant Proteins; Spectrophotometry, Ultraviolet

2005
Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus.
    Structure (London, England : 1993), 2006, Volume: 14, Issue:1

    Topics: Amino Acid Sequence; Binding Sites; Calcium; Catalysis; Crystallography, X-Ray; Cytochrome-c Peroxidase; Enzyme Activation; Heme; Histidine; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Paracoccus pantotrophus; Protein Conformation; Protein Structure, Tertiary; Pseudomonas; Sequence Alignment

2006
Linker chains of the gigantic hemoglobin of the earthworm Lumbricus terrestris: primary structures of linkers L2, L3, and L4 and analysis of the connectivity of the disulfide bonds in linker L1.
    Proteins, 2006, Apr-01, Volume: 63, Issue:1

    Topics: Amino Acid Sequence; Animals; Aspartic Acid; Base Sequence; Binding Sites; Calcium; Chromatography, High Pressure Liquid; Cysteine; Disulfides; Dithiothreitol; DNA, Complementary; Glutamic Acid; Heme; Hemoglobins; Histidine; Humans; Ligands; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Oligochaeta; Protein Binding; Protein Processing, Post-Translational; Protein Structure, Tertiary; Receptors, LDL; RNA, Messenger; Sequence Homology, Amino Acid; Sodium Dodecyl Sulfate; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Superoxide Dismutase

2006
Water and ligand entry in myoglobin: assessing the speed and extent of heme pocket hydration after CO photodissociation.
    Proceedings of the National Academy of Sciences of the United States of America, 2006, Jan-31, Volume: 103, Issue:5

    Topics: Animals; Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Electrons; Heme; Histidine; Kinetics; Ligands; Models, Chemical; Models, Molecular; Mutation; Myoglobin; Recombinant Proteins; Spectrophotometry; Sperm Whale; Temperature; Thermodynamics; Time Factors; Water; X-Rays

2006
On the relationship of coral allene oxide synthase to catalase. A single active site mutation that induces catalase activity in coral allene oxide synthase.
    The Journal of biological chemistry, 2006, May-05, Volume: 281, Issue:18

    Topics: Animals; Anthozoa; Binding Sites; Catalase; Heme; Histidine; Hydrogen Bonding; Hydrogen Peroxide; Intramolecular Oxidoreductases; Models, Chemical; Models, Molecular; Mutation; Spectrum Analysis, Raman; Threonine

2006
Soret spectral and bioinformatic approaches provide evidence for a critical role of the alpha -subunit in assembly of tetrameric hemoglobin.
    The protein journal, 2006, Volume: 25, Issue:1

    Topics: Amino Acid Sequence; Binding Sites; Computational Biology; Heme; Hemin; Hemoglobins; Histidine; Humans; Hydrogen-Ion Concentration; Molecular Sequence Data; Protein Subunits; Sequence Alignment; Spectrum Analysis; Temperature

2006
Modeling proline ligation in the heme-dependent CO sensor, CooA, using small-molecule analogs.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2006, Volume: 11, Issue:5

    Topics: Bacterial Proteins; Carbon Monoxide; Computational Biology; Crystallography, X-Ray; Heme; Hemeproteins; Histidine; Imidazoles; Iron; Ligands; Models, Molecular; Molecular Structure; Proline; Pyrrolidines; Trans-Activators

2006
Structure and dynamics of dioxygen bound to cobalt and iron heme.
    Biophysical journal, 2006, Sep-15, Volume: 91, Issue:6

    Topics: Binding Sites; Cobalt; Computer Simulation; Ferric Compounds; Heme; Histidine; Imidazoles; Iron; Models, Molecular; Myoglobin; Oxides; Oxygen; Porphyrins; Protein Conformation

2006
Redox infrared markers of the heme and axial ligands in microperoxidase: Bases for the analysis of c-type cytochromes.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2006, Volume: 11, Issue:7

    Topics: Biomarkers; Cytochrome c Group; Electrochemistry; Heme; Histidine; Imidazoles; Ligands; Molecular Structure; Oxidation-Reduction; Peroxidases; Spectroscopy, Fourier Transform Infrared

2006
Quantum chemical evaluation of protein control over heme ligation: CO/O2 discrimination in myoglobin.
    The journal of physical chemistry. B, 2005, Feb-24, Volume: 109, Issue:7

    Topics: Animals; Binding Sites; Carbon; Carbon Monoxide; Heme; Histidine; Isoleucine; Models, Molecular; Molecular Conformation; Myoglobin; Oxygen; Photochemistry; Protein Binding; Quantum Theory; Software

2005
Insights into the structure and function of redox-active tyrosines from model compounds.
    The journal of physical chemistry. B, 2005, Apr-21, Volume: 109, Issue:15

    Topics: Cross-Linking Reagents; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Electrons; Heme; Histidine; Hydrogen-Ion Concentration; Light; Magnetic Resonance Spectroscopy; Models, Chemical; Oxidation-Reduction; Oxidoreductases; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Tyrosine

2005
Effect of mutation on the dissociation and recombination dynamics of CO in transcriptional regulator CooA: a picosecond infrared transient absorption study.
    Biochemistry, 2006, Aug-01, Volume: 45, Issue:30

    Topics: Bacterial Proteins; Carbon Monoxide; Glycine; Heme; Hemeproteins; Histidine; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Recombination, Genetic; Regulatory Elements, Transcriptional; Rhodospirillum rubrum; Spectroscopy, Near-Infrared; Trans-Activators

2006
Roles of the heme and heme ligands in the activation of CooA, the CO-sensing transcriptional activator.
    Biochemical and biophysical research communications, 2006, Sep-22, Volume: 348, Issue:2

    Topics: Amino Acid Sequence; Bacterial Proteins; Cysteine; Heme; Hemeproteins; Histidine; Ligands; Trans-Activators

2006
Drosophila nuclear receptor E75 is a thiolate hemoprotein.
    Biochemistry, 2006, Aug-15, Volume: 45, Issue:32

    Topics: Alanine; Amino Acid Sequence; Animals; Cysteine; DNA-Binding Proteins; Drosophila melanogaster; Drosophila Proteins; Electron Spin Resonance Spectroscopy; Gene Expression; Heme; Hemeproteins; Histidine; Humans; Ligands; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Tertiary; Receptors, Cytoplasmic and Nuclear; Sequence Alignment; Solubility; Spectrophotometry, Ultraviolet; Sulfur; Transcription Factors

2006
Cyanide binding and heme cavity conformational transitions in Drosophila melanogaster hexacoordinate hemoglobin.
    Biochemistry, 2006, Aug-22, Volume: 45, Issue:33

    Topics: Animals; Binding Sites; Crystallography, X-Ray; Cyanides; Cytoglobin; Drosophila melanogaster; Drosophila Proteins; Globins; Heme; Hemoglobins; Histidine; Humans; Kinetics; Ligands; Mice; Molecular Sequence Data; Nerve Tissue Proteins; Neuroglobin; Protein Conformation; Sequence Analysis, Protein

2006
Cofacial heme binding is linked to dimerization by a bacterial heme transport protein.
    Journal of molecular biology, 2006, Oct-06, Volume: 362, Issue:5

    Topics: Bacterial Proteins; Biological Transport; Campylobacter jejuni; Crystallization; Dimerization; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Ligands; Lysine; Models, Molecular; Mutation; Phylogeny; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Sequence Analysis, Protein; Tyrosine; Ultracentrifugation

2006
Structural and chemical changes of the P(M) intermediate of paracoccus denitrificans cytochrome c oxidase revealed by IR spectroscopy with labeled tyrosines and histidine.
    Biochemistry, 2006, Sep-12, Volume: 45, Issue:36

    Topics: Amides; Amino Acids; Carbon Isotopes; Electron Transport Complex IV; Heme; Histidine; Mutation; Nitrogen Isotopes; Paracoccus denitrificans; Spectroscopy, Fourier Transform Infrared; Tyrosine

2006
Characterization of heme-coordinating histidyl residues of cytochrome b5 based on the reactivity with diethylpyrocarbonate: a mechanism for the opening of axial imidazole rings.
    Journal of biochemistry, 2006, Volume: 140, Issue:4

    Topics: Amino Acid Sequence; Cloning, Molecular; Cytochromes b5; Diethyl Pyrocarbonate; Electron Spin Resonance Spectroscopy; Heme; Histidine; Humans; Hydrogen Bonding; Imidazoles; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

2006
Probing the unusual oxidation/reduction behavior of Paracoccus pantotrophus cytochrome cd1 nitrite reductase by replacing a switchable methionine heme iron ligand with histidine.
    Biochemistry, 2006, Sep-19, Volume: 45, Issue:37

    Topics: Amino Acid Sequence; Cytochromes; Heme; Histidine; Iron; Ligands; Methionine; Nitrite Reductases; Oxidation-Reduction; Paracoccus pantotrophus

2006
Proximal influences in two-on-two globins: effect of the Ala69Ser replacement on Synechocystis sp. PCC 6803 hemoglobin.
    Biochemistry, 2006, Sep-26, Volume: 45, Issue:38

    Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Cyanides; Ferric Compounds; Globins; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Myoglobin; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Denaturation; Recombinant Proteins; Serine; Sperm Whale; Structure-Activity Relationship; Synechocystis; Temperature; Urea

2006
Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His-193.
    The Journal of biological chemistry, 2006, Dec-01, Volume: 281, Issue:48

    Topics: Alanine; Carbon Monoxide; Catalysis; Chromatography, Gas; Crystallography, X-Ray; Escherichia coli O157; Escherichia coli Proteins; Heme; Heme Oxygenase (Decyclizing); Histidine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; X-Ray Diffraction

2006
Heme-heme interactions in the cytochrome b6f complex: EPR spectroscopy and correlation with structure.
    Journal of the American Chemical Society, 2006, Nov-08, Volume: 128, Issue:44

    Topics: Cysteine; Cytochrome b6f Complex; Electron Spin Resonance Spectroscopy; Heme; Histidine; Molecular Structure

2006
DNA binding by an imidazole-sensing CooA variant is dependent on the heme redox state.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2007, Volume: 12, Issue:2

    Topics: Bacterial Proteins; Carbon Monoxide; Circular Dichroism; DNA-Binding Proteins; Gene Expression Regulation, Bacterial; Heme; Hemeproteins; Histidine; Imidazoles; Oxidation-Reduction; Rhodospirillum rubrum; Trans-Activators

2007
The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand.
    Journal of molecular biology, 2007, Jan-26, Volume: 365, Issue:4

    Topics: Bacterial Proteins; Carrier Proteins; Crystallography, X-Ray; Dimerization; Escherichia coli; Heme; Hemin; Histidine; Ligands; Magnetic Resonance Spectroscopy; Membrane Proteins; Molecular Conformation; Protein Conformation; Protein Structure, Secondary; Serratia marcescens; Tyrosine

2007
Axial coordination of heme in ferric CcmE chaperone characterized by EPR spectroscopy.
    Biophysical journal, 2007, Feb-15, Volume: 92, Issue:4

    Topics: Bacterial Outer Membrane Proteins; Electron Spin Resonance Spectroscopy; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Molecular Chaperones; Mutation

2007
Cytochrome C in a dry trehalose matrix: structural and dynamical effects probed by x-ray absorption spectroscopy.
    Biophysical journal, 2007, Feb-15, Volume: 92, Issue:4

    Topics: Animals; Cytochromes c; Heme; Histidine; Horses; Iron; Models, Molecular; Myocardium; Polyvinyl Alcohol; Protein Conformation; Solutions; Spectrum Analysis; Trehalose; X-Rays

2007
Two conserved non-canonical histidines are essential for activity of the cbb (3)-type oxidase in Rhodobacter capsulatus: non-canonical histidines are essential for cbb (3)-type oxidase activity in R. capsulatus.
    Molecular biology reports, 2007, Volume: 34, Issue:3

    Topics: Amino Acid Sequence; Catalytic Domain; Conserved Sequence; Electron Transport Complex IV; Heme; Histidine; Models, Biological; Mutagenesis, Site-Directed; Rhodobacter capsulatus

2007
Weak-field anions displace the histidine ligand in a synthetic heme peptide but not in N-acetylmicroperoxidase-8: possible role of heme geometry differences.
    Inorganic chemistry, 2007, Jan-08, Volume: 46, Issue:1

    Topics: Animals; Anions; Azides; Binding Sites; Cyanides; Cytochromes c; Fluorides; Heme; Hemeproteins; Histidine; Horses; Ligands; Molecular Structure; Myocardium; Peptide Fragments; Peptides; Protein Conformation

2007
Theoretical density functional theory studies on interactions of small biologically active molecules with isolated heme group.
    Journal of computational chemistry, 2007, Volume: 28, Issue:4

    Topics: Carbon Monoxide; Computational Biology; Ferrous Compounds; Heme; Histidine; Ligands; Models, Molecular; Molecular Conformation; Nitric Oxide; Nitrogen Dioxide; Water

2007
Design of a functional membrane protein by engineering a heme-binding site in glycophorin A.
    Journal of the American Chemical Society, 2007, Jan-24, Volume: 129, Issue:3

    Topics: Amino Acid Sequence; Binding Sites; Electrophoresis, Polyacrylamide Gel; Glycophorins; Heme; Histidine; Hydrophobic and Hydrophilic Interactions; Membrane Proteins; Molecular Sequence Data; Phosphatidylcholines; Protein Conformation; Spectrum Analysis; Time Factors; Ultracentrifugation

2007
Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation.
    Protein science : a publication of the Protein Society, 2007, Volume: 16, Issue:2

    Topics: Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Cyanides; Guanidine; Heme; Hemoglobins; Histidine; Iron; Ligands; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Synechocystis

2007
De novo design of DeltaF -containing heme-binding peptides.
    Chemical biology & drug design, 2007, Volume: 69, Issue:2

    Topics: Amino Acid Sequence; Cobalt; Coproporphyrins; Heme; Histidine; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Peptides, Cyclic

2007
Characterization of the outer membrane receptor ShuA from the heme uptake system of Shigella dysenteriae. Substrate specificity and identification of the heme protein ligands.
    The Journal of biological chemistry, 2007, May-18, Volume: 282, Issue:20

    Topics: Amino Acid Substitution; Bacterial Outer Membrane Proteins; Bacterial Proteins; Biological Transport, Active; Heme; Hemoglobins; Histidine; Iron; Ligands; Membrane Proteins; Membranes, Artificial; Micelles; Multiprotein Complexes; Mutagenesis, Site-Directed; Mutation, Missense; Oxidation-Reduction; Protein Binding; Receptors, Cell Surface; Shigella dysenteriae; Substrate Specificity

2007
Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE.
    The FEBS journal, 2007, Volume: 274, Issue:9

    Topics: Adenosine Triphosphate; Amino Acid Motifs; Aspartic Acid; ATP-Binding Cassette Transporters; Bacterial Outer Membrane Proteins; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Hydrolysis; Lysine; Mutagenesis, Site-Directed; Protein Processing, Post-Translational; Protein Subunits; Sequence Deletion

2007
Solution conformation of the His-47 to Ala-47 mutant of Pseudomonas stutzeri ZoBell ferrocytochrome c-551.
    Biophysical journal, 2007, Sep-01, Volume: 93, Issue:5

    Topics: Alanine; Bacterial Proteins; Cytochrome c Group; Cytochromes c; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Models, Chemical; Molecular Conformation; Mutation; Oxidation-Reduction; Protein Conformation; Pseudomonas stutzeri; Thermodynamics

2007
Synthetic models of the active site of cytochrome C oxidase: influence of tridentate or tetradentate copper chelates bearing a His--Tyr linkage mimic on dioxygen adduct formation by heme/Cu complexes.
    Chemistry (Weinheim an der Bergstrasse, Germany), 2007, Volume: 13, Issue:22

    Topics: Animals; Binding Sites; Biomimetic Materials; Cattle; Copper; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Ferric Compounds; Heme; Histidine; Models, Molecular; Myocardium; Organometallic Compounds; Oxygen; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Tyrosine

2007
Activation of the cytochrome c peroxidase of Pseudomonas aeruginosa. The role of a heme-linked protein loop: a mutagenesis study.
    Journal of inorganic biochemistry, 2007, Volume: 101, Issue:8

    Topics: Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Enzyme Activation; Glycine; Heme; Hemeproteins; Histidine; Ligands; Mutagenesis, Site-Directed; Protein Structure, Secondary; Pseudomonas aeruginosa; Recombinant Proteins; Sequence Deletion

2007
Sequence composition effects on denatured state loop formation in iso-1-cytochrome c variants: polyalanine versus polyglycine inserts.
    Journal of molecular biology, 2007, Aug-17, Volume: 371, Issue:3

    Topics: Amino Acid Sequence; Cytochromes c; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutagenesis, Insertional; Mutant Proteins; Peptides; Protein Denaturation; Protein Structure, Secondary; Saccharomyces cerevisiae Proteins; Thermodynamics; Titrimetry

2007
What is the active species of cytochrome P450 during camphor hydroxylation? QM/MM studies of different electronic states of compound I and of reduced and oxidized iron-oxo intermediates.
    Journal of the American Chemical Society, 2007, Jul-25, Volume: 129, Issue:29

    Topics: Aspartic Acid; Camphor; Computational Biology; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Electrons; Free Radicals; Heme; Histidine; Hydroxylation; Iron; Oxidation-Reduction; Protons; Quantum Theory

2007
Axial ligation and stoichiometry of heme centers in adrenal cytochrome b561.
    Biochemistry, 2007, Jul-24, Volume: 46, Issue:29

    Topics: Adrenal Medulla; Animals; Cattle; Cell Membrane; Cytochrome b Group; Cytoplasm; Electron Spin Resonance Spectroscopy; Heme; Histidine; Ligands; Models, Biological; Mutation; Recombinant Proteins

2007
Modulation of heme redox potential in the cytochrome c6 family.
    Journal of the American Chemical Society, 2007, Aug-01, Volume: 129, Issue:30

    Topics: Amino Acid Sequence; Crystallography, X-Ray; Cyanobacteria; Cytochromes c6; Electrochemistry; Electron Transport; Glutamine; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Ligands; Methionine; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Valine

2007
Alkaline conformational transition and gated electron transfer with a Lys 79 --> his variant of iso-1-cytochrome c.
    Biochemistry, 2007, Sep-18, Volume: 46, Issue:37

    Topics: Alkalies; Anaerobiosis; Cytochromes c; Electron Transport; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Lysine; Magnetic Resonance Spectroscopy; Mutant Proteins; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protons; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics

2007
Effect of strain in the proximal ligand on the binding of nitric oxide and carbon monoxide to chelated protoheme complexes.
    Inorganic chemistry, 2007, Oct-15, Volume: 46, Issue:21

    Topics: Carbon Monoxide; Dimethyl Sulfoxide; Dose-Response Relationship, Drug; Heme; Histidine; Imidazoles; Iron; Ligands; Methanol; Models, Chemical; Molecular Structure; Nitric Oxide; Stress, Mechanical; Thermodynamics

2007
Tyrosinase-generated quinones induce covalent modification, unfolding, and aggregation of human holo-myoglobin.
    Biomacromolecules, 2007, Volume: 8, Issue:10

    Topics: Biocompatible Materials; Circular Dichroism; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Monophenol Monooxygenase; Myoglobin; Oxygen; Phenols; Protein Denaturation; Protein Engineering; Protein Structure, Secondary; Quinones; Spectrometry, Mass, Electrospray Ionization; Temperature

2007
Heme attachment motif mobility tunes cytochrome c redox potential.
    Biochemistry, 2007, Oct-23, Volume: 46, Issue:42

    Topics: Amino Acid Motifs; Amino Acid Sequence; Bacteria; Bacterial Proteins; Cytochrome c Group; Deuterium; Electrochemistry; Genetic Variation; Heme; Histidine; Hydrogen; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Mutation; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Plasmids; Protein Conformation; Pseudomonas aeruginosa; Solubility; Templates, Genetic

2007
Nitrite controls the release of nitric oxide in Pseudomonas aeruginosa cd1 nitrite reductase.
    Biochemical and biophysical research communications, 2007, Nov-23, Volume: 363, Issue:3

    Topics: Bacterial Proteins; Catalysis; Catalytic Domain; Cyanides; Heme; Histidine; Kinetics; Models, Molecular; Mutagenesis; Nitric Oxide; Nitrite Reductases; Nitrites; Protein Binding; Pseudomonas aeruginosa; Substrate Specificity

2007
Histidine cycle mechanism for the concerted proton/electron transfer from ascorbate to the cytosolic haem b centre of cytochrome b561: a unique machinery for the biological transmembrane electron transfer.
    Journal of biochemistry, 2007, Volume: 142, Issue:5

    Topics: Ascorbic Acid; Chromaffin Cells; Cytochrome b Group; Cytosol; Electrochemistry; Electron Transport; Eukaryotic Cells; Free Radicals; Heme; Histidine; Membrane Proteins; NADH, NADPH Oxidoreductases; Neurosecretory Systems; Oxidation-Reduction; Protons; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

2007
Non-native heme-histidine ligation promotes microsecond time scale secondary structure formation in reduced horse heart cytochrome c.
    Biochemistry, 2007, Oct-30, Volume: 46, Issue:43

    Topics: Animals; Circular Dichroism; Cytochromes c; Guanidine; Heme; Histidine; Horses; Myocardium; Protein Folding; Protein Structure, Secondary; Spectrophotometry, Ultraviolet

2007
Characterization of a globin-coupled oxygen sensor with a gene-regulating function.
    The Journal of biological chemistry, 2007, Dec-28, Volume: 282, Issue:52

    Topics: Amino Acid Sequence; Azotobacter vinelandii; Bacterial Proteins; Escherichia coli; Gene Expression Regulation, Bacterial; Heme; Hemeproteins; Histidine; Iron; Kinetics; Ligands; Models, Biological; Molecular Sequence Data; Nitric Oxide; Oxygen; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Spectrum Analysis, Raman; Time Factors

2007
Heme binding properties of Staphylococcus aureus IsdE.
    Biochemistry, 2007, Nov-06, Volume: 46, Issue:44

    Topics: Carrier Proteins; Heme; Histidine; Ligands; Models, Biological; Mutagenesis, Site-Directed; Protein Binding; Protein Folding; Recombinant Proteins; Staphylococcus aureus

2007
Exploring the molecular basis of heme coordination in human neuroglobin.
    Proteins, 2008, May-01, Volume: 71, Issue:2

    Topics: Animals; Computer Simulation; Crystallography, X-Ray; Globins; Heme; Histidine; Humans; Ligands; Mice; Models, Molecular; Nerve Tissue Proteins; Neuroglobin; Protein Binding; Protein Conformation; Thermodynamics

2008
Identification of two heme-binding sites in the cytoplasmic heme-trafficking protein PhuS from Pseudomonas aeruginosa and their relevance to function.
    Biochemistry, 2007, Dec-18, Volume: 46, Issue:50

    Topics: Bacterial Proteins; Binding Sites; Carrier Proteins; Cytoplasm; Heme; Heme-Binding Proteins; Hemeproteins; Histidine; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Mutation; Protein Structure, Secondary; Protein Structure, Tertiary; Pseudomonas aeruginosa; Spectrum Analysis, Raman; Tyrosine

2007
Deciphering the structural role of histidine 83 for heme binding in hemophore HasA.
    The Journal of biological chemistry, 2008, Feb-29, Volume: 283, Issue:9

    Topics: Bacterial Proteins; Carrier Proteins; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Membrane Proteins; Mutation, Missense; Protein Binding; Protein Structure, Tertiary; Serratia marcescens; Structure-Activity Relationship

2008
Functional characterization of human duodenal cytochrome b (Cybrd1): Redox properties in relation to iron and ascorbate metabolism.
    Biochimica et biophysica acta, 2008, Volume: 1777, Issue:3

    Topics: Aminolevulinic Acid; Animals; Ascorbic Acid; Baculoviridae; Cell Line; Cloning, Molecular; Cytochrome b Group; Duodenum; Electron Spin Resonance Spectroscopy; Ferricyanides; Genetic Vectors; Heme; Histidine; Humans; Iron; Ligands; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Potentiometry; Recombinant Proteins; Transduction, Genetic

2008
DFT analysis of axial and equatorial effects on heme-CO vibrational modes: applications to CooA and H-NOX heme sensor proteins.
    Biochemistry, 2008, Feb-26, Volume: 47, Issue:8

    Topics: Bacterial Proteins; Biosensing Techniques; Carbon; Carbon Dioxide; Heme; Histidine; Hydrogen Bonding; Imidazoles; Models, Biological; Models, Molecular; Molecular Conformation; Nitric Oxide; Oxides; Oxygen; Porphyrins; Propionates; Protein Folding; Quantum Theory; Thermoanaerobacter; Vibration

2008
Measurement of distal histidine coordination equilibrium and kinetics in hexacoordinate hemoglobins.
    Methods in enzymology, 2008, Volume: 436

    Topics: Electrochemistry; Heme; Hemoglobins; Histidine; Iron; Kinetics; Ligands; Nitric Oxide; Oxidation-Reduction

2008
Protonation of the proximal histidine ligand in heme peroxidases.
    The journal of physical chemistry. B, 2008, Feb-28, Volume: 112, Issue:8

    Topics: Aspartic Acid; Heme; Histidine; Ligands; Models, Chemical; Peroxidase; Protons; Quantum Theory; Solvents; Thermodynamics

2008
Hydrogen atom transfer reactions of iron-porphyrin-imidazole complexes as models for histidine-ligated heme reactivity.
    Journal of the American Chemical Society, 2008, Mar-05, Volume: 130, Issue:9

    Topics: Heme; Histidine; Hydrogen; Imidazoles; Iron; Kinetics; Ligands; Models, Chemical; Molecular Structure; Porphyrins

2008
The pH dependence of heme pocket hydration and ligand rebinding kinetics in photodissociated carbonmonoxymyoglobin.
    The Journal of biological chemistry, 2008, May-16, Volume: 283, Issue:20

    Topics: Animals; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Models, Biological; Models, Statistical; Myoglobin; Protein Conformation; Spectrophotometry; Sperm Whale; Water

2008
Structural propensities in the heme binding region of apocytochrome b5. I. Free peptides.
    Biopolymers, 2008, Volume: 90, Issue:4

    Topics: Amino Acid Sequence; Animals; Binding Sites; Circular Dichroism; Cytochromes b5; Heme; Histidine; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Peptides; Protein Structure, Secondary; Rats; Solubility; Solutions; Trifluoroethanol

2008
An X-ray diffraction and X-ray absorption spectroscopy joint study of neuroglobin.
    Archives of biochemistry and biophysics, 2008, Jul-01, Volume: 475, Issue:1

    Topics: Animals; Carbon Monoxide; Cloning, Molecular; Escherichia coli; Globins; Heme; Histidine; Iron; Mice; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Protein Binding; Recombinant Proteins; Spectrum Analysis; X-Ray Diffraction; X-Rays

2008
Polyvalent display of heme on hepatitis B virus capsid protein through coordination to hexahistidine tags.
    Chemistry & biology, 2008, Volume: 15, Issue:5

    Topics: Base Sequence; Capsid; Chromatography, Gel; Cryoelectron Microscopy; DNA Primers; Heme; Hepatitis B virus; Histidine; Oligopeptides; Spectrum Analysis, Raman

2008
Ligand preference and orientation in b- and c-type heme-binding proteins.
    Proteins, 2008, Nov-15, Volume: 73, Issue:3

    Topics: Amino Acid Motifs; Binding Sites; Carrier Proteins; Databases, Protein; Heme; Heme-Binding Proteins; Hemeproteins; Histidine; Hydrogen-Ion Concentration; Ligands; Models, Molecular; Propionates; Static Electricity; Thermodynamics

2008
Probing the bottom of a folding funnel using conformationally gated electron transfer reactions.
    Journal of the American Chemical Society, 2008, Jun-18, Volume: 130, Issue:24

    Topics: Cytochromes c; Electron Transport; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Mutation; Protein Conformation; Protein Folding

2008
His92 and His110 selectively affect different heme centers of adrenal cytochrome b(561).
    Biochimica et biophysica acta, 2008, Volume: 1777, Issue:9

    Topics: Adrenal Glands; Amino Acid Sequence; Animals; Ascorbic Acid; Cattle; Cytochrome b Group; Electron Spin Resonance Spectroscopy; Heme; Histidine; Humans; Models, Molecular; Molecular Sequence Data; Mutant Proteins; Mutation; Oxidation-Reduction; Protein Structure, Secondary; Recombinant Proteins; Sequence Alignment; Spectrum Analysis; Structure-Activity Relationship; Titrimetry

2008
Evidence that two enzyme-derived histidine ligands are sufficient for iron binding and catalysis by factor inhibiting HIF (FIH).
    The Journal of biological chemistry, 2008, Sep-19, Volume: 283, Issue:38

    Topics: Catalysis; Crystallography, X-Ray; Dioxygenases; Heme; Histidine; Humans; Iron; Ketoglutaric Acids; Ligands; Metals; Mixed Function Oxygenases; Models, Chemical; Models, Molecular; Molecular Conformation; Protein Binding; Repressor Proteins

2008
Functional characterization of the Shigella dysenteriae heme ABC transporter.
    Biochemistry, 2008, Aug-05, Volume: 47, Issue:31

    Topics: Adenosine Triphosphate; ATP-Binding Cassette Transporters; Bacterial Proteins; Biological Transport; Heme; Histidine; Models, Biological; Mutagenesis, Site-Directed; Protein Binding; Protein Structure, Secondary; Shigella dysenteriae

2008
Geometric constraints for porphyrin binding in helical protein binding sites.
    Proteins, 2009, Feb-01, Volume: 74, Issue:2

    Topics: Amino Acid Sequence; Binding Sites; Computer Simulation; Cytochrome c Group; Databases, Protein; Heme; Hemeproteins; Histidine; Ligands; Models, Molecular; Porphyrins; Propionates; Protein Binding; Protein Conformation; Protein Structure, Secondary

2009
Characterization of heme-coordinating histidyl residues of an engineered six-coordinated myoglobin mutant based on the reactivity with diethylpyrocarbonate, mass spectrometry, and electron paramagnetic resonance spectroscopy.
    Journal of bioscience and bioengineering, 2008, Volume: 105, Issue:6

    Topics: Diethyl Pyrocarbonate; Electron Spin Resonance Spectroscopy; Heme; Histidine; Mass Spectrometry; Mutation; Myoglobin; Protein Engineering; Protein Structure, Tertiary

2008
Multiple step assembly of the transmembrane cytochrome b6.
    Journal of molecular biology, 2008, Oct-17, Volume: 382, Issue:4

    Topics: Cytochromes b6; Heme; Histidine; Models, Molecular; Oxidation-Reduction; Plant Proteins; Protein Binding; Protein Conformation; Protein Isoforms; Recombinant Fusion Proteins; Spinacia oleracea

2008
A Soret marker band for four-coordinate ferric heme proteins from absorption spectra of isolated Fe(III)-Heme+ and Fe(III)-Heme+(His) ions in vacuo.
    Journal of the American Chemical Society, 2008, Sep-10, Volume: 130, Issue:36

    Topics: Ferric Compounds; Heme; Hemin; Histidine; Spectrophotometry; Static Electricity

2008
Dynamical characterization of the heme NO oxygen binding (HNOX) domain. Insight into soluble guanylate cyclase allosteric transition.
    Biochemistry, 2008, Sep-09, Volume: 47, Issue:36

    Topics: Allosteric Regulation; Animals; Bacterial Proteins; Computer Simulation; Enzyme Activation; Guanylate Cyclase; Heme; Histidine; Humans; Iron; Models, Molecular; Nitric Oxide; Oxygen; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Signal Transduction; Structure-Activity Relationship; Thermoanaerobacter

2008
Evaluation of the (haem)Fe--Nepsilon(2)(HisF8) bond distances from haemoglobin structures deposited in the Protein Data Bank.
    Acta crystallographica. Section D, Biological crystallography, 2008, Volume: 64, Issue:Pt 9

    Topics: Amino Acid Sequence; Crystallography, X-Ray; Databases, Protein; Heme; Hemoglobins; Histidine; Iron; Models, Structural

2008
Replacement of the axial histidine heme ligand with cysteine in nitrophorin 1: spectroscopic and crystallographic characterization.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2009, Volume: 14, Issue:2

    Topics: Circular Dichroism; Crystallography, X-Ray; Cysteine; Heme; Hemeproteins; Histidine; Ligands; Models, Molecular; Mutation; Protein Conformation; Protein Engineering; Salivary Proteins and Peptides; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman

2009
Kinetic characterization of recombinant human cystathionine beta-synthase purified from E. coli.
    Protein expression and purification, 2009, Volume: 64, Issue:2

    Topics: Catalysis; Chromatography, Affinity; Cystathionine beta-Synthase; Escherichia coli; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Pyridoxal Phosphate; Recombinant Proteins

2009
Stability of the heme Fe-N-terminal amino group coordination bond in denatured cytochrome c.
    Inorganic chemistry, 2009, Jan-05, Volume: 48, Issue:1

    Topics: Amino Acid Sequence; Aquifoliaceae; Cytochromes c; Electrons; Guanidine; Heme; Histidine; Iron; Magnetic Resonance Spectroscopy; Mutation; Nitrogen; Oxidation-Reduction; Protein Denaturation; Pseudomonas aeruginosa

2009
HisE11 and HisF8 provide bis-histidyl heme hexa-coordination in the globin domain of Geobacter sulfurreducens globin-coupled sensor.
    Journal of molecular biology, 2009, Feb-13, Volume: 386, Issue:1

    Topics: Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Databases, Protein; Electron Spin Resonance Spectroscopy; Geobacter; Globins; Heme; Histidine; Models, Molecular; Protein Structure, Quaternary; Spectrum Analysis, Raman

2009
Competition between reversible aggregation and loop formation in denatured iso-1-cytochrome c.
    Biochemistry, 2009, Jan-20, Volume: 48, Issue:2

    Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cytochromes c; Enzyme Stability; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Ligands; Models, Chemical; Molecular Sequence Data; Mutation; Protein Binding; Protein Denaturation; Protein Multimerization; Protein Renaturation; Protein Structure, Secondary; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Temperature

2009
Probing structure of heme A synthase from Bacillus subtilis by site-directed mutagenesis.
    Journal of biochemistry, 2009, Volume: 145, Issue:5

    Topics: Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Blotting, Western; Chromatography, Affinity; Chromatography, High Pressure Liquid; Cytochrome b Group; Electrophoresis, Polyacrylamide Gel; Heme; Histidine; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutant Proteins; Oligopeptides; Oxidation-Reduction; Protein Binding; Spectrum Analysis

2009
Photodissociation of isolated ferric heme and heme-His cations in an electrostatic ion storage ring.
    The journal of physical chemistry. A, 2009, Feb-26, Volume: 113, Issue:8

    Topics: Cations; Electrons; Ferric Compounds; Gases; Heme; Histidine; Kinetics; Models, Statistical; Photolysis; Static Electricity; Thermodynamics; Time Factors

2009
Why do cysteine dioxygenase enzymes contain a 3-His ligand motif rather than a 2His/1Asp motif like most nonheme dioxygenases?
    The journal of physical chemistry. A, 2009, Mar-05, Volume: 113, Issue:9

    Topics: Amino Acid Motifs; Aspartic Acid; Biocatalysis; Catalytic Domain; Cysteine; Cysteine Dioxygenase; Heme; Histidine; Humans; Ligands; Models, Chemical; Models, Molecular

2009
Over-expression and characterization of Bacillus subtilis heme O synthase.
    Journal of biochemistry, 2009, Volume: 145, Issue:5

    Topics: Alkyl and Aryl Transferases; Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Blotting, Western; Chromatography, Affinity; Chromatography, High Pressure Liquid; Conserved Sequence; Cytoplasm; Escherichia coli; Heme; Histidine; Molecular Sequence Data; Spectrum Analysis

2009
Intramolecular electron transfer processes in Cu(B)-deficient cytochrome bo studied by pulse radiolysis.
    Journal of biochemistry, 2009, Volume: 145, Issue:5

    Topics: Alanine; Amino Acid Substitution; Copper; Cytochrome b Group; Electron Transport; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Mutation; Oxidation-Reduction; Potassium Cyanide; Potentiometry; Pulse Radiolysis

2009
Design and engineering of an O(2) transport protein.
    Nature, 2009, Mar-19, Volume: 458, Issue:7236

    Topics: Biological Transport; Carbon Monoxide; Carrier Proteins; Drug Design; Globins; Glutamic Acid; Heme; Histidine; Humans; Kinetics; Ligands; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Oxygen; Protein Engineering; Protein Structure, Secondary; Rotation; Spectroscopy, Fourier Transform Infrared; Substrate Specificity; Water

2009
CcsBA is a cytochrome c synthetase that also functions in heme transport.
    Proceedings of the National Academy of Sciences of the United States of America, 2009, Jun-23, Volume: 106, Issue:25

    Topics: Amino Acid Sequence; Bacteria; Cell Membrane; Conserved Sequence; Core Binding Factors; Escherichia coli; Heme; Histidine; Imidazoles; Ligands; Lyases; Membrane Proteins; Mutation; Phylogeny; Protein Structure, Tertiary; Recombinant Proteins

2009
His protects heme as it crosses the membrane.
    Proceedings of the National Academy of Sciences of the United States of America, 2009, Jun-23, Volume: 106, Issue:25

    Topics: Biological Transport; Catalysis; Cell Membrane; Chloroplasts; Cytochromes c; Heme; Histidine

2009
Essential role of proximal histidine-asparagine interaction in mammalian peroxidases.
    The Journal of biological chemistry, 2009, Sep-18, Volume: 284, Issue:38

    Topics: Asparagine; Cell Line; Chlorides; Crystallography, X-Ray; Glycosylation; Heme; Histidine; Humans; Hypochlorous Acid; Lactoperoxidase; Leukocytes; Mutation, Missense; Oxidation-Reduction; Peroxidase; Protein Processing, Post-Translational; Protein Structure, Tertiary

2009
(1)H, (15)N, and (13)C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state.
    Biomolecular NMR assignments, 2009, Volume: 3, Issue:2

    Topics: Bacterial Proteins; Heme; Hemoglobins; Histidine; Iron; Nuclear Magnetic Resonance, Biomolecular; Protein Processing, Post-Translational; Synechococcus

2009
Stringency of the 2-His-1-Asp active-site motif in prolyl 4-hydroxylase.
    PloS one, 2009, Nov-05, Volume: 4, Issue:11

    Topics: Alanine; Amino Acid Motifs; Aspartic Acid; Carbon; Catalysis; Catalytic Domain; Collagen; Glycine; Heme; Histidine; Humans; Hydrogen; Iron; Ligands; Procollagen-Proline Dioxygenase

2009
The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron.
    Journal of the American Chemical Society, 2009, Dec-23, Volume: 131, Issue:50

    Topics: Animals; Crystallography, X-Ray; Heme; Histidine; Horses; Hydrogen Bonding; Iron; Metmyoglobin; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Myocardium; Nitrites; Oxidation-Reduction; Plasmids; Protein Binding; Protein Conformation; X-Ray Diffraction

2009
Unusual proximal heme pocket geometry in the deoxygenated Thermobifida fusca: A combined spectroscopic investigation.
    Biophysical chemistry, 2010, Volume: 147, Issue:1-2

    Topics: Actinomycetales; Animals; Crystallography, X-Ray; Heme; Hemoglobins; Histidine; Horses; Iron; Myoglobin; Spectrophotometry, Infrared

2010
Nonadiabatic histidine dissociation of hexacoordinate heme in neuroglobin protein.
    The journal of physical chemistry. A, 2010, Feb-04, Volume: 114, Issue:4

    Topics: Computer Simulation; Globins; Heme; Histidine; Models, Molecular; Monte Carlo Method; Nerve Tissue Proteins; Neuroglobin; Quantum Theory

2010
The main role of inner histidines in the molecular mechanism of myoglobin oxidation catalyzed by copper compounds.
    Inorganic chemistry, 2010, Feb-15, Volume: 49, Issue:4

    Topics: Amino Acid Substitution; Animals; Catalysis; Copper; Heme; Histidine; Hydrogen Bonding; Hydrogen Peroxide; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Oxidation-Reduction; Oxygen; Sperm Whale; Structure-Activity Relationship; Swine; Zinc

2010
Co-expression of ferrochelatase allows for complete heme incorporation into recombinant proteins produced in E. coli.
    Protein expression and purification, 2010, Volume: 73, Issue:1

    Topics: Bacterial Proteins; Carrier Proteins; Cytochrome P-450 Enzyme System; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Ferrochelatase; Heme; Hemeproteins; Histidine; Nitric Oxide Synthase; Recombinant Fusion Proteins; Spectrum Analysis; Spectrum Analysis, Raman

2010
c-Type cytochrome biogenesis can occur via a natural Ccm system lacking CcmH, CcmG, and the heme-binding histidine of CcmE.
    The Journal of biological chemistry, 2010, Jul-23, Volume: 285, Issue:30

    Topics: Amino Acid Sequence; Bacterial Proteins; Cytochromes c; Desulfovibrio desulfuricans; Escherichia coli; Gene Deletion; Genome, Bacterial; Heme; Histidine; Models, Molecular; Molecular Sequence Data; Protein Conformation; Solubility

2010
Structure and properties of a bis-histidyl ligated globin from Caenorhabditis elegans.
    Biochemistry, 2010, Jul-13, Volume: 49, Issue:27

    Topics: Animals; Caenorhabditis elegans; Cytoglobin; Globins; Heme; Hemeproteins; Histidine; Kinetics; Ligands; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Oxygen; Sensory Receptor Cells

2010
Denatured states of low-complexity polypeptide sequences differ dramatically from those of foldable sequences.
    Proceedings of the National Academy of Sciences of the United States of America, 2010, Jun-22, Volume: 107, Issue:25

    Topics: Cytochromes c; Heme; Histidine; Histones; Hydrogen-Ion Concentration; Kinetics; Molecular Conformation; Peptides; Protein Conformation; Protein Denaturation; Protein Folding; Proteins; Rhodopseudomonas; Thermodynamics

2010
Molecular insight into intrinsic heme distortion in ligand binding in hemoprotein.
    Biochemistry, 2010, Jul-13, Volume: 49, Issue:27

    Topics: Carbon Monoxide; Heme; Hemeproteins; Histidine; Iron; Ligands; Magnetic Resonance Spectroscopy; Myoglobin; Nitric Oxide; Oxygen; Water

2010
The structure of cbb3 cytochrome oxidase provides insights into proton pumping.
    Science (New York, N.Y.), 2010, Jul-16, Volume: 329, Issue:5989

    Topics: Amino Acid Sequence; Catalytic Domain; Crystallography, X-Ray; Cytoplasm; Electron Transport; Electron Transport Complex IV; Heme; Histidine; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Oxygen; Periplasm; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Proton Pumps; Protons; Pseudomonas stutzeri; Tyrosine

2010
The heme pocket of the globin domain of the globin-coupled sensor of Geobacter sulfurreducens--an EPR study.
    Journal of inorganic biochemistry, 2010, Volume: 104, Issue:10

    Topics: Bacterial Proteins; Binding Sites; Electron Spin Resonance Spectroscopy; Geobacter; Globins; Heme; Histidine; Models, Molecular; Protein Conformation; Protein Structure, Tertiary

2010
Molecular modeling and dynamics simulation of a histidine-tagged cytochrome b₅.
    Journal of molecular modeling, 2011, Volume: 17, Issue:5

    Topics: Crystallography, X-Ray; Cytochromes b5; Heme; Histidine; Hydrophobic and Hydrophilic Interactions; Ligands; Models, Chemical; Molecular Dynamics Simulation; Nuclear Magnetic Resonance, Biomolecular; Oligopeptides; Protein Structure, Secondary; Recombinant Proteins

2011
A heme fusion tag for protein affinity purification and quantification.
    Protein science : a publication of the Protein Society, 2010, Volume: 19, Issue:10

    Topics: Amino Acid Sequence; Azurin; Binding, Competitive; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Heme; Histidine; Maltose-Binding Proteins; Molecular Sequence Data; Molecular Structure; Protein Binding; Recombinant Fusion Proteins; Resins, Synthetic; Sepharose; Spectrophotometry

2010
Variation and analysis of second-sphere interactions and axial histidinate character in c-type cytochromes.
    Inorganic chemistry, 2010, Sep-06, Volume: 49, Issue:17

    Topics: Amino Acid Motifs; Bacteria; Binding Sites; Cytochromes c; Heme; Histidine; Hydrogen Bonding; Iron; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Binding

2010
Essential histidine pairs indicate conserved haem binding in epsilonproteobacterial cytochrome c haem lyases.
    Microbiology (Reading, England), 2010, Volume: 156, Issue:Pt 12

    Topics: Amino Acid Motifs; Bacterial Proteins; Binding Sites; Conserved Sequence; Heme; Histidine; Lyases; Wolinella

2010
Modification of the heme active site to increase the peroxidase activity of thermophilic cytochrome P450: a rational approach.
    Journal of inorganic biochemistry, 2010, Volume: 104, Issue:11

    Topics: Amino Acid Substitution; Binding Sites; Catalysis; Chloride Peroxidase; Cytochrome b Group; Cytochrome P-450 Enzyme System; Enzyme Stability; Glutamine; Heme; Hemeproteins; Histidine; Horseradish Peroxidase; Hydrogen Bonding; Hydrogen-Ion Concentration; Oxidation-Reduction; Peroxidases; Structure-Activity Relationship; Thermus thermophilus

2010
Structural determinants for the formation of sulfhemeprotein complexes.
    Biochemical and biophysical research communications, 2010, Oct-01, Volume: 400, Issue:4

    Topics: Animals; Heme; Histidine; Humans; Hydrogen Sulfide; Oxygen; Spectrum Analysis, Raman; Sulfhemoglobin; Water; Whales

2010
Intramolecular heme ligation of the cytochrome P450 2C9 R108H mutant demonstrates pronounced conformational flexibility of the B-C loop region: implications for substrate binding.
    Biochemistry, 2010, Oct-12, Volume: 49, Issue:40

    Topics: Animals; Aryl Hydrocarbon Hydroxylases; Chromatography, Gel; Cytochrome P-450 CYP2C9; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Histidine; Humans; Molecular Dynamics Simulation; Mutant Proteins; Mutation; Protein Binding; Protein Conformation; Rabbits; Spectrophotometry, Ultraviolet; Substrate Specificity

2010
Absorption in the Q-band region by isolated ferric heme+ and heme+(histidine) in vacuo.
    The Journal of chemical physics, 2010, Aug-28, Volume: 133, Issue:8

    Topics: Algorithms; Anions; Cations; Ferric Compounds; Glycine; Heme; Hemeproteins; Histidine; Hydrophobic and Hydrophilic Interactions; Methanol; Methylene Chloride; Models, Chemical; Solvents; Spectrum Analysis; Static Electricity; Vacuum; Water

2010
Short circuiting a sulfite oxidising enzyme with direct electrochemistry: active site substitutions and their effect on catalysis and electron transfer.
    Biochimica et biophysica acta, 2011, Volume: 1807, Issue:1

    Topics: Amino Acid Substitution; Arginine; Catalytic Domain; Crystallography, X-Ray; Electrochemistry; Electron Transport; Genetic Variation; Heme; Histidine; Hydrogen-Ion Concentration; Models, Molecular; Oxidation-Reduction; Protein Conformation; Sulfite Dehydrogenase

2011
Functional importance of tyrosine 294 and the catalytic selectivity for the bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine .
    Biochemistry, 2010, Nov-16, Volume: 49, Issue:45

    Topics: Ferric Compounds; Ferrous Compounds; Heme; Histidine; Ligands; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Protein Conformation; Protein Precursors; Quinolines; Smad1 Protein; Spectrum Analysis, Raman; Tyrosine

2010
Compound ES of dehaloperoxidase decays via two alternative pathways depending on the conformation of the distal histidine.
    Journal of the American Chemical Society, 2010, Dec-15, Volume: 132, Issue:49

    Topics: Animals; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Hemoglobins; Histidine; Hydrogen Peroxide; Kinetics; Models, Molecular; Molecular Conformation; Peroxidases; Polychaeta; Protein Conformation

2010
Axial ligation of the high-potential heme center in an Arabidopsis cytochrome b561.
    FEBS letters, 2011, Feb-04, Volume: 585, Issue:3

    Topics: Amino Acid Substitution; Arabidopsis; Arabidopsis Proteins; Cytochrome b Group; Electron Spin Resonance Spectroscopy; Heme; Histidine; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins; Oxidation-Reduction; Recombinant Proteins; Spectrophotometry; Spectrum Analysis, Raman; Vacuoles

2011
Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: covalent heme attachment and bishistidine coordination.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2011, Volume: 16, Issue:4

    Topics: Heme; Hemoglobins; Histidine; Hydrogen Peroxide; Models, Molecular; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Synechococcus; Synechocystis

2011
Unusual flexibility of distal and proximal histidine residues in the haem pocket of Drosophila melanogaster haemoglobin.
    Metallomics : integrated biometal science, 2009, Volume: 1, Issue:3

    Topics: Animals; Drosophila melanogaster; Drosophila Proteins; Electron Spin Resonance Spectroscopy; Globins; Heme; Histidine; Hydrogen-Ion Concentration; Spectrophotometry, Ultraviolet

2009
Reduction potential of yeast cytochrome c peroxidase and three distal histidine mutants: dependence on pH.
    Journal of inorganic biochemistry, 2011, Volume: 105, Issue:4

    Topics: Binding Sites; Cytochrome-c Peroxidase; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Mutation; Saccharomyces cerevisiae

2011
Protonation of histidine 55 affects the oxygen access to heme in the alpha chain of the hemoglobin from the Antarctic fish Trematomus bernacchii.
    IUBMB life, 2011, Volume: 63, Issue:3

    Topics: Animals; Antarctic Regions; Heme; Hemoglobins; Histidine; Models, Molecular; Oxygen; Protons

2011
Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from Campylobacter jejuni.
    Biochemistry, 2011, May-17, Volume: 50, Issue:19

    Topics: Bacterial Proteins; Campylobacter jejuni; Glycine; Heme; Histidine; Hydrogen Bonding; Ligands; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Oxygen; Protein Binding; Spectrum Analysis, Raman; Truncated Hemoglobins; Tryptophan; Tyrosine

2011
Cobalt cystathionine β-synthase: a cobalt-substituted heme protein with a unique thiolate ligation motif.
    Inorganic chemistry, 2011, May-16, Volume: 50, Issue:10

    Topics: Circular Dichroism; Cloning, Molecular; Cobalt; Coordination Complexes; Cystathionine beta-Synthase; Cysteine; Escherichia coli; Heme; Hemeproteins; Histidine; Humans; Hydrogen-Ion Concentration; Ligands; Models, Molecular; Oxidation-Reduction; Protein Binding; Protein Structure, Tertiary; Pyridoxal Phosphate; Recombinant Proteins; Spectrophotometry, Atomic

2011
Heme binding to the second, lower-affinity site of the global iron regulator Irr from Rhizobium leguminosarum promotes oligomerization.
    The FEBS journal, 2011, Volume: 278, Issue:12

    Topics: Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins; Binding Sites; Electron Spin Resonance Spectroscopy; Heme; Histidine; Iron; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Multimerization; Protein Structure, Quaternary; Recombinant Proteins; Rhizobium leguminosarum; Spectrophotometry; Transcription Factors

2011
Multifrequency electron paramagnetic resonance characterization of PpoA, a CYP450 fusion protein that catalyzes fatty acid dioxygenation.
    Journal of the American Chemical Society, 2011, Jun-15, Volume: 133, Issue:23

    Topics: Biocatalysis; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Fatty Acids; Free Radicals; Heme; Histidine; Mutation; Oxygen; Recombinant Fusion Proteins; Tyrosine

2011
Highly selective ligand binding by Methylophilus methylotrophus cytochrome c''.
    Biochemistry, 2011, Jun-28, Volume: 50, Issue:25

    Topics: Bacterial Proteins; Cytochromes c; Diatoms; Disulfides; Ferrous Compounds; Heme; Histidine; Ligands; Methylophilus methylotrophus; Nitric Oxide; Oxidation-Reduction; Protein Binding

2011
Electron transfer function versus oxygen delivery: a comparative study for several hexacoordinated globins across the animal kingdom.
    PloS one, 2011, Volume: 6, Issue:6

    Topics: Amino Acid Sequence; Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Carbon Monoxide; Cytochromes c; Cytoglobin; Electron Transport; Globins; Heme; Histidine; Humans; Iron; Kinetics; Nerve Tissue Proteins; Neuroglobin; Oxygen; Protein Structure, Quaternary; Protein Structure, Tertiary

2011
The origin of the Fe(IV)=O intermediates in cytochrome aa(3) oxidase.
    Biochimica et biophysica acta, 2012, Volume: 1817, Issue:4

    Topics: Bacillus subtilis; Bacterial Proteins; Binding Sites; Biological Transport; Electron Transport; Electron Transport Complex IV; Ferric Compounds; Heme; Histidine; Hydrogen Peroxide; Iron; Models, Chemical; Models, Molecular; Molecular Structure; Oxidation-Reduction; Oxygen; Protein Conformation; Protons; Spectrum Analysis, Raman

2012
Crystallographic trapping of heme loss intermediates during the nitrite-induced degradation of human hemoglobin.
    Biochemistry, 2011, Oct-04, Volume: 50, Issue:39

    Topics: Crystallography, X-Ray; Heme; Hemoglobins; Histidine; Humans; Models, Molecular; Nitrites

2011
Breaking the proximal Fe(II)-N(His) bond in heme proteins through local structural tension: lessons from the heme b proteins nitrophorin 4, nitrophorin 7, and related site-directed mutant proteins.
    Biochemistry, 2011, Oct-11, Volume: 50, Issue:40

    Topics: Animals; Binding Sites; Ferrous Compounds; Heme; Hemeproteins; Histidine; Humans; Mutagenesis, Site-Directed; Mutant Proteins; Protein Binding; Salivary Proteins and Peptides

2011
Heme binding in gas-phase holo-myoglobin cations: distal becomes proximal?
    Journal of the American Society for Mass Spectrometry, 2011, Volume: 22, Issue:10

    Topics: Amino Acid Sequence; Animals; Binding Sites; Cations; Heme; Histidine; Horses; Models, Molecular; Molecular Sequence Data; Myoglobin; Protein Binding; Spectrometry, Mass, Electrospray Ionization

2011
Dynamic water networks in cytochrome cbb3 oxidase.
    Biochimica et biophysica acta, 2012, Volume: 1817, Issue:5

    Topics: Electron Transport Complex IV; Glutamine; Heme; Histidine; Hydrogen Bonding; Kinetics; Models, Molecular; Potassium Channels; Protons; Pseudomonas stutzeri; Water

2012
Manipulating the proximal triad His-Asn-Arg in human myeloperoxidase.
    Archives of biochemistry and biophysics, 2011, Dec-01, Volume: 516, Issue:1

    Topics: Amino Acid Substitution; Arginine; Asparagine; Binding Sites; Cell Line; Cloning, Molecular; Ferric Compounds; Ferrous Compounds; Heme; Histidine; Humans; Models, Molecular; Mutant Proteins; Oxidation-Reduction; Peroxidase

2011
Probing the dynamics of a His73-heme alkaline transition in a destabilized variant of yeast iso-1-cytochrome c with conformationally gated electron transfer methods.
    Biochemistry, 2011, Nov-22, Volume: 50, Issue:46

    Topics: Cytochromes c1; Electron Transport; Heme; Histidine; Hydrogen-Ion Concentration; Models, Molecular; Mutation; Oxidation-Reduction; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics

2011
An enlarged, adaptable active site in CYP164 family P450 enzymes, the sole P450 in Mycobacterium leprae.
    Antimicrobial agents and chemotherapy, 2012, Volume: 56, Issue:1

    Topics: Antifungal Agents; Bacterial Proteins; Binding Sites; Catalytic Domain; Conserved Sequence; Crystallography, X-Ray; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Econazole; Heme; Histidine; Humans; Iron; Kinetics; Leprosy; Models, Molecular; Mycobacterium Infections, Nontuberculous; Mycobacterium leprae; Mycobacterium smegmatis; Porphyrins; Protein Binding; Protein Structure, Secondary

2012
Heme ligand identification and redox properties of the cytochrome c synthetase, CcmF.
    Biochemistry, 2011, Dec-20, Volume: 50, Issue:50

    Topics: Amino Acid Substitution; Binding Sites; Biocatalysis; Enzyme Activation; Escherichia coli Proteins; Heme; Histidine; Holoenzymes; Imidazoles; Indicators and Reagents; Ligands; Lyases; Models, Molecular; Mutant Proteins; Oxidation-Reduction; Phylogeny; Protein Conformation; Protein Subunits; Recombinant Proteins; Spectrum Analysis, Raman

2011
Effects of the bHLH domain on axial coordination of heme in the PAS-A domain of neuronal PAS domain protein 2 (NPAS2): conversion from His119/Cys170 coordination to His119/His171 coordination.
    Journal of inorganic biochemistry, 2012, Volume: 108

    Topics: Cysteine; Heme; Histidine; Protein Structure, Tertiary; Transcription Factors

2012
Significant increase of oxidase activity through the genetic incorporation of a tyrosine-histidine cross-link in a myoglobin model of heme-copper oxidase.
    Angewandte Chemie (International ed. in English), 2012, Apr-27, Volume: 51, Issue:18

    Topics: Catalytic Domain; Electrophoresis, Polyacrylamide Gel; Heme; Histidine; Models, Biological; Myoglobin; Oxidoreductases; Tyrosine; Up-Regulation

2012
Is histidine dissociation a critical component of the NO/H-NOX signaling mechanism? Insights from X-ray absorption spectroscopy.
    Dalton transactions (Cambridge, England : 2003), 2012, Jul-14, Volume: 41, Issue:26

    Topics: Binding Sites; Ferrous Compounds; Guanylate Cyclase; Heme; Histidine; Hydrogen Bonding; Nitric Oxide; Protein Structure, Tertiary; Pseudoalteromonas; Receptors, Cytoplasmic and Nuclear; Shewanella; Signal Transduction; Soluble Guanylyl Cyclase; Thermoanaerobacter; X-Ray Absorption Spectroscopy

2012
Induced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO).
    Proceedings of the National Academy of Sciences of the United States of America, 2012, Apr-10, Volume: 109, Issue:15

    Topics: Apoproteins; Bacterial Proteins; Cytoplasm; Heme; Heme Oxygenase (Decyclizing); Histidine; Kinetics; Models, Biological; Mutant Proteins; Porphyrins; Protein Binding; Protein Structure, Secondary; Proteolysis; Pseudomonas aeruginosa; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrum Analysis; Surface Plasmon Resonance; Thermodynamics

2012
Structural characterization of spectroscopic substates in carbonmonoxy neuroglobin.
    Faraday discussions, 2011, Volume: 150

    Topics: Animals; Carbon Monoxide; Chemistry, Physical; Globins; Heme; Histidine; Humans; Hydrogen Bonding; Mice; Molecular Dynamics Simulation; Myoglobin; Nerve Tissue Proteins; Neuroglobin; Protein Conformation; Protons; Quantum Theory; Spectrophotometry, Infrared; Stereoisomerism; Thermodynamics

2011
QM/MM study on the catalytic mechanism of heme-containing aliphatic aldoxime dehydratase.
    The journal of physical chemistry. B, 2012, May-17, Volume: 116, Issue:19

    Topics: Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Electrons; Heme; Histidine; Hydro-Lyases; Hydrogen; Hydrogen Bonding; Iron; Models, Molecular; Molecular Structure; Nitrogen; Oxygen; Protein Conformation; Protons; Quantum Theory; Rotation; Serine; Water

2012
Structural dynamics of proximal heme pocket in HemAT-Bs associated with oxygen dissociation.
    Biochimica et biophysica acta, 2012, Volume: 1824, Issue:7

    Topics: Bacillus subtilis; Bacterial Proteins; Carbon Monoxide; Escherichia coli; Gene Expression; Heme; Heme-Binding Proteins; Hemeproteins; Histidine; Iron; Kinetics; Oxygen; Protein Structure, Tertiary; Recombinant Fusion Proteins; Signal Transduction; Spectrum Analysis, Raman

2012
Amino acid sequence of myoglobin from white-tailed deer (Odocoileus virginianus).
    Meat science, 2012, Volume: 92, Issue:2

    Topics: Amino Acid Sequence; Amino Acids; Animals; Deer; Dietary Proteins; Heme; Histidine; Meat; Molecular Sequence Data; Myocardium; Myoglobin; Ruminants; Sequence Analysis, Protein

2012
Chemical rescue of the distal histidine mutants of tryptophan 2,3-dioxygenase.
    Journal of the American Chemical Society, 2012, Jul-25, Volume: 134, Issue:29

    Topics: Binding Sites; Catalytic Domain; Cupriavidus; Heme; Histidine; Imidazoles; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Substrate Specificity; Tryptophan Oxygenase

2012
Influence of heme post-translational modification and distal ligation on the backbone dynamics of a monomeric hemoglobin.
    Biochemistry, 2012, Jul-24, Volume: 51, Issue:29

    Topics: Bacterial Proteins; Carbon Monoxide; Cyanides; Heme; Histidine; Molecular Dynamics Simulation; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Conformation; Protein Processing, Post-Translational; Synechococcus; Truncated Hemoglobins

2012
Novel FixL homologues in Chlamydomonas reinhardtii bind heme and O(2).
    FEBS letters, 2012, Dec-14, Volume: 586, Issue:24

    Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Chlamydomonas reinhardtii; Escherichia coli; Genome, Bacterial; Heme; Hemeproteins; Histidine; Histidine Kinase; Molecular Sequence Data; Mutation; Oxygen; Phosphorylation; Spectrophotometry

2012
The role of the distal histidine in H2O2 activation and heme protection in both peroxidase and globin functions.
    The journal of physical chemistry. B, 2012, Oct-11, Volume: 116, Issue:40

    Topics: Biocatalysis; Chlorophenols; Heme; Hemoglobin A; Histidine; Hydrogen Peroxide; Models, Molecular; Molecular Structure; Mutation; Oxidation-Reduction; Peroxidases; Quinones

2012
Geometric and electronic structures of the His-Fe(IV)=O and His-Fe(IV)-Tyr hemes of MauG.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2012, Volume: 17, Issue:8

    Topics: Absorptiometry, Photon; Cross-Linking Reagents; Electrons; Heme; Histidine; Iron; Kinetics; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Protein Binding; Protein Processing, Post-Translational; Quantum Theory; Tyrosine

2012
Detection and identification of heme c-modified peptides by histidine affinity chromatography, high-performance liquid chromatography-mass spectrometry, and database searching.
    Journal of proteome research, 2012, Dec-07, Volume: 11, Issue:12

    Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Bacterial Proteins; Betaproteobacteria; Cattle; Chromatography, Affinity; Chromatography, High Pressure Liquid; Cytochromes c; Databases, Protein; Escherichia coli; Heme; Histidine; Ions; Molecular Sequence Data; Peptide Mapping; Peptides; Search Engine; Signal-To-Noise Ratio; Tandem Mass Spectrometry

2012
Spectroscopic evidence of the role of an axial ligand histidinate in the mechanism of adrenal cytochrome b561.
    Biochemistry, 2012, Nov-06, Volume: 51, Issue:44

    Topics: Adrenal Glands; Ascorbic Acid; Chromaffin Granules; Cytochromes b; Electron Spin Resonance Spectroscopy; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Oxidation-Reduction; Spectrum Analysis

2012
His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosis.
    Journal of the American Chemical Society, 2012, Nov-21, Volume: 134, Issue:46

    Topics: Apoptosis; Circular Dichroism; Cytochromes c; Heme; Histidine; Models, Molecular; Protons; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman

2012
Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.
    FEBS letters, 2012, Dec-14, Volume: 586, Issue:24

    Topics: Bacterial Proteins; Heme; Heme-Binding Proteins; Hemeproteins; Histidine; Indolequinones; Ligands; Lysine; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Peroxides; Protein Processing, Post-Translational; Spectrophotometry; Tryptophan; Tyrosine

2012
Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2013, Volume: 18, Issue:1

    Topics: Cyanides; Disulfides; Dithiothreitol; Globins; Heme; Histidine; Humans; Kinetics; Ligands; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Protein Binding; Protein Structure, Secondary

2013
Human mitochondrial holocytochrome c synthase's heme binding, maturation determinants, and complex formation with cytochrome c.
    Proceedings of the National Academy of Sciences of the United States of America, 2013, Feb-26, Volume: 110, Issue:9

    Topics: Amino Acid Sequence; Bacterial Proteins; Cytochromes c; Heme; Histidine; Humans; Ligands; Lyases; Mitochondria; Models, Molecular; Molecular Sequence Data; Protein Binding; Rhodobacter capsulatus; Spectrophotometry, Ultraviolet

2013
Conformational properties of polyglutamine sequences in guanidine hydrochloride solutions.
    Biophysical journal, 2012, Nov-07, Volume: 103, Issue:9

    Topics: Alanine; Amino Acid Sequence; Cytochromes c; Guanidine; Heme; Histidine; Lysine; Molecular Sequence Data; Mutagenesis, Insertional; Peptides; Protein Denaturation; Protein Stability; Protein Structure, Tertiary

2012
Probing the conformational mobility of the active site of a heme peroxidase.
    Dalton transactions (Cambridge, England : 2003), 2013, Mar-07, Volume: 42, Issue:9

    Topics: Ascorbate Peroxidases; Catalytic Domain; Glycine max; Heme; Histidine; Models, Molecular; Mutagenesis, Site-Directed; Mutation

2013
Dynamic factors affecting gaseous ligand binding in an artificial oxygen transport protein.
    Biochemistry, 2013, Jan-22, Volume: 52, Issue:3

    Topics: Binding Sites; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Globins; Glutamic Acid; Heme; Histidine; Kinetics; Ligands; Mutant Proteins; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Oxygen; Protein Binding; Protein Conformation; Protein Engineering; Protein Folding; Recombinant Proteins; Water

2013
Signal transduction and phosphoryl transfer by a FixL hybrid kinase with low oxygen affinity: importance of the vicinal PAS domain and receiver aspartate.
    Biochemistry, 2013, Jan-22, Volume: 52, Issue:3

    Topics: Amino Acid Substitution; Aspartic Acid; Bacterial Proteins; Heme; Hemeproteins; Histidine; Histidine Kinase; Kinetics; Ligands; Mutant Proteins; Oxidation-Reduction; Oxygen; Peptide Fragments; Phosphorylation; Protein Binding; Protein Interaction Domains and Motifs; Protein Processing, Post-Translational; Protein Serine-Threonine Kinases; Recombinant Proteins; Rhizobium; Signal Transduction

2013
A cytochrome C electron transfer switch modulated by heme ligation and isomerization of a peptidyl-prolyl bond.
    Biopolymers, 2013, Volume: 100, Issue:1

    Topics: Cytochromes c; Electrons; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligation; Protein Conformation

2013
Picosecond binding of the His ligand to four-coordinate heme in cytochrome c': a one-way gate for releasing proximal NO.
    Journal of the American Chemical Society, 2013, Feb-27, Volume: 135, Issue:8

    Topics: Cytochromes c; Heme; Histidine; Ligands; Models, Molecular; Nitric Oxide; Protein Binding; Spectrum Analysis

2013
The Porphyromonas gingivalis HmuY haemophore binds gallium(iii), zinc(ii), cobalt(iii), manganese(iii), nickel(ii), and copper(ii) protoporphyrin IX but in a manner different to iron(iii) protoporphyrin IX.
    Metallomics : integrated biometal science, 2013, Volume: 5, Issue:4

    Topics: Absorption; Bacterial Proteins; Circular Dichroism; Cobalt; Copper; Gallium; Heme; Hemeproteins; Histidine; Ligands; Magnetic Resonance Spectroscopy; Manganese; Metals; Mutant Proteins; Nickel; Porphyromonas gingivalis; Protein Binding; Protoporphyrins; Spectrophotometry, Ultraviolet; Zinc

2013
Comparative analysis of inner cavities and ligand migration in non-symbiotic AHb1 and AHb2.
    Biochimica et biophysica acta, 2013, Volume: 1834, Issue:9

    Topics: Arabidopsis; Arabidopsis Proteins; Heme; Hemoglobins; Histidine; Kinetics; Models, Molecular; Nitric Oxide; Oxygen; Protein Binding; Protein Conformation

2013
Effects of local protein environment on the binding of diatomic molecules to heme in myoglobins. DFT and dispersion-corrected DFT studies.
    Journal of molecular modeling, 2013, Volume: 19, Issue:8

    Topics: Amino Acid Motifs; Binding Sites; Carbon Monoxide; Heme; Histidine; Humans; Hydrogen Bonding; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Myoglobin; Oxygen; Protein Binding; Quantum Theory; Thermodynamics

2013
Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG.
    Proceedings of the National Academy of Sciences of the United States of America, 2013, Jun-11, Volume: 110, Issue:24

    Topics: Catalysis; Enzyme Precursors; Ferric Compounds; Heme; Hemeproteins; Histidine; Indolequinones; Models, Chemical; Models, Molecular; Molecular Structure; Mutation; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Protein Processing, Post-Translational; Spectroscopy, Near-Infrared; Tryptophan; Tyrosine

2013
The protein effect in the structure of two ferryl-oxo intermediates at the same oxidation level in the heme copper binuclear center of cytochrome c oxidase.
    The Journal of biological chemistry, 2013, Jul-12, Volume: 288, Issue:28

    Topics: Bacterial Proteins; Copper; Electron Transport Complex IV; Heme; Histidine; Hydrogen Bonding; Iron; Oxidation-Reduction; Oxygen; Oxygen Isotopes; Paracoccus denitrificans; Peroxides; Spectrum Analysis, Raman

2013
Kinetics of reversible reductive carbonylation of heme in human cystathionine β-synthase.
    Biochemistry, 2013, Jul-02, Volume: 52, Issue:26

    Topics: Carbon Monoxide; Cystathionine beta-Synthase; Cysteine; Heme; Histidine; Humans; Kinetics; Ligands; Oxygen; Protein Binding; Protein Carbonylation; Signal Transduction; Spectrum Analysis, Raman; Sulfur Dioxide; Superoxides

2013
The role of T56 in controlling the flexibility of the distal histidine in dehaloperoxidase-hemoglobin from Amphitrite ornata.
    Biochimica et biophysica acta, 2013, Volume: 1834, Issue:10

    Topics: Animals; Biocatalysis; Heme; Hemoglobins; Histidine; Iron; Kinetics; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Peroxidases; Polychaeta; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Thermodynamics; Threonine

2013
Dynamics of the His79-heme alkaline transition of yeast iso-1-cytochrome c probed by conformationally gated electron transfer with Co(II)bis(terpyridine).
    Journal of the American Chemical Society, 2013, Aug-28, Volume: 135, Issue:34

    Topics: Alkalies; Cytochromes c1; Electron Transport; Heme; Histidine; Hydrogen-Ion Concentration; Models, Molecular; Mutation; Organometallic Compounds; Saccharomyces cerevisiae; Thermodynamics

2013
Investigations of heme ligation and ligand switching in cytochromes p450 and p420.
    Biochemistry, 2013, Aug-27, Volume: 52, Issue:34

    Topics: Camphor 5-Monooxygenase; Carbon Monoxide; Cytochrome P-450 Enzyme System; Heme; Histidine; Ligands; Models, Molecular; Myoglobin; Protein Conformation; Spectrum Analysis, Raman

2013
Crystal structures of α-dioxygenase from Oryza sativa: insights into substrate binding and activation by hydrogen peroxide.
    Protein science : a publication of the Protein Society, 2013, Volume: 22, Issue:10

    Topics: Arginine; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Dioxygenases; Enzyme Activation; Heme; Histidine; Hydrogen Peroxide; Models, Molecular; Oryza; Palmitic Acid; Plant Proteins; Protein Structure, Tertiary; Substrate Specificity

2013
Electrochemical determination of heme-linked pKa values and the importance of using fluoride binding in heme proteins.
    Analytical biochemistry, 2013, Dec-01, Volume: 443, Issue:1

    Topics: Animals; Binding Sites; Electrochemical Techniques; Electron Transport; Fluorides; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Muscle, Skeletal; Myoglobin; Oxidation-Reduction; Protein Binding; Protons; Spectrophotometry; Thermodynamics

2013
Intersubunit communication via changes in hemoglobin quaternary structures revealed by time-resolved resonance Raman spectroscopy: direct observation of the Perutz mechanism.
    The journal of physical chemistry. B, 2013, Oct-17, Volume: 117, Issue:41

    Topics: Carbon Monoxide; Heme; Hemoglobins; Histidine; Humans; Iron; Models, Molecular; Nickel; Protein Structure, Quaternary; Protein Subunits; Spectrum Analysis, Raman; Time Factors

2013
How does catalase release nitric oxide? A computational structure-activity relationship study.
    Journal of chemical information and modeling, 2013, Nov-25, Volume: 53, Issue:11

    Topics: Asparagine; Catalase; Catalytic Domain; Glycine; Heme; Histidine; Humans; Hydrogen Bonding; Hydroxyurea; Isoenzymes; Kinetics; Molecular Docking Simulation; Molecular Dynamics Simulation; Nitric Oxide; Structure-Activity Relationship; Thermodynamics

2013
Electronic control of discrimination between O2 and CO in myoglobin lacking the distal histidine residue.
    Inorganic chemistry, 2014, Jan-21, Volume: 53, Issue:2

    Topics: Animals; Carbon Monoxide; Electrons; Heme; Histidine; Mutant Proteins; Mutation; Myoglobin; Oxygen; Substrate Specificity; Vibration

2014
The CcmFH complex is the system I holocytochrome c synthetase: engineering cytochrome c maturation independent of CcmABCDE.
    Molecular microbiology, 2014, Volume: 91, Issue:5

    Topics: Amino Acid Sequence; Amino Acid Substitution; Conserved Sequence; Cysteine; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Lyases; Molecular Sequence Data; Multiprotein Complexes; Protein Engineering

2014
The ferrous-dioxy complex of Leishmania major globin coupled heme containing adenylate cyclase: the role of proximal histidine on its stability.
    Biochimica et biophysica acta, 2014, Volume: 1844, Issue:3

    Topics: Adenylyl Cyclases; Enzyme Stability; Ferrous Compounds; Globins; Heme; Histidine; Kinetics; Leishmania major; Models, Molecular; Mutagenesis, Site-Directed

2014
Identification and characterization of the 'missing' terminal enzyme for siroheme biosynthesis in α-proteobacteria.
    Molecular microbiology, 2014, Volume: 92, Issue:1

    Topics: Bacterial Proteins; Catalytic Domain; Crystallography, X-Ray; Ferrochelatase; Heme; Histidine; Models, Molecular; Mutation; Paracoccus pantotrophus; Protein Structure, Tertiary

2014
Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis.
    Organic letters, 2014, Apr-18, Volume: 16, Issue:8

    Topics: Betaine; Catalysis; Cysteine; Cysteine Dioxygenase; Heme; Histidine; Humans; Methylhistidines; Models, Biological; Molecular Structure; Mycobacterium smegmatis; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction

2014
The structure of a class 3 nonsymbiotic plant haemoglobin from Arabidopsis thaliana reveals a novel N-terminal helical extension.
    Acta crystallographica. Section D, Biological crystallography, 2014, Volume: 70, Issue:Pt 5

    Topics: Arabidopsis Proteins; Binding Sites; Circular Dichroism; Crystallography, X-Ray; Heme; Hemoglobins; Histidine; Hydrogen Bonding; Ligands; Models, Molecular; Protein Conformation; Protein Multimerization

2014
Affinity purification of heme-tagged proteins.
    Methods in molecular biology (Clifton, N.J.), 2014, Volume: 1177

    Topics: Chromatography, Affinity; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Heme; Histidine; Molecular Biology; Protein Biosynthesis; Recombinant Fusion Proteins

2014
Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase.
    Science (New York, N.Y.), 2014, Jul-11, Volume: 345, Issue:6193

    Topics: Crystallography, X-Ray; Cytochrome-c Peroxidase; Heme; Histidine; Iron; Neutron Diffraction; Neutrons; Oxygen; Protons

2014
Structural and functional characterization of a cytochrome P450 2B4 F429H mutant with an axial thiolate-histidine hydrogen bond.
    Biochemistry, 2014, Aug-12, Volume: 53, Issue:31

    Topics: Amino Acid Substitution; Aryl Hydrocarbon Hydroxylases; Binding Sites; Crystallography, X-Ray; Cytochrome P450 Family 2; Cytochromes b5; Electron Transport; Heme; Histidine; Hydrogen Bonding; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Phenylalanine; Protein Conformation; Recombinant Proteins; Structural Homology, Protein; Substrate Specificity; Thermodynamics

2014
Systematic tuning of heme redox potentials and its effects on O2 reduction rates in a designed oxidase in myoglobin.
    Journal of the American Chemical Society, 2014, Aug-27, Volume: 136, Issue:34

    Topics: Alanine; Animals; Binding Sites; Biocatalysis; Copper; Electron Transport Complex IV; Heme; Histidine; Hydrogen Bonding; Male; Models, Molecular; Myoglobin; Oxidation-Reduction; Oxygen; Protein Engineering; Serine; Spermatozoa; Whales

2014
The crystal structure of siroheme decarboxylase in complex with iron-uroporphyrin III reveals two essential histidine residues.
    Journal of molecular biology, 2014, Sep-23, Volume: 426, Issue:19

    Topics: Amino Acid Sequence; Bacteria; Bacterial Proteins; Binding Sites; Carboxy-Lyases; Catalytic Domain; Decarboxylation; Heme; Histidine; Iron; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding; Sequence Alignment; Uroporphyrins

2014
Identification of essential histidine residues involved in heme binding and Hemozoin formation in heme detoxification protein from Plasmodium falciparum.
    Scientific reports, 2014, Aug-20, Volume: 4

    Topics: Binding Sites; Catalytic Domain; Dimerization; Heme; Hemeproteins; Histidine; Plasmodium falciparum; Protein Binding; Protozoan Proteins; Recombinant Proteins; Spectrum Analysis, Raman

2014
Mechanisms of mitochondrial holocytochrome c synthase and the key roles played by cysteines and histidine of the heme attachment site, Cys-XX-Cys-His.
    The Journal of biological chemistry, 2014, Oct-17, Volume: 289, Issue:42

    Topics: Binding Sites; Catalytic Domain; Conserved Sequence; Cysteine; Cytochromes c; Escherichia coli; Heme; Histidine; Humans; Ligands; Lyases; Mitochondria; Oligonucleotides; Plasmids; Protein Folding; Pyridines; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Sulfhydryl Compounds

2014
Key roles of Arg(5), Tyr(10) and his residues in Aβ-heme peroxidase: relevance to Alzheimer's disease.
    Biochemical and biophysical research communications, 2014, Sep-26, Volume: 452, Issue:3

    Topics: Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Animals; Arginine; Heme; Histidine; Humans; Mice; Molecular Sequence Data; Mutation; Oxidation-Reduction; Peptide Fragments; Peroxidases; Solutions; Tyrosine

2014
Structural insights into the role of iron-histidine bond cleavage in nitric oxide-induced activation of H-NOX gas sensor proteins.
    Proceedings of the National Academy of Sciences of the United States of America, 2014, Oct-07, Volume: 111, Issue:40

    Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Heme; Hemeproteins; Histidine; Iron; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mutation; Nitric Oxide; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Shewanella; Spectrophotometry, Atomic

2014
Introduction of a covalent histidine-heme linkage in a hemoglobin: a promising tool for heme protein engineering.
    Journal of inorganic biochemistry, 2014, Volume: 141

    Topics: Amino Acid Substitution; Bacterial Proteins; Chlamydomonas; Escherichia coli; Gene Expression; Heme; Histidine; Models, Molecular; Mutagenesis, Site-Directed; Plant Proteins; Protein Engineering; Protein Structure, Secondary; Protein Structure, Tertiary; Protoporphyrins; Recombinant Proteins; Synechococcus; Synechocystis; Truncated Hemoglobins

2014
The extracellular heme-binding protein HbpS from the soil bacterium Streptomyces reticuli is an aquo-cobalamin binder.
    The Journal of biological chemistry, 2014, Dec-05, Volume: 289, Issue:49

    Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Binding, Competitive; Biological Transport; Carrier Proteins; Escherichia coli; Evolution, Molecular; Gene Expression; Heme; Heme-Binding Proteins; Hemeproteins; Histidine; Iron; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Protein Binding; Recombinant Proteins; Sequence Alignment; Soil Microbiology; Streptomyces; Structural Homology, Protein; Vitamin B 12

2014
Significantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by nonaxial histidine to heme (vinyl) in synechocystis hemoglobin.
    The Journal of biological chemistry, 2015, Jan-23, Volume: 290, Issue:4

    Topics: Amino Acid Sequence; Calorimetry, Differential Scanning; Circular Dichroism; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Myoglobin; Protein Engineering; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Synechocystis; Truncated Hemoglobins

2015
Methionine ligand lability of homologous monoheme cytochromes c.
    Inorganic chemistry, 2015, Jan-05, Volume: 54, Issue:1

    Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins; Cytochromes c; Electrochemical Techniques; Electrodes; Escherichia coli; Gene Expression; Heme; Histidine; Kinetics; Ligands; Methionine; Molecular Sequence Data; Nitrosomonas europaea; Oxidation-Reduction; Protein Folding; Pseudomonas aeruginosa; Recombinant Proteins; Sequence Alignment; Shewanella; Temperature; Thermodynamics

2015
Exploring the mechanisms of the reductase activity of neuroglobin by site-directed mutagenesis of the heme distal pocket.
    Biochemistry, 2015, Jan-27, Volume: 54, Issue:3

    Topics: Binding Sites; Globins; Heme; Histidine; Humans; Kinetics; Mutagenesis, Site-Directed; Mutant Proteins; Myoglobin; Nerve Tissue Proteins; Neuroglobin; Nitrite Reductases; Nitrites; Oxidation-Reduction

2015
Motion of proximal histidine and structural allosteric transition in soluble guanylate cyclase.
    Proceedings of the National Academy of Sciences of the United States of America, 2015, Apr-07, Volume: 112, Issue:14

    Topics: Allosteric Site; Animals; Cattle; Guanylate Cyclase; Heme; Hemoglobins; Histidine; Iron; Molecular Conformation; Nitric Oxide; Protein Binding; Receptors, Cytoplasmic and Nuclear; Signal Transduction; Soluble Guanylyl Cyclase; Spectrophotometry; Time Factors

2015
Cloning, expression and functional characterization of heme detoxification protein (HDP) from the rodent malaria parasite Plasmodium vinckei.
    Gene, 2015, Jul-15, Volume: 566, Issue:1

    Topics: Amino Acid Sequence; Antimalarials; Cloning, Molecular; Gene Expression; Heme; Hemeproteins; Histidine; Molecular Sequence Data; Phylogeny; Plasmodium; Protozoan Proteins; Sequence Alignment

2015
Properties of Hemoglobin Decolorized with a Histidine-Specific Protease.
    Journal of food science, 2015, Volume: 80, Issue:6

    Topics: Animals; Aspartic Acid Endopeptidases; Aspergillus niger; Blood Proteins; Color; Endopeptidases; Food Handling; Heme; Hemoglobins; Histidine; Hydrolysis; Meat; Subtilisins; Swine

2015
Structure of Chlamydomonas reinhardtii THB1, a group 1 truncated hemoglobin with a rare histidine-lysine heme ligation.
    Acta crystallographica. Section F, Structural biology communications, 2015, Volume: 71, Issue:Pt 6

    Topics: Algal Proteins; Amino Acid Motifs; Chlamydomonas reinhardtii; Crystallography, X-Ray; Escherichia coli; Gene Expression; Heme; Histidine; Iron; Ligands; Lysine; Models, Molecular; Molecular Sequence Data; Nitrate Reductase; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Structural Homology, Protein; Truncated Hemoglobins

2015
O2 and Water Migration Pathways between the Solvent and Heme Pockets of Hemoglobin with Open and Closed Conformations of the Distal HisE7.
    Biochemistry, 2015, Sep-01, Volume: 54, Issue:34

    Topics: Amino Acid Substitution; Binding Sites; Diffusion; Heme; Hemoglobin A; Histidine; Humans; Hydrophobic and Hydrophilic Interactions; Models, Molecular; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Oxygen; Protein Conformation; Protein Subunits; Solvents; Water

2015
Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.
    Journal of the American Chemical Society, 2015, Nov-04, Volume: 137, Issue:43

    Topics: Archaeal Proteins; Cytochrome P-450 Enzyme System; Heme; Histidine; Models, Molecular; Mutation; Protein Conformation; Sulfolobus acidocaldarius

2015
Heme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment.
    Biochemistry, 2015, Nov-03, Volume: 54, Issue:43

    Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Conserved Sequence; Corynebacterium diphtheriae; Heme; Histidine; Ligands; Lipoproteins; Models, Molecular; Mutagenesis, Site-Directed; Protein Binding; Protein Conformation; Recombinant Proteins; Spectrophotometry; Tyrosine

2015
Helix-Capping Histidines: Diversity of N-H···N Hydrogen Bond Strength Revealed by (2h)JNN Scalar Couplings.
    Biochemistry, 2015, Nov-24, Volume: 54, Issue:46

    Topics: Bacterial Proteins; Chlamydomonas; Cytochromes b5; Heme; Hemoglobins; Histidine; Hydrogen Bonding; Methemoglobin; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; Proteins; Recombinant Proteins; Synechococcus; Synechocystis; Truncated Hemoglobins

2015
Tuning of Hemes b Equilibrium Redox Potential Is Not Required for Cross-Membrane Electron Transfer.
    The Journal of biological chemistry, 2016, Mar-25, Volume: 291, Issue:13

    Topics: Amino Acid Substitution; Binding Sites; Catalytic Domain; Electron Transport; Electron Transport Complex III; Electrons; Escherichia coli; Gene Expression; Heme; Histidine; Iron; Kinetics; Lysine; Membrane Potentials; Mutation; Quinones; Rhodobacter capsulatus; Thermodynamics

2016
Heme interacts with histidine- and tyrosine-based protein motifs and inhibits enzymatic activity of chloramphenicol acetyltransferase from Escherichia coli.
    Biochimica et biophysica acta, 2016, Volume: 1860, Issue:6

    Topics: Amino Acid Motifs; Chloramphenicol O-Acetyltransferase; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Escherichia coli; Heme; Histidine; Magnetic Resonance Spectroscopy; Spectrum Analysis, Raman; Tyrosine

2016
Discovery of a regioselectivity switch in nitrating P450s guided by molecular dynamics simulations and Markov models.
    Nature chemistry, 2016, Volume: 8, Issue:5

    Topics: Catalysis; Catalytic Domain; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Heme; Histidine; Markov Chains; Molecular Dynamics Simulation; Mutagenesis; Protein Conformation; Stereoisomerism; Streptomyces; Tryptophan

2016
Regulating the nitrite reductase activity of myoglobin by redesigning the heme active center.
    Nitric oxide : biology and chemistry, 2016, 07-01, Volume: 57

    Topics: Animals; Heme; Histidine; Hydrogen Bonding; Iron; Myoglobin; Nitric Oxide; Nitrite Reductases; Nitrites; Protein Engineering; Sperm Whale; Water

2016
Heme-coordinated histidine residues form non-specific functional "ferritin-heme" peroxidase system: Possible and partial mechanistic relevance to oxidative stress-mediated pathology in neurodegenerative diseases.
    International journal of biological macromolecules, 2016, Volume: 91

    Topics: Animals; Catalase; Ferritins; Heme; Histidine; Neurodegenerative Diseases; Oxidation-Reduction; Oxidative Stress; Peroxidase; Sheep

2016
Structural characterization of the heme-based oxygen sensor, AfGcHK, its interactions with the cognate response regulator, and their combined mechanism of action in a bacterial two-component signaling system.
    Proteins, 2016, Volume: 84, Issue:10

    Topics: Aeromonas salmonicida; Aspartic Acid; Bacterial Proteins; Cloning, Molecular; Deuterium Exchange Measurement; Escherichia coli; Heme; Histidine; Histidine Kinase; Iron; Myxococcales; Oxygen; Phosphorylation; Protein Domains; Protein Structure, Secondary; Recombinant Proteins; Signal Transduction; Structural Homology, Protein

2016
Structural basis of haem-iron acquisition by fungal pathogens.
    Nature microbiology, 2016, Sep-12, Volume: 1, Issue:11

    Topics: Aspartic Acid; Biological Transport; Candida albicans; Crystallography, X-Ray; Cysteine; Fungal Proteins; Heme; Hemeproteins; Histidine; Iron; Membrane Proteins; Molecular Conformation

2016
CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2016, Volume: 21, Issue:8

    Topics: Binding Sites; Carbon Monoxide; Circular Dichroism; Cysteine; Ferric Compounds; Ferrous Compounds; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Ligands; Lysine; MicroRNAs; Models, Biological; Nitric Oxide; Protein Binding; RNA-Binding Proteins; Spectrum Analysis, Raman

2016
Synthesis and Evaluation of Amyloid β Derived and Amyloid β Independent Enhancers of the Peroxidase-like Activity of Heme.
    Journal of medicinal chemistry, 2017, 01-12, Volume: 60, Issue:1

    Topics: Amino Acid Sequence; Amyloid beta-Peptides; Binding Sites; Catalysis; Heme; Histidine; Lipoproteins, LDL; Models, Molecular; Peroxidases; Spectrometry, Mass, Electrospray Ionization

2017
Role of Ionic Strength and pH in Modulating Thermodynamic Profiles Associated with CO Escape from Rice Nonsymbiotic Hemoglobin 1.
    The journal of physical chemistry. B, 2017, 01-19, Volume: 121, Issue:2

    Topics: Calorimetry; Carbon Monoxide; Heme; Hemeproteins; Histidine; Hydrogen-Ion Concentration; Iron; Kinetics; Ligands; Molecular Dynamics Simulation; Oryza; Osmolar Concentration; Plant Proteins; Protein Binding; Protein Conformation; Temperature; Thermodynamics

2017
A distal ligand mutes the interaction of hydrogen sulfide with human neuroglobin.
    The Journal of biological chemistry, 2017, 04-21, Volume: 292, Issue:16

    Topics: Catalysis; Crystallography, X-Ray; Cysteine; Electron Spin Resonance Spectroscopy; Globins; Heme; Hemoglobins; Histidine; Humans; Hydrogen Sulfide; Hydrogen-Ion Concentration; Kinetics; Ligands; Mass Spectrometry; Mutation; Myoglobin; Nerve Tissue Proteins; Neuroglobin; Oxygen; Protein Conformation; Spectrometry, Mass, Electrospray Ionization; Spectrum Analysis, Raman; Sulfides; Thiosulfates; Thrombin

2017
Cobalt tetradehydrocorrins coordinated by imidazolate-like histidine in the heme pocket of horseradish peroxidase.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2017, Volume: 22, Issue:5

    Topics: Cobalt; Coordination Complexes; Corrinoids; Heme; Histidine; Horseradish Peroxidase; Imidazoles; Models, Molecular; Molecular Conformation

2017
Insights Into How Heme Reduction Potentials Modulate Enzymatic Activities of a Myoglobin-based Functional Oxidase.
    Angewandte Chemie (International ed. in English), 2017, 06-01, Volume: 56, Issue:23

    Topics: Catalytic Domain; Electron Transport; Heme; Histidine; Models, Biological; Mutagenesis; Myoglobin; Oxidation-Reduction; Oxidoreductases; Oxygen; Spectrum Analysis; Substrate Specificity

2017
Heme Proximal Hydrogen Bonding between His170 and Asp132 Plays an Essential Role in the Heme Degradation Reaction of HutZ from Vibrio cholerae.
    Biochemistry, 2017, 05-30, Volume: 56, Issue:21

    Topics: Aspartic Acid; Bacterial Proteins; Heme; Histidine; Hydrogen Bonding; Molecular Structure; Vibrio cholerae

2017
Dissecting binding of a β-barrel membrane protein by phage display.
    Molecular bioSystems, 2017, Jul-25, Volume: 13, Issue:8

    Topics: Amino Acid Sequence; Bacterial Outer Membrane Proteins; Bacteriophage M13; Binding Sites; Capsid Proteins; Cell Surface Display Techniques; Cloning, Molecular; Escherichia coli; Gene Expression; Genetic Vectors; Heme; Hemoglobins; Histidine; Models, Molecular; Protein Binding; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Protein Structure, Tertiary; Recombinant Fusion Proteins; Shigella dysenteriae

2017
Identification and functional analysis of new peroxygenases in oat.
    Planta, 2017, Volume: 246, Issue:4

    Topics: Alanine; Amino Acid Sequence; Amino Acids; Avena; Binding Sites; Catalysis; Cloning, Molecular; Escherichia coli; Fatty Acids; Gene Expression; Heme; Histidine; Ligands; Mixed Function Oxygenases; Mutagenesis, Site-Directed; Mutation; Pichia; Sequence Alignment; Substrate Specificity; Transgenes

2017
Copper induced spin state change of heme-Aβ associated with Alzheimer's disease.
    Dalton transactions (Cambridge, England : 2003), 2017, Oct-10, Volume: 46, Issue:39

    Topics: Alzheimer Disease; Amyloid beta-Peptides; Catalytic Domain; Copper; Electron Spin Resonance Spectroscopy; Heme; Histidine; Humans; Kinetics; Quantum Theory; Reactive Oxygen Species

2017
Design of silk proteins with increased heme binding capacity and fabrication of silk-heme materials.
    Journal of inorganic biochemistry, 2017, Volume: 177

    Topics: Animals; Bees; Binding Sites; Electromagnetic Phenomena; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Histidine; Insect Proteins; Mutation; Protein Engineering; Protein Structure, Quaternary; Silk

2017
Tertiary dynamics of human adult hemoglobin fixed in R and T quaternary structures.
    Physical chemistry chemical physics : PCCP, 2018, Jan-31, Volume: 20, Issue:5

    Topics: Adult; Heme; Hemoglobins; Histidine; Humans; Hydrogen Bonding; Mutagenesis, Site-Directed; Protein Structure, Quaternary; Recombinant Proteins; Spectrum Analysis, Raman

2018
Histidine-Lysine Axial Ligand Switching in a Hemoglobin: A Role for Heme Propionates.
    Biochemistry, 2018, 02-06, Volume: 57, Issue:5

    Topics: Amino Acid Sequence; Bacterial Proteins; Coordination Complexes; Esterification; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Lysine; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Pressure; Propionates; Protein Conformation; Protein Folding; Protoporphyrins; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Static Electricity; Synechococcus; Truncated Hemoglobins

2018
Theory Uncovers the Role of the Methionine-Tyrosine-Tryptophan Radical Adduct in the Catalase Reaction of KatGs: O
    Chemistry (Weinheim an der Bergstrasse, Germany), 2018, Apr-06, Volume: 24, Issue:20

    Topics: Catalase; Catalytic Domain; Electron Transport; Free Radicals; Heme; Histidine; Methionine; Molecular Dynamics Simulation; Oxidation-Reduction; Oxygen; Peroxidases; Protein Conformation; Protons; Tryptophan; Tyrosine

2018
Characterization of the complex between native and reduced bovine serum albumin with aquacobalamin and evidence of dual tetrapyrrole binding.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2018, Volume: 23, Issue:5

    Topics: Alkylation; Cyanides; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Protein Binding; Serum Albumin, Bovine; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tetrapyrroles; Vitamin B 12

2018
Heme redox potentials hold the key to reactivity differences between nitric oxide reductase and heme-copper oxidase.
    Proceedings of the National Academy of Sciences of the United States of America, 2018, 06-12, Volume: 115, Issue:24

    Topics: Bacterial Proteins; Heme; Histidine; Kinetics; Models, Molecular; Nitric Oxide; Oxidation-Reduction; Oxidoreductases; Spectrum Analysis

2018
The Treponema denticola PAS Domain-Containing Histidine Kinase Hpk2 Is a Heme Binding Sensor of Oxygen Levels.
    Journal of bacteriology, 2018, 09-15, Volume: 200, Issue:18

    Topics: Aerobiosis; Amino Acid Sequence; Anaerobiosis; Bacterial Proteins; Gene Expression Regulation, Bacterial; Heme; Histidine; Histidine Kinase; Mutagenesis, Site-Directed; Oxygen; Periodontal Diseases; Phosphorylation; Promoter Regions, Genetic; Protein Serine-Threonine Kinases; Protein Structure, Secondary; Treponema denticola

2018
LC-MS/MS Proteoform Profiling Exposes Cytochrome c Peroxidase Self-Oxidation in Mitochondria and Functionally Important Hole Hopping from Its Heme.
    Journal of the American Chemical Society, 2018, 09-26, Volume: 140, Issue:38

    Topics: Chromatography, Liquid; Cytochrome-c Peroxidase; Glutathione; Heme; Histidine; Hydrogen Peroxide; Mitochondria; Oxidation-Reduction; Proteogenomics; Saccharomyces cerevisiae; Tandem Mass Spectrometry; Tyrosine

2018
Replacement of the Distal Histidine Reveals a Noncanonical Heme Binding Site in a 2-on-2 Hemoglobin.
    Biochemistry, 2018, 10-09, Volume: 57, Issue:40

    Topics: Bacterial Proteins; Binding Sites; Heme; Hemoglobins; Histidine; Synechocystis; Truncated Hemoglobins

2018
Heme-dependent Inactivation of 5-Aminolevulinate Synthase from Caulobacter crescentus.
    Scientific reports, 2018, 09-21, Volume: 8, Issue:1

    Topics: 5-Aminolevulinate Synthetase; Amino Acid Sequence; Bacterial Proteins; Caulobacter crescentus; Coenzymes; Heme; Histidine; Humans; Ligands; Pyridoxal Phosphate; RNA, Messenger

2018
Crystal structure of Kumaglobin: a hexacoordinated heme protein from an anhydrobiotic tardigrade, Ramazzottius varieornatus.
    The FEBS journal, 2019, Volume: 286, Issue:7

    Topics: Amino Acid Sequence; Animals; Arthropod Proteins; Crystallography, X-Ray; Globins; Heme; Hemeproteins; Histidine; Mutation; Protein Conformation; Sequence Homology; Tardigrada

2019
2-Alkenal modification of hemoglobin: Identification of a novel hemoglobin-specific alkanoic acid-histidine adduct.
    Redox biology, 2019, Volume: 23

    Topics: Amino Acids; Chromatography, Liquid; Erythrocytes; Heme; Hemoglobins; Histidine; Humans; Hydrolysis; Iron; Lipid Peroxidation; Oxidation-Reduction; Spectrometry, Mass, Electrospray Ionization; Tandem Mass Spectrometry

2019
A Density Functional Theory-Based Scheme to Compute the Redox Potential of a Transition Metal Complex: Applications to Heme Compound.
    Molecules (Basel, Switzerland), 2019, Feb-25, Volume: 24, Issue:4

    Topics: Coordination Complexes; Density Functional Theory; Electrochemical Techniques; Heme; Histidine; Ligands; Models, Molecular; Oxidation-Reduction; Protein Conformation; Transition Elements

2019
Unique Tyr-heme double cross-links in F43Y/T67R myoglobin: an artificial enzyme with a peroxidase activity comparable to that of native peroxidases.
    Chemical communications (Cambridge, England), 2019, Jun-11, Volume: 55, Issue:46

    Topics: Animals; Arginine; Benzothiazoles; Biomimetic Materials; Guaiacol; Heme; Histidine; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Molecular Structure; Mutation; Myoglobin; Oxidation-Reduction; Peroxidases; Protein Processing, Post-Translational; Sperm Whale; Sulfonic Acids; Tyrosine

2019
Proton mediated spin state transition of cobalt heme analogs.
    Nature communications, 2019, 05-24, Volume: 10, Issue:1

    Topics: Biocatalysis; Cobalt; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Iron; Ligands; Oxidation-Reduction; Protons

2019
Determination of the magnetic properties and orientation of the heme axial ligands of PpcA from Geobacter metallireducens by paramagnetic NMR.
    Journal of inorganic biochemistry, 2019, Volume: 198

    Topics: Bacterial Proteins; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Geobacter; Heme; Histidine; Ligands; Magnetic Phenomena; Molecular Structure

2019
A single mutation converts Alr5027 from cyanobacteria Nostoc sp. PCC 7120 to a heme-binding protein with heme-degrading ability.
    Journal of inorganic biochemistry, 2020, Volume: 203

    Topics: Bacterial Proteins; Binding Sites; Heme; Heme Oxygenase (Decyclizing); Histidine; Lysine; Mutation, Missense; Nostoc; Protein Binding

2020
Direct observation of ligand migration within human hemoglobin at work.
    Proceedings of the National Academy of Sciences of the United States of America, 2020, 03-03, Volume: 117, Issue:9

    Topics: Carbon Monoxide; Crystallography, X-Ray; Diffusion; Heme; Hemoglobins; Histidine; Humans; Ligands; Models, Molecular; Protein Conformation; Protein Subunits; Recombinant Fusion Proteins

2020
    International journal of molecular sciences, 2020, Jun-10, Volume: 21, Issue:11

    Topics: Bacterial Proteins; Binding Sites; Biofilms; Gene Expression Regulation, Bacterial; Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); Heme; Histidine; Humans; Microbiota; Mouth; Mutation; Porphyromonas gingivalis; Streptococcus gordonii

2020
The pH-Induced Selectivity Between Cysteine or Histidine Coordinated Heme in an Artificial α-Helical Metalloprotein.
    Angewandte Chemie (International ed. in English), 2021, 02-19, Volume: 60, Issue:8

    Topics: Amino Acid Sequence; Catalysis; Cysteine; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Metalloproteins; Oxidation-Reduction; Oxygen; Peptides; Protein Conformation, alpha-Helical

2021
Histidine
    The journal of physical chemistry. B, 2021, 01-14, Volume: 125, Issue:1

    Topics: Chlorides; Cysteine; Halogens; Heme; Histidine; Oxidation-Reduction; Peroxidase; Peroxidases

2021
Radical transfer but not heme distal residues is essential for pH dependence of dye-decolorizing activity of peroxidase from Vibrio cholerae.
    Journal of inorganic biochemistry, 2021, Volume: 219

    Topics: Amino Acid Substitution; Amino Acids; Anthraquinones; Binding Sites; Catalysis; Catalytic Domain; Coloring Agents; Crystallography, X-Ray; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Mutation; Peroxidase; Vibrio cholerae

2021
Unusually Fast
    International journal of molecular sciences, 2021, Mar-08, Volume: 22, Issue:5

    Topics: Heme; Hemoglobins; Histidine; Medicago truncatula; Plant Proteins; Protein Binding

2021
Abiological catalysis by myoglobin mutant with a genetically incorporated unnatural amino acid.
    The Biochemical journal, 2021, 05-14, Volume: 478, Issue:9

    Topics: Amino Acid Substitution; Biocatalysis; Catalytic Domain; Cloning, Molecular; Dihydroxyphenylalanine; Escherichia coli; Gene Expression; Genetic Vectors; Heme; Histidine; Humans; Hydrogen Bonding; Hydrogen Peroxide; Iron; Kinetics; Models, Molecular; Myoglobin; Oxidation-Reduction; Peroxidases; Protein Binding; Protein Conformation; Protein Engineering; Recombinant Proteins

2021
Control of distal lysine coordination in a monomeric hemoglobin: A role for heme peripheral interactions.
    Journal of inorganic biochemistry, 2021, Volume: 219

    Topics: Chlamydomonas reinhardtii; Crystallography, X-Ray; Ferric Compounds; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Iron; Ligands; Lysine; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Oxygenases; Protein Conformation; Truncated Hemoglobins

2021
Reactivity of inorganic sulfide species towards a pentacoordinated heme model system.
    Journal of inorganic biochemistry, 2021, Volume: 220

    Topics: Ferric Compounds; Heme; Hemeproteins; Histidine; Oxidation-Reduction; Peroxidases; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Sulfides; Surface-Active Agents

2021
Roles of Fe-Histidine bonds in stability of hemoglobin: Recognition of protein flexibility by Q Sepharose.
    Biophysical journal, 2021, 07-06, Volume: 120, Issue:13

    Topics: Heme; Hemoglobins; Histidine; Humans; Sepharose; Spectrum Analysis, Raman

2021
Insight into the function of active site residues in the catalytic mechanism of human ferrochelatase.
    The Biochemical journal, 2021, 09-17, Volume: 478, Issue:17

    Topics: Biocatalysis; Catalytic Domain; Crystallization; Ferrochelatase; Heme; Histidine; Humans; Iron; Kinetics; Ligands; Models, Molecular; Protein Binding; Protons; Protoporphyrins

2021
Nanosecond heme-to-heme electron transfer rates in a multiheme cytochrome nanowire reported by a spectrally unique His/Met-ligated heme.
    Proceedings of the National Academy of Sciences of the United States of America, 2021, 09-28, Volume: 118, Issue:39

    Topics: Cytochrome c Group; Cytochromes; Electron Transport; Electrons; Heme; Histidine; Methionine; Molecular Dynamics Simulation; Nanowires; Oxidation-Reduction; Shewanella

2021
New Insights into Hemopexin-Binding to Hemin and Hemoglobin.
    International journal of molecular sciences, 2022, Mar-30, Volume: 23, Issue:7

    Topics: Ferric Compounds; Heme; Hemin; Hemoglobins; Hemolysis; Hemopexin; Histidine; Humans; Molecular Docking Simulation

2022
Regulation of nitrite reductase and lipid binding properties of cytoglobin by surface and distal histidine mutations.
    Nitric oxide : biology and chemistry, 2022, 08-01, Volume: 125-126

    Topics: Cytoglobin; Globins; Heme; Histidine; Lipids; Mutation; Nitric Oxide; Nitrite Reductases; Nitrites

2022
Concerning the enigmatic cytochrome b-559 of oxygenic photosynthesis.
    Photosynthesis research, 2022, Volume: 153, Issue:3

    Topics: Cytochrome b Group; Cytochrome b6f Complex; Cytochromes b; Electron Transport; Heme; Histidine; Oxidation-Reduction; Oxygen; Photosynthesis; Photosystem II Protein Complex

2022
Spectral features of the ferrous-CO complex in cytochrome P450: a revisit using TDDFT calculations.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2023, Volume: 28, Issue:1

    Topics: Cytochrome P-450 Enzyme System; Density Functional Theory; Heme; Histidine; Ligands

2023
Combined spectroscopic and structural approaches to explore the mechanism of histidine-ligated heme-dependent aromatic oxygenases.
    Methods in enzymology, 2023, Volume: 685

    Topics: Electron Spin Resonance Spectroscopy; Heme; Heme Oxygenase (Decyclizing); Hemeproteins; Histidine

2023
Histidine-rich protein II nanoparticle delivery of heme iron load drives endothelial inflammation in cerebral malaria.
    Proceedings of the National Academy of Sciences of the United States of America, 2023, 06-27, Volume: 120, Issue:26

    Topics: Animals; Endothelial Cells; Heme; Hemeproteins; Histidine; Inflammation; Iron; Malaria, Cerebral; Malaria, Falciparum; Mice

2023
Molecular Engineering of
    Molecules (Basel, Switzerland), 2023, Jun-09, Volume: 28, Issue:12

    Topics: Bacterial Proteins; Escherichia coli; Ferritins; Gold; Heme; Histidine; Metal Nanoparticles

2023