histidine and heme
histidine has been researched along with heme in 745 studies
Research
Studies (745)
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 143 (19.19) | 18.7374 |
| 1990's | 165 (22.15) | 18.2507 |
| 2000's | 268 (35.97) | 29.6817 |
| 2010's | 148 (19.87) | 24.3611 |
| 2020's | 21 (2.82) | 2.80 |
Authors
| Authors | Studies |
|---|---|
| Appleby, CA; Bradbury, JH; Johnson, RN | 1 |
| Cohen, JS; Hagenmaier, H; Hayes, MB; Ohms, JP | 1 |
| Rein, H; Ristau, O; Ruckpaul, K | 1 |
| Gelin, BR; Karplus, M | 1 |
| Bethge, PH; Czerwinski, EW; Mathews, FS; Xavier, AV | 1 |
| Phillips, SE | 1 |
| Morgan, WT | 3 |
| Perutz, MF | 1 |
| Mazza, G; Welinder, KG | 1 |
| Morgan, WT; Muller-eberhard, U | 1 |
| Bazile, J; Cordier, JP; Frourin, A; Jondeau, D; Thenot, M | 1 |
| Vuk Pavlović, S | 1 |
| Caughey, WS; Maxwell, JC | 1 |
| Frye, JS; La Mar, GN; Satterlee, JD | 1 |
| Calhoun, MW; Gennis, RB; Ingledew, WJ; Lemieux, LJ; Thomas, JW | 1 |
| Babcock, GT; Ferguson-Miller, S; Gennis, RB; Hosler, JP; Kim, Y; Shapleigh, JP; Tecklenburg, MM | 1 |
| Dugad, LB; Goff, HM | 1 |
| Bollen, A; Deleersnyder, V; Garcia-Quintana, L; Jacquet, A; Moguilevsky, N | 1 |
| Cai, M; Timkovich, R | 1 |
| Adachi, S; Morishima, I | 1 |
| Andersson, LA; George, GN; Hori, H; Ikeda-Saito, M; Lutz, RS; Mattera, R; McKelvey, EJ; Pickering, IJ; Prince, RC; Sanders, CR | 1 |
| Salemme, FR; Weber, PC; Wendoloski, JJ | 1 |
| Crofts, AR; Gennis, RB; Yun, CH | 1 |
| Kraut, J; Miller, MA; Smulevich, G; Spiro, TG | 1 |
| Gersonde, K; La Mar, GN; Peyton, DH; Ramaprasad, S; Sankar, S; Unger, SW | 1 |
| Dugad, LB; Goff, HM; Lukat, GS; Wang, CC; Wang, X | 1 |
| DeWitt, DL; Shimokawa, T; Smith, WL | 1 |
| Shimokawa, T; Smith, WL | 1 |
| De Ciechi, P; Pakrasi, HB; Whitmarsh, J | 1 |
| Baboulène, M; Lattes, A; Seris, JL; Souppe, J; Urrutigoïty, M | 1 |
| Peyton, DH; Yee, S | 1 |
| Champion, PM; Li, PS; Sage, JT | 1 |
| Bax, A; Highet, RJ; Osawa, Y; Pohl, LR | 1 |
| Chiu, ML; La Mar, GN; Lee, KB; Sligar, SG; Walker, FA; Wu, JZ; Yu, LP | 1 |
| Fridén, H; Hederstedt, L | 1 |
| Berry, MJ; George, SJ; Santos, H; Thomson, AJ; Turner, DL | 1 |
| Kuppusamy, P; Levy, A; Rifkind, JM | 1 |
| Andersson, KK; Cheesman, MR; Fridén, H; Hederstedt, L; Thomson, AJ | 1 |
| Mathews, FS; Xia, ZX | 1 |
| La Mar, GN; Mizukami, H; Yu, LP | 1 |
| Chûjô, R; Nanai, N; Suzuki, T; Yamamoto, Y | 1 |
| Cully, BC; Holeman, B; Muller-Eberhard, U; Vincent, SH | 1 |
| Muller-Eberhard, U; Vincent, SH | 1 |
| Gadsby, PM; Hartshorn, RT; Moura, JJ; Sinclair-Day, JD; Sykes, AG; Thomson, AJ | 1 |
| Han, KH; La Mar, GN; Nagai, K | 1 |
| Lieutenant, K; Redhardt, A; Steinhoff, HJ | 1 |
| Behere, DV; Mitra, S; Modi, S | 1 |
| Gray, HB; Raphael, AL | 1 |
| Adachi, S; Morishima, I; Orii, Y; Shiro, Y; Yano, Y | 1 |
| Fang, H; Gennis, RB; Lin, RJ | 1 |
| Esposti, MD | 1 |
| Champion, PM; Morikis, D; Sligar, SG; Springer, BA | 1 |
| Konopka, K; Waskell, L | 1 |
| English, AM; Fishel, LA; Kraut, J; Mauro, JM; Smulevich, G; Spiro, TG | 1 |
| Behere, DV; Goff, HM; Gonzalez-Vergara, E | 1 |
| Senn, H; Wüthrich, K | 1 |
| Hashimoto, S; Inubushi, T; Kitagawa, T; Teraoka, J; Yonetani, T | 1 |
| Moench, S; Satterlee, JD | 1 |
| de Ropp, JS; La Mar, GN; Thanabal, V | 1 |
| Brady, JC; Everse, J; Lin, H; McFaul, SJ | 1 |
| Blouquit, Y; Craescu, CT; Rosa, J; Schaeffer, C | 1 |
| Yamamoto, Y | 3 |
| Shaklai, N; Shviro, Y | 1 |
| Dasgupta, S; Rousseau, DL; Sassaroli, M | 1 |
| Bianconi, A; Burattini, E; Congiu-Castellano, A; Dell'Ariccia, M; Durham, PJ; Giacometti, GM; Giovannelli, A | 1 |
| Alden, RG; Ondrias, MR; Shelnutt, JA | 1 |
| Dreybrodt, W; el Naggar, S; Schweitzer-Stenner, R | 1 |
| Dalvit, C; Ho, C | 1 |
| Levy, A; Rifkind, JM | 1 |
| Biserte, G; Havez, R; Hayem-Lévy, A; Moschetto, Y | 1 |
| Kon, H | 1 |
| Alpert, Y; Banerjee, R; Leterrier, F; Williams, RJ | 1 |
| Burris, RH; Swank, RT | 1 |
| Loew, GM | 1 |
| Jänig, GR; Jung, F; Rein, H; Ristau, O; Ruckpaul, K | 1 |
| Dervartanian, DV; Legall, J | 1 |
| Caughey, WS | 1 |
| Branefors-Helander, P | 1 |
| Babul, G; Rysavy, R; Stellwagen, E | 1 |
| Azzi, A; Folin, M; Jori, G; Tamburro, AM | 1 |
| Momenteau, M | 1 |
| Campbell, LL; Trousil, EB | 1 |
| Cohen, JS; Fisher, WR; Schechter, AN | 1 |
| Aviram, I; Krauss, Y | 1 |
| LeGall, J; McDonald, CC; Phillips, WD | 1 |
| Loock, B; Momenteau, M | 1 |
| Bitar, KG; Lowenkron, S; Vinogradov, SN | 1 |
| Gurd, FR; Hanania, GI; Shire, SJ | 1 |
| Perutz, MF; TenEyck, LF | 1 |
| Comi, P; Gianni, AM; Giglioni, B; Ottolenghi, S; Rungger, D | 1 |
| Irving, EA; Porra, RJ; Tennick, AM | 1 |
| Byrne, MJ; Davison, AJ; Kaminsky, LS | 1 |
| Hutner, SH | 1 |
| Atassi, MZ; Singhal, RP | 1 |
| Ho, C; Lindstrom, TR | 1 |
| Balegh, MS; Sandberg, HE | 1 |
| Antonini, E; Bonaventura, C; Bonaventura, J; Bossa, F; Brunori, M; Giardina, B; Wyman, J | 1 |
| Love, WE; Padlan, EA | 1 |
| Gibson, QH; Olson, JS | 1 |
| Coulson, AF; Yonetani, T | 1 |
| Fisher, JM; Mizuno, S; Rabinovitz, M | 1 |
| Babul, J; McGowan, EB; Stellwagen, E | 1 |
| Chang, JY; Schroeder, WA | 1 |
| Ogawa, S; Shulman, RG; Yamane, T | 1 |
| Fujiwara, M; Ogawa, S; Shulman, RG; Yamane, T | 1 |
| Folin, M; Galiazzo, G; Gennari, G; Jori, G | 1 |
| Bucci, E; Fronticelli, C | 1 |
| Maruyama, K; Yagi, T | 1 |
| Antonini, E; Forlani, L; Phelps, C | 1 |
| Chien, JC; Dickinson, LC | 1 |
| Gurdon, JB; Lane, CD; Marbaix, G | 1 |
| Reed, T | 1 |
| Nakaya, K; Shibata, K; Suzuki, T; Takenaka, O | 1 |
| Molday, RS; Steinhardt, J | 1 |
| Caughey, W; McCoy, S | 1 |
| Hager, LP; Warme, PK | 2 |
| Gaĭduk, VI; Koreneva, LG | 1 |
| Jacob, HS; Winterhalter, KH | 1 |
| Amit, N; Formanek, H | 1 |
| de Bruin, SH; Janssen, LH; van Os, GA | 1 |
| Tentori, L | 1 |
| Geraci, G; Gibson, QH; Parkhurst, LJ | 1 |
| Guerritore, D; Zito, R | 1 |
| Craigie, JS; Laycock, MV | 1 |
| Braunitzer, G; Neuwirth, H; Reinhard, F | 1 |
| Bucci, E; Fronticelli, C; Ragatz, B | 1 |
| Clark, JF; Gurd, FR; Hartzell, CR | 1 |
| Nanzyo, N; Sano, S | 1 |
| Efron, ML; Shahidi, NT | 1 |
| Stellwagen, E | 1 |
| Imai, K | 1 |
| Brill, AS; Sandberg, HE | 1 |
| Galiazzo, G; Jori, G; Scoffone, E | 1 |
| Shichi, H | 1 |
| Horinishi, H; Kurihara, K; Shibata, K | 1 |
| Stotz, E; Vanderkooi, G | 1 |
| Kraut, J; Poulos, TL | 1 |
| Cleary, ML; Haynes, JR; Lingrel, JB; Schon, EA | 1 |
| Hayashi, K; Kobayashi, K; Tamura, M | 1 |
| Krogmann, DW; Markley, JL; Ulrich, EL | 1 |
| Eglinton, DG; Greenwood, C; Hill, BC; Thomson, AJ | 1 |
| Han, K; Jue, T; La Mar, GN; Yamamoto, Y | 1 |
| Gelin, BR; Karplus, M; Lee, AW | 1 |
| Cutnell, JD; Kong, SB; La Mar, GN | 2 |
| Layrisse, M; Leets, I; Martínez-Torres, C; Ramírez, J; Taylor, P | 1 |
| Friedman, JM; Ikeda-Saito, M; Scott, TW; Yonetani, T | 1 |
| Kitagawa, T; Nagai, K | 1 |
| Ondrias, MR; Rousseau, DL; Simon, SR | 2 |
| Braunitzer, G; Liljeqvist, G; Paléus, S | 1 |
| Ho, C; Lin, AK; Takahashi, S | 1 |
| Friedman, JM; Ondrias, MR; Rousseau, DL; Stepnoski, RA | 1 |
| Kitagawa, T; Teraoka, J | 1 |
| Adams, ML; Asher, SA; Schuster, TM | 1 |
| Anderson, RR; Budd, DL; Gersonde, K; La Mar, GN; Langry, KC; Sick, H; Smith, KM | 1 |
| Asher, S | 1 |
| de Ropp, JS; La Mar, GN; Langry, KC; Smith, KM | 1 |
| Krümpelmann, D; Ribbing, W; Rüterjans, H | 1 |
| Ribbing, W; Rüterjans, H | 2 |
| Bucci, E; Fronticelli, C; Scholberg, HP | 1 |
| Masters, BS; McMillan, K | 1 |
| Ferrer, JC; Hildebrand, DP; Mauk, AG; Smith, M; Tang, HL | 1 |
| Banci, L; Pierattelli, R; Turner, DL | 1 |
| Choudhury, K; Marzocchi, MP; Neri, F; Poulos, TL; Smulevich, G; Willemsen, O | 1 |
| Gennis, RB; Georgiou, C; Ghaim, JB; Kaysser, TM | 1 |
| Meunier, B; Rich, PR; Rodriguez-Lopez, JN; Smith, AT; Thorneley, RN | 1 |
| Fetrow, JS; Fumo, G; Spitzer, JS | 1 |
| Admiraal, SJ; Dou, Y; George, GN; Ikeda-Saito, M; Krzywda, S; Li, T; Olson, JS; Pickering, IJ; Prince, RC; Wilkinson, AJ | 1 |
| Ahmed, I; Blackburn, NJ; Boswell, JS; Fann, YC; Hoffman, BM; Verkhovskaya, ML; Wikström, M | 1 |
| Newmyer, SL; Ortiz de Montellano, PR | 1 |
| Amada, F; Fukuyama, K; Kubota, T; Kunishima, N; Matsubara, H | 1 |
| Funasaki, N; Neya, S | 1 |
| Alam, J; Kao, SM; Morgan, WT; Muster, P; Smith, A; Tatum, F | 1 |
| Jewsbury, P; Kitagawa, T | 1 |
| Burstyn, JN; Dawson, JH; Dierks, EA; Hawkins, BK; Yu, AE | 1 |
| Goldberg, DE; Kloek, AP; Mathews, FS; Yang, J | 1 |
| Cheesman, MR; Gennis, RB; Kaysser, T; Peng, Q; Peterson, J; Spinner, F; Thomson, AJ | 1 |
| Desbois, A; Le Lirzin, A; Othman, S | 2 |
| Fitzgerald, MM; Goodin, DB; Jensen, GM; McRee, DE; Siegel, HA | 1 |
| Bohn, B; Franzen, S; Martin, JL; Poyart, C | 1 |
| Ditta, GS; Helinski, DR; Monson, EK | 1 |
| Joshi, AA; McDonald, MJ | 1 |
| Böhme, E; Foerster, J; Harteneck, C; Humbert, P; Koesling, D; Malkewitz, J; Schultz, G; Wedel, B | 1 |
| Loehr, TM; Ortiz de Montellano, PR; Sun, J; Wilks, A | 1 |
| Doseeva, VV; Galkin, AG; Gazaryan, IG; Tishkov, VI | 1 |
| Bruschi, M; Czjzek, M; Guerlesquin, F; Haser, R; Payan, F | 1 |
| Gennis, RB; Peterson, J; Vibat, C | 1 |
| Burke, JF; Paoli, M; Sanders, SA; Smith, AT; Smulevich, G; Thorneley, RN | 1 |
| Bogumil, R; Brayer, GD; Hunter, CL; Lee, H; Lloyd, E; Mauk, AG; Maurus, R; Smith, M; Tang, HL | 1 |
| Banci, L; Bertini, I; Ferrer, JC; Mauk, AG; Morris, IK; Smith, KM; Smith, M; Turano, P | 1 |
| Campos, AP; Canters, GW; Hill, HA; Hunt, NI; Teixeira, M; Ubbink, M | 1 |
| Hrkal, Z; Iwahara, S; Muller-Eberhard, U; Peyton, DH; Satoh, H; Satoh, T | 1 |
| Conover, RC; Finnegan, MG; Garcia Castillo, MC; Johnson, MK; Knaff, DB | 1 |
| Bogumil, R; Brayer, GD; Luo, Y; Mauk, AG; Maurus, R; Smith, M; Tang, HL | 1 |
| Barrick, D | 1 |
| Hori, H; Masuya, F | 1 |
| Alben, JO; Calhoun, MW; Gennis, RB; Goswitz, VC; Hill, JJ; Lemieux, LJ; Thomas, JW | 1 |
| Admiraal, SJ; Dou, Y; Ikeda-Saito, M; La Mar, GN; Qin, J | 1 |
| Marzluf, GA; Okamoto, PM | 1 |
| Adachi, S; Egawa, T; Ishimori, K; Kitagawa, T; Makino, R; Morishima, I; Nagano, S; Watanabe, Y | 1 |
| Aguiar, AP; Campos, AP; Costa, HS; Santos, H; Teixeira, M; Turner, DL; Xavier, AV | 1 |
| Goodin, DB; McRee, DE | 1 |
| Barker, PD; Eltis, LD; Guillemette, JG; Inglis, SC; Mauk, AG; Miller, CM; Northrup, SH; Thomasson, KA | 1 |
| Blauer, G; Sreerama, N; Woody, RW | 1 |
| Aguiar, AP; Campos, AP; De La Rosa, MA; Hervás, M; Navarro, JA; Ortega, JM; Regalla, M; Teixeira, M; Xavier, AV | 1 |
| Brown, KA; Erman, JE; Kraut, J; Miller, MA; Shaw, A; Vitello, LB | 1 |
| Chapman, SK; Manson, FD; Miles, CS; Reid, GA | 1 |
| Fujii, M; Iizuka, T; Isogai, Y; Iwata, T; Makino, R; Shiro, Y | 1 |
| Alben, JO; Babcock, GT; Calhoun, MW; Ferguson-Miller, S; Gennis, RB; Hill, JJ; Hosler, JP; Shapleigh, JP; Tecklenburg, MM; Thomas, JW | 1 |
| Barnard, ML; Diep, D; Gurdian, S; Ladd, M; Turrens, JF | 1 |
| Boffi, A; Chiancone, E; Friedman, JM; Rousseau, DL; Song, S | 1 |
| Maines, MD; McCoubrey, WK | 1 |
| Chiu, ML; La Mar, GN; Qin, J; Rajarathnam, K; Sligar, SG | 1 |
| Craescu, CT; Martineau, L | 1 |
| Cox, MC; Le Brun, N; Moore, GR; Morgan, WT; Smith, A; Thomson, AJ | 1 |
| Doseeva, VV; Galkin, AG; Gazarian, IG; Tishkov, VI | 1 |
| Amada, F; Fukuyama, K; Kawamoto, M; Kunishima, N; Matsubara, H; Matsunaga, T | 1 |
| Anraku, Y; Hori, H; Mogi, T; Tsubaki, M | 1 |
| Gerber, NC; Ortiz de Montellano, PR; Rodríguez-Crespo, I | 1 |
| Phillips, GN; Yang, F | 1 |
| de Montellano, PR; Newmyer, SL | 1 |
| Chance, MR; Fischetti, RF; Hai, Y; Huang, WX; Miller, LM; Scheuring, E; Sclavi, B; Sullivan, M | 1 |
| Desbois, A; Othman, S; Richaud, P; Verméglio, A | 1 |
| Bertolucci, C; Gilles-Gonzalez, MA; Gonzalez, G; Ming, LJ | 1 |
| Hennecke, H; Thöny-Meyer, L; Zufferey, R | 1 |
| Döpner, S; Gerscher, S; Gleissner, M; Hildebrandt, P; Schäfer, G | 1 |
| Ishimori, K; Matsui, T; Morishima, I; Nagano, S; Watanabe, Y | 1 |
| Ishimori, K; Morishima, I; Tanaka, M | 1 |
| Cooper, CE; Pezeshk, A; Symons, MR; Torres, J; Wilson, M | 1 |
| Gao, Y; Veitch, NC; Welinder, KG | 1 |
| Adachi, S; Bourgeois, D; Moffat, K; Pradervand, C; Ren, Z; Schildkamp, W; Srajer, V; Teng, T; Ursby, T; Wulff, M | 1 |
| Polm, MW; Schaafsma, TJ | 1 |
| Kushkuley, B; Stavrov, SS | 1 |
| Chen, YP; Dawson, JH; Lincoln, DE; Lovell, CR; Roach, MP; Woodin, SA | 1 |
| Beck, R; Rambach, A; Raux, E; Thermes, C; Warren, M | 1 |
| Chen, Y; Liu, G; Lu, J; Shao, W; Tang, W | 1 |
| Oganesyan, VS; Sharonov, YA | 1 |
| Furlong Nickels, E; Gennis, RB; Rumbley, JN | 1 |
| Dodson, G; Liddington, RC; Paoli, M; Wilkinson, AJ | 1 |
| Dyer, RB; Hummer, G; Puustinen, A; Riistama, S; Wikström, M; Woodruff, WH | 1 |
| Blasco, F; Frixon, C; Lemesle-Meunier, D; Magalon, A; Rothery, RA; Weiner, JH | 1 |
| Baker, AR; Brittain, T; Butler, CS; Greenwood, C; Little, RH; Lowe, DJ; Watmough, NJ | 1 |
| Buchter, S; Galkin, O; Schulte, A; Tabirian, A | 1 |
| Büschlen, S; Choquet, Y; Culler, D; de Vitry, C; Girard-Bascou, J; Kuras, R; Merchant, S; Wollman, FA | 1 |
| Fujii, H; Ikeda-Saito, M; Ishikawa, K; Matera, KM; Sato, M; Yoshida, T; Yoshimura, T; Zhou, H | 1 |
| Bucci, E; Fronticelli, C; Gilliland, GL; Ji, X; Karavitis, M; Kwansa, H; Razynska, A; Vásquez, G | 1 |
| Bowler, BE; Godbole, S; Hammack, B | 2 |
| Indiani, C; Neri, F; Smulevich, G; Welinder, KG | 1 |
| Hellinga, HW | 1 |
| Cecchini, G; Gennis, RB; Kita, K; Nakamura, K; Vibat, CR | 1 |
| Babcock, GT; Marletta, MA; Schelvis, JP; Zhao, Y | 2 |
| Boffi, A; Chiancone, E; Colotti, G; Das, TK; Gibson, QH; Guarrera, L; Rousseau, DL | 1 |
| Beck, DL; Goldman, BS; Kranz, RG; Monika, EM | 1 |
| Chien, EY; La Mar, GN; Sligar, SG; Wu, Y | 1 |
| Bocian, DF; Kalsbeck, WA; Olson, JS; Tang, Q | 1 |
| Barquera, B; García-Horsman, JA; Gennis, RB; Toledo-Cuevas, M; Wikström, M | 1 |
| Hennecke, H; Schulz, H; Thöny-Meyer, L | 1 |
| Chien, EY; Friedman, JM; Peterson, ES; Sligar, SG | 1 |
| Akutsu, H; Cusanovich, MA; Nakamura, H; Niki, K; Ohmura, T | 1 |
| Rivera, M; Rodríguez, JC | 1 |
| Lukat-Rodgers, GS; Rexine, JL; Rodgers, KR | 1 |
| Inaba, K; Ishimori, K; Morishima, I | 1 |
| Saruta, F; Tatsuzawa, O; Tsunawaki, S; Yoshida, LS; Yoshikawa, K | 1 |
| Bocian, DF; Dutton, PL; Kalsbeck, WA; Moser, CC; Shifman, JM | 1 |
| Feis, A; Nissum, M; Smulevich, G | 1 |
| de Ropp, JS; La Mar, GN; Mandal, PK | 1 |
| Liong, E; Matsui, T; Ozaki, Si; Phillips, GN; Watanabe, Y | 1 |
| Boffi, A; Chiancone, E; Das, TK; Rousseau, DL | 1 |
| Das, TK; Duff, SM; Hill, RD; Lee, HC; Peisach, J; Rousseau, DL; Wittenberg, BA; Wittenberg, JB | 1 |
| Burstyn, JN; Chung, SY; Kerby, RL; Parks, RB; Reynolds, MF; Roberts, GP; Shelver, D; Thorsteinsson, MV | 1 |
| Hori, H; Iizuka, T; Makino, R; Matsuda, H; Obayashi, E; Shiro, Y | 1 |
| Hildebrand, DP; Liu, Y; Loehr, TM; Mauk, AG; Moënne-Loccoz, P; Ortiz de Montellano, PR; Wilks, A | 1 |
| Ramadas, N; Rifkind, JM | 1 |
| Bartunik, HD; Kachalova, GS; Popov, AN | 1 |
| 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, WH | 1 |
| Daldal, F; Darrouzet, E; Knaff, DB; Li, J; Mandaci, S; Qin, H | 1 |
| Sagnella, DE; Straub, JE | 1 |
| Lu, Y; Wang, X | 1 |
| de Montellano, PR; Knudsen, GM; Nishida, CR; Rodríguez-Crespo, I | 1 |
| Kitagawa, T; Nagai, M; Nagatomo, S; Tsuneshige, A; Yonetani, T | 1 |
| Chien, EY; McMahon, BH; Müller, JD; Nienhaus, GU; Sligar, SG | 1 |
| Adachi, S; Hasnain, SS; Iizuka, T; Miyatake, H; Mukai, M; Nakamura, H; Shiro, Y; Strange, RW; Tamura, K | 1 |
| Becker, OM; Margoliash, E; Navon, G; Qin, W; Schejter, A; Taler, G | 1 |
| Dawson, JH; Lu, Y; Pond, AE; Sigman, JA | 1 |
| Ortiz de Montellano, PR; Poulos, TL; Schuller, DJ; Wilks, A | 1 |
| Bravo, J; Bujons, J; Ens, W; Fita, I; Hu, B; Loewen, PC; Maté, MJ; Sevinc, MS; Switala, J | 1 |
| Abdur-Rashid, A; Baer, MT; Bracken, CS; Helms, W; Stojiljkovic, I | 1 |
| Berendzen, J; Chu, K; Schlichting, I; Sweet, RM; Vojtechovský, J | 1 |
| Hager, LP; Manoj, KM; Mroczko, M; Wang, X; Yi, X | 1 |
| Bertini, I; Luchinat, C; Parigi, G; Walker, FA | 1 |
| Koesling, D | 1 |
| Barker, PD; Fearnley, IM; Rice, JK | 1 |
| Babcock, GT; Cerda, JF; Choi, CY; Chu, HA; Marletta, MA | 1 |
| Anthony, LC; Donohue, TJ; Falkowski, MJ; Newman, JD; Schilke, BA | 1 |
| Chen, JJ; Guo, Y; Matts, RL; Uma, S; White, S | 1 |
| Bruschi, M; Chottard, G; Kazanskaya, I | 1 |
| Cho, YS; Pakrasi, HB; Whitmarsh, J | 1 |
| Behr, J; Hellwig, P; Mäntele, W; Michel, H | 1 |
| Ozaki, S; Roach, MP; Watanabe, Y | 1 |
| Brunori, M; Cutruzzolà, F; Federici, L; Musto, R; Savino, C; Travaglini-Allocatelli, C | 1 |
| Das, TK; Ferguson-Miller, S; Gennis, RB; Lee, HM; Mills, D; Rousseau, DL | 1 |
| Boffi, A; Chiancone, E; Giangiacomo, L; Guarrera, L; Spagnuolo, C | 1 |
| Bemski, G; Flores, M; Wajnberg, E | 1 |
| Chu, GC; Ikeda-Saito, M; Katakura, K; Kayama, T; Sasahara, M; Sato, M; Sun, D; Tomita, T; Yoshida, T; Zhang, X | 1 |
| Allen, JW; Chapman, SK; Ferguson, SJ; Koppenhöfer, A; Turner, KL | 1 |
| Moënne-Loccoz, P; Wilks, A | 1 |
| Nall, BT; Pierce, MM | 1 |
| Feis, A; Howes, BD; Indiani, C; Marzocchi, MP; Smulevich, G | 1 |
| Goodwin, DC; Marnett, LJ; Rowlinson, SW | 1 |
| Ihara, M; Ishimori, K; Morishima, I; Takahashi, S | 1 |
| Arakawa, T; Babcock, GT; Cerda, JF; Garavito, RM; Mulichak, AM; Seibold, SA; Smith, WL; Song, I | 1 |
| Arp, DJ; Meek, L | 1 |
| Chapman, SK; Cuthbertson, PM; Gordon, EH; Hill, AE; Pike, AD; Reid, GA | 1 |
| Couture, M; Das, TK; Guertin, M; Ouellet, Y; Rousseau, DL; Savard, PY; Wittenberg, BA; Wittenberg, JB | 1 |
| Turner, DL | 1 |
| Fang, TY; Ho, C; Ho, NT; Lukin, JA; Simplaceanu, V; Zou, M | 1 |
| Lukat-Rodgers, GS; Rodgers, KR; Rusnak, F; Wengenack, NL | 1 |
| Gibson, QH; Olson, JS; Scott, EE | 1 |
| Aono, S; Ishikawa, H; Ishimori, K; Kitagawa, T; Mizutani, Y; Morishima, I; Nakajima, H; Uchida, T | 1 |
| Puspita, WJ; Roach, MP; Watanabe, Y | 1 |
| Aki, M; Jin, Y; Kitagawa, T; Li, R; Nagai, M; Nagatomo, S; Sakai, H | 1 |
| Bowler, BE; Nelson, CJ | 1 |
| Iizuka, T; Mukai, M; Nakamura, H; Nakamura, K; Shiro, Y | 1 |
| Chapman, SK; Cheesman, MR; Miles, CS; Mowat, CG; Munro, AW; Quaroni, LG; Reid, GA | 1 |
| Aono, S; Honma, Y; Kato, T; Miyatake, H; Nakajima, H; Park, SY; Shiro, Y; Tawara, T | 1 |
| Blankenship, J; Goodin, DB; Hirst, J; McRee, DE; Wilcox, SK; Williams, PA | 1 |
| Ai, J; Goodin, DB; Hirst, J; Loehr, TM; Moënne-Loccoz, P; Wilcox, SK | 1 |
| Brennan, L; Chapman, SK; Cuthbertson, PM; Pessanha, M; Reid, GA; Salgueiro, CA; Turner, DL; Xavier, AV | 1 |
| Bhattacharya, S; Falzone, CJ; Lecomte, JT; Scott, NL; Vu, BC; Wang, Y | 1 |
| Estabrook, RW; Gilep, AA; Guryev, OL; Usanov, SA | 1 |
| Bailey, J; Boxer, SG; Dyer, RB; Franzen, S; Hu, RB; Thomas, MR; Woodruff, WH | 1 |
| Brennan, L; Fareleira, P; Santos, H; Turner, DL | 1 |
| Cao, W; Champion, PM; Christian, JF; Rosca, F; Sage, JT | 1 |
| Falzone, CJ; Lecomte, JT; Scott, NL; Vu, BC | 1 |
| Arciero, DM; Hooper, AB; Iverson, TM; Rees, DC | 1 |
| Arnaudeau, S; Banfi, B; Demaurex, N; Hossle, JP; Krause, KH; Maturana, A; Ryser, S; Schlegel, W | 1 |
| Gold, MH; Li, B; Renganathan, V; Rotsaert, FA | 1 |
| Biberstine-Kinkade, KJ; DeLeo, FR; Dinauer, MC; Epstein, RI; LeRoy, BA; Nauseef, WM | 1 |
| Eichinger, M; Evanseck, JD; Parrinello, M; Rovira, C; Schulze, B | 1 |
| Abbruzzetti, S; Libertini, LJ; Small, EW; Small, JR; Viappiani, C | 1 |
| Hori, H | 1 |
| Correia, MA; Dick, R; Murray, BP; Reid, MJ | 1 |
| Canters, GW; Diederix, RE; Ubbink, M | 1 |
| Henderson, LM; Mankelow, TJ | 2 |
| Dutton, PL; Fuentes, EJ; Gibney, BR; Huang, SS; Skalicky, JJ; Wand, AJ | 1 |
| Bowler, BE; Hammack, BN; Smith, CR | 1 |
| Losada, M; Ortega, JM; Roncel, M | 1 |
| Arese, M; Brown, K; Brunori, M; Cambillau, C; Cutruzzola', F; Roig-Zamboni, V; Sun, W; Tegoni, M | 1 |
| Christmas, P; Henne, KR; Kunze, KL; Rettie, AE; Soberman, RJ; Zheng, YM | 1 |
| Brudvig, GW; de Paula, JC; Kievit, O; Lakshmi, KV; Reifler, MJ; Vrettos, JS | 1 |
| Ahuja, U; Ren, Q; Thöny-Meyer, L | 1 |
| Ajayi, WU; Chaudhuri, M; Hill, GC | 1 |
| Dolgikh, DA; Hagen, SJ; Latypov, RF; Roder, H | 1 |
| Ludwig, B; Pfitzner, U; Pinakoulaki, E; Varotsis, C | 1 |
| Antholine, W; Ferguson-Miller, S; Kang, UG; Schmidt, B; Zhen, Y | 1 |
| Baptista, AM; Soares, CM; Teixeira, VH | 1 |
| Delepierre, M; Deniau, C; Kumar, V; Lecroisey, A; Létoffé, S; Simenel, C; Stojiljkovic, I; Wandersman, C; Wolff, N | 1 |
| Adachi, S; Chong, KT; Mito, M; Miyazaki, G; Morimoto, H; Park, SY; Tame, JR | 1 |
| Banci, L; Bertini, I; Cavallaro, G; Luchinat, C | 1 |
| Bryant, DA; Falzone, CJ; Lecomte, JT; Scott, NL; Vuletich, DA; Zhao, J | 1 |
| Boffi, A; Draghi, F; Miele, AE; Vallone, B | 1 |
| Kitagawa, T; Mizutani, Y; Sagami, I; Sasakura, Y; Sato, A; Shimizu, T; Sugiyama, S | 1 |
| Jones, AD; Lecomte, JT; Vu, BC | 1 |
| Berks, BC; Cartron, ML; Ferguson, SJ; Richardson, DJ; Roldán, MD | 1 |
| Kang, C; Park, HJ; Satterlee, JD; Treff, N; Yang, C | 1 |
| Asokan, A; de Ropp, JS; La Mar, GN; Newmyer, S; Ortiz de Montellano, PR; Sham, S | 1 |
| Bandyopadhyay, D; Bandyopadhyay, U; Banerjee, RK; Mazumdar, A | 1 |
| Cheng, Y; Ho, C; Shen, TJ; Simplaceanu, V | 1 |
| Dreyfuss, BW; Gabilly, ST; Hamel, PP; Merchant, S; Xie, Z | 1 |
| Enggist, E; Güntert, P; Pervushin, K; Thöny-Meyer, L | 1 |
| Hori, H; Ishikawa, H; Ishimori, K; Matts, RL; Morishima, I; Takahashi, S; Yun, BG | 1 |
| Bunce, RA; Caignan, GA; Deshmukh, R; Eastman, MA; Huang, HW; Moënne-Loccoz, P; Rivera, M; Wilks, A; Zeng, Y | 1 |
| Hargrove, MS; Kundu, S | 1 |
| Shokhirev, NV; Shokhireva, TKh; Walker, FA | 1 |
| Migita, CT; Yoshida, T; Zhang, X | 1 |
| Farmer, PJ; Fleischer, E; La Mar, GN; Ma, D; Sulc, F | 1 |
| Bowler, BE; Smith, CR; Wandschneider, E | 1 |
| Doctorovich, FA; Estrin, DA; Martí, MA; Ordejón, P; Scherlis, DA | 1 |
| Daltrop, O; Ferguson, SJ; Higham, CW; Stevens, JM | 1 |
| Mabrouk, PA; Sivakolundu, SG | 1 |
| Bhaskar, B; Farmer, PJ; Immoos, CE; Poulos, TL; Shimizu, H; Sulc, F | 1 |
| Littlejohn, TK; Takikawa, O; Truscott, RJ; Walker, MJ | 1 |
| Cao, C; Huang, ZX; Ma, J; Wang, YH; Wu, H; Xue, LL; Zhang, Q | 1 |
| Arnone, A; Robinson, VL; Smith, BB | 1 |
| Adachi, K; Lakka, V; Reddy, KS; Surrey, S; Wehrli, S; Yang, Y | 1 |
| Abeysinghe, RD; Ball, T; Cukier, RI; Hsi, LC; Micielli, R; Mills, DA; Rieke, CJ; Seibold, SA; Smith, WL | 1 |
| Erman, JE; Foshay, M; Satterlee, JD; Savenkova, MI | 1 |
| Schmidt, P; Schramm, M; Schröder, H; Stasch, JP | 1 |
| NAKAMURA, Y; SHIBATA, K; TOHJO, M | 1 |
| SHIBATA, K; TOHJO, M | 1 |
| LENDLE, L | 1 |
| LOSSE, G; MUELLER, G | 1 |
| Debarbieux, L; Delepelaire, P; Izadi, N; Létoffé, S; Wandersman, C | 1 |
| Dalosto, SD; Kaposi, AD; Prabhu, NV; Sharp, KA; Stavrov, SS; Vanderkooi, JM; Wright, WW | 1 |
| Ahuja, U; Thöny-Meyer, L | 1 |
| Bominaar, EL; Hill, BC; Pearce, LL; Peterson, J | 1 |
| Battaini, G; Bolognesi, M; Casella, L; Monzani, E; Murtas, M; Pennati, A; Roncone, R; Sanangelantoni, AM; Zuccotti, S | 1 |
| Chapman, SK; Miles, CS; Mowat, CG; Reid, GA; Rothery, EL; Walkinshaw, MD | 1 |
| Rothery, RA; Weiner, JH; Zhao, Z | 1 |
| Cao, C; Huang, ZX; Wang, YF; Wang, YH; Wang, ZQ; Wu, H; Zhang, Q | 1 |
| Hayashi, T; Ishikawa, Y; Ryu, D; Sato, H; Tomisugi, Y; Tsutsumi, H; Uno, T; Wilkinson, AJ | 1 |
| Gupta, K; Katz, AK; Kaub, CJ; Loll, PJ; Selinsky, BS | 1 |
| Hori, H; Inuzuka, T; Ishikawa, H; Ishimori, K; Matts, RL; Morishima, I; Takahashi, S; Yun, BG | 1 |
| Arnone, A; Chan, NL; Kavanaugh, JS; Rogers, PH | 1 |
| Ando, T; Hayashi, T; Hisaeda, Y; Sato, H; Ueno, T; Watanabe, Y | 1 |
| Falzone, CJ; Kuriakose, SA; Lecomte, JT; Vu, BC; Vuletich, DA | 1 |
| Hirota, S; Suzuki, M; Watanabe, Y | 1 |
| Chishiro, T; Liu, JG; Naruta, Y; Tachi, Y; Tani, F | 1 |
| Jensen, KP; Ryde, U | 1 |
| Benson, DR; Cowley, AB; Lukat-Rodgers, GS; Rodgers, KR | 1 |
| Walker, FA | 2 |
| Aznar, C; Britt, RD; Brynda, M; Kim, SH; Michalczyk, R; Silks, LA; Unkefer, CJ; Woodruff, WH | 1 |
| Huang, ZX; Lu, JX; Wang, WH; Xie, Y; Yao, P | 1 |
| Hirayama, M; Kinoshita, S; Kobiyama, A; Watabe, S | 1 |
| Fujiwara, S; Kawamura, K; Takabayashi, T; Takahashi, F; Yubisui, T | 1 |
| Dutton, PL; Huang, SS; Koder, RL; Lewis, M; Wand, AJ | 1 |
| Ferguson-Miller, S; Hillier, W; McCracken, J; Schmidt, B | 1 |
| Bowler, BE; Wandschneider, E | 1 |
| Manoharan, PT; Mohanty, JG; Nagababu, E; Ramasamy, S; Rifkind, JM | 1 |
| Allen, JW; Cartron, ML; Ferguson, SJ; Richardson, DJ; Zajicek, RS | 1 |
| Fiorucci, L; Santoni, E; Santucci, R; Scatragli, S; Sinibaldi, F; Smulevich, G | 1 |
| Berezhna, S; Cao, W; Champion, PM; Demidov, AA; Georgiev, GY; Sage, JT; Sjodin, T; Wang, W; Ye, X | 1 |
| Herold, S; Kalinga, S; Matsui, T; Watanabe, Y | 1 |
| Jin, Y; Kitagawa, T; Nagai, M; Nagai, Y; Nagatomo, S | 1 |
| Dohmae, N; Iizuka, T; Ishida, M; Isogai, Y; Oku, T; Shiro, Y | 1 |
| Alves, T; Bonifácio, C; Bourgeois, D; Dias, JM; Moura, I; Pereira, AS; Romão, MJ; Trincão, J | 1 |
| Akutsu, H; Harada, E; Kobayashi, R; Ozawa, K; Takayama, Y | 1 |
| Barrick, D; Berezhna, S; Cao, W; Champion, PM; Christian, JF; Demidov, AA; Sage, JT; Sjodin, T; Wang, W; Ye, X | 1 |
| Austin, CJ; Jamie, JF; Kosim-Satyaputra, P; Matin, A; Mizdrak, J; Parker, MW; Polekhina, G; Roberts, TH; Sirijovski, N; Truscott, RJ; Willows, RD | 1 |
| Hargrove, MS; Hoy, JA; Kundu, S; Trent, JT; Weiland, TR | 1 |
| Ciaccio, C; Coletta, M; De Sanctis, G; Fasciglione, GF; Fiorucci, L; Gioia, M; Marini, S; Santucci, R; Sinibaldi, F | 1 |
| Bottin, H; Boussac, A; Ducruet, JM; Kirilovsky, D; Ortega, JM; Roncel, M; Rutherford, AW; Sugiura, M; Wilson, A; Zurita, JL | 1 |
| Falzone, CJ; Lecomte, JT; Nothnagel, HJ; Vu, BC; Vuletich, DA | 1 |
| Kitagawa, T; Mogi, T; Nakamura, H; Uchida, T | 1 |
| Daltrop, O; Ferguson, SJ; Harvat, EM; Hong, L; Kitagawa, T; Stevens, JM; Uchida, T | 1 |
| Ishikawa, H; Ishimori, K; Morishima, I; Takahashi, S | 1 |
| Koesling, D; Russwurm, M | 1 |
| Andrews, H; Burnap, RL; Eaton-Rye, JJ; Li, Z | 1 |
| Igarashi, J; Kitagawa, T; Sagami, I; Sato, A; Sato, E; Shimizu, T; Uchida, T | 1 |
| Bonilla-Rodriguez, GO; Canduri, F; de Azevedo, WF; Dos Santos, GC; Lombardi, FR; Olivieri, JR; Peres, P | 1 |
| Fukuzono, S; Han, MH; Kanda, K; Matsui, T; Sasakura, Y; Shimizu, T; Yoshimura-Suzuki, T | 1 |
| Antalík, M; Augustynski, J; Bánó, M; Dawson, JH; Fedurco, M; Glascock, MC; Indiani, C; Sedlák, E; Smulevich, G | 1 |
| Ishimori, K; O'Brian, MR; Yang, J | 1 |
| Bertero, MG; Blasco, F; Boroumand, N; Ginet, N; Palak, M; Rothery, RA; Strynadka, NC; Weiner, JH | 1 |
| Coon, MJ; Peng, HM; Vatsis, KP | 1 |
| Guo, Z; Lu, Y; Wang, Z; Yeung, N; Zhao, X | 1 |
| Brandolin, G; Dahout-Gonzalez, C; Dassa, EP; Dianoux, AC | 1 |
| Foley, E; Kakkar, R; Kamensky, Y; Kulmacz, RJ; Liu, W; Palmer, G | 1 |
| Bischof, D; Braun, M; Lee, D; Pervushin, K; Thöny-Meyer, L | 1 |
| Kitagawa, T; Sagami, I; Sato, A; Sato, E; Shimizu, T; Uchida, T | 1 |
| Allen, JW; Ferguson, SJ; Leach, N | 1 |
| Amadei, A; Anselmi, M; Bossa, C; Brunori, M; Daidone, I; Di Nola, A; Vallone, B | 1 |
| Lu, Y; Nilges, MJ; Zhao, X | 1 |
| Albrecht, T; Haehnel, W; Hildebrandt, P; Li, W; Ulstrup, J | 1 |
| Cheesman, MR; Ferguson, SJ; Gordon, EH; Zajicek, RS | 1 |
| Ascenzi, P; Bolognesi, M; Burmester, T; de Sanctis, D; Dewilde, S; Hankeln, T; Moens, L; Nardini, M; Pesce, A; Ponassi, M; Vonrhein, C | 1 |
| Falzone, CJ; Lecomte, JT; Vu, BC | 1 |
| Choi, PS; Scholes, CP; Shapleigh, JP; Usov, OM | 1 |
| Hori, H; Ishikawa, H; Ishimori, K; Iwai, K; Kato, M; Kirisako, T; Tokunaga, F | 1 |
| Burmester, T; Dewilde, S; Hamdane, D; Hankeln, T; Hoa, GH; Kiger, L; Marden, MC; Moens, L; Uzan, J | 1 |
| Battistuzzi, G; Bellei, M; Borsari, M; Di Rocco, G; Ranieri, A; Sola, M | 1 |
| Kakinuma, K; Maru, Y; Nishino, T | 1 |
| Blouin, G; Dantsker, D; Friedman, JM; Olson, JS; Roche, C; Samuni, U | 1 |
| Kawada, N; Kitagawa, T; Makino, M; Mizutani, Y; Ohta, T; Sawai, H; Shiro, Y; Sugimoto, H; Uno, T; Yoshizato, K | 1 |
| Djordjevic, S; Kendall, SL; Movahedzadeh, F; Rison, SC; Sardiwal, S; Stoker, NG | 1 |
| McLean, KJ; Mewies, M; Munro, AW; Papadopoulou, ND; Raven, EL; Seward, HE; Svistunenko, DA | 1 |
| Kitagawa, T; Ohta, T; Pinakoulaki, E; Soulimane, T; Varotsis, C | 1 |
| Hederstedt, L; Lewin, A; Throne-Holst, M | 1 |
| Casella, L; Coletta, M; Dallacosta, C; De Sanctis, G; Fasciglione, GF; Marini, S; Monzani, E; Santucci, R; Sinibaldi, F | 1 |
| Morais, F; Pereira, IA; Pires, RH; Teixeira, M; Venceslau, SS; Xavier, AV | 1 |
| Hsu, PY; Tsai, AL; Wang, JS; Wang, LH; Yeh, HC | 1 |
| Echalier, A; Fülöp, V; Goodhew, CF; Pettigrew, GW | 1 |
| Chait, BT; Fushitani, K; Gorr, TA; Kao, WY; Knapp, JE; Qin, J; Riggs, AF; Riggs, CK; Smith, SS | 1 |
| Bhaskaran, S; Esquerra, RM; Goldbeck, RA; Kliger, DS; Mendoza, JL; Olson, JS; Ortega, C; Soman, J | 1 |
| Brash, AR; Kitagawa, T; Tosha, T; Uchida, T | 1 |
| McDonald, MJ; Vasudevan, G | 1 |
| Burstyn, JN; Clark, RW; Pinkert, JC | 1 |
| Degtyarenko, I; Nieminen, RM; Rovira, C | 1 |
| Berthomieu, C; Boussac, A; Marboutin, L | 1 |
| Car, R; De Angelis, F; Jarzecki, AA; Spiro, TG | 1 |
| Barry, BA; Einarsdóttir, O | 1 |
| Aono, S; Nakajima, H; Rubtsov, IV; Yoshihara, K; Zhang, T | 1 |
| Chung, SY; Conrad, M; Roberts, GP; Youn, H | 1 |
| Borel, F; de Groot, A; de Rosny, E; Fontecilla-Camps, JC; Gaillard, J; Jouve, HM; Jullian-Binard, C; Pebay-Peyroula, E | 1 |
| Ascenzi, P; Bocedi, A; Bolognesi, M; Burmester, T; de Sanctis, D; Dewilde, S; Hankeln, T; Moens, L | 1 |
| Chan, AC; I Rosell, F; Lelj-Garolla, B; Mauk, AG; Murphy, ME; Pedersen, KA | 1 |
| Iwaki, M; Puustinen, A; Rich, PR; Wikström, M | 1 |
| Hori, H; Nakanishi, N; Okamoto, H; Takeuchi, F; Tamura, A; Tsubaki, M | 1 |
| Cartron, ML; Ferguson, SJ; Zajicek, RS | 1 |
| Knappenberger, JA; Kuriakose, SA; Lecomte, JT; Nothnagel, HJ; Vu, BC; Vuletich, DA | 1 |
| Jaffer, N; Jia, Z; Suits, MD | 1 |
| Cramer, WA; Gunderson, WA; Hendrich, MP; Zatsman, AI; Zhang, H | 1 |
| Burstyn, JN; Clark, RW; Lee, AJ; Roberts, GP; Youn, H | 1 |
| Czjzek, M; Delepierre, M; Izadi-Pruneyre, N; Lecroisey, A; Létoffé, S; Wandersman, C | 1 |
| Braun, M; García-Rubio, I; Gromov, I; Schweiger, A; Thöny-Meyer, L | 1 |
| Boscherini, F; Cordone, L; Francia, F; Giachini, L; Venturoli, G | 1 |
| Mandaci, S; Oztürk, M | 1 |
| Benson, DR; Cowley, AB | 1 |
| Rutkowska-Zbik, D; Stochel, G; Witko, M | 1 |
| Cordova, JM; Ghirlanda, G; Hilcove, SA; Lear, JD; Noack, PL | 1 |
| Halder, P; Hargrove, MS; Hoy, JA; Smagghe, BJ | 1 |
| Raghothama, S; Rai, J; Sahal, D | 1 |
| Burkhard, KA; Wilks, A | 2 |
| Christensen, O; Ferguson, SJ; Harvat, EM; Stevens, JM; Thöny-Meyer, L | 1 |
| Beeghley, CA; Graf, CB; Liang, Q; Miller, GT; Timkovich, R | 1 |
| Liu, JG; Naruta, Y; Tani, F | 1 |
| Boycheva, S; Brittain, T; Hsiao, HC; Watmough, NJ | 1 |
| Bowler, BE; Kurchan, E; Tzul, FO | 1 |
| Altun, A; Shaik, S; Thiel, W | 1 |
| Kamensky, Y; Kulmacz, RJ; Liu, W; Palmer, G; Tsai, AL | 1 |
| Bendall, DS; Hirst, J; Howe, CJ; Luisi, BF; Marcaida, MJ; Moorlen, RJ; Reda, T; Schlarb-Ridley, BG; Wastl, J; Worrall, JA | 1 |
| Baddam, S; Bandi, S; Bowler, BE | 1 |
| Casella, L; Gullotti, M; Monzani, E; Santagostini, L | 1 |
| Casella, L; Granata, A; Monzani, E; Roncone, R | 1 |
| Bowman, SE; Bren, KL; Elliott, SJ; Hahn, MA; Levin, BD; Michel, LV; Russell, BS; Ye, T | 1 |
| Brunori, M; Cutruzzolà, F; Rinaldo, S | 1 |
| Nakanishi, N; Takeuchi, F; Tsubaki, M | 1 |
| Abel, CJ; Chen, E; Goldbeck, RA; Kliger, DS | 1 |
| Alam, M; Ascenzi, P; Bolli, A; Coletta, M; Dewilde, S; Fago, A; Hoogewijs, D; Moens, L; Thijs, L; Trandafir, F; Van Doorslaer, S; Vinck, E; Wan, X; Weber, RE | 1 |
| Heinrichs, DE; Mack, J; Pluym, M; Stillman, MJ; Vermeiren, CL | 1 |
| Bolognesi, M; Estrin, DA; Martí, MA; Nadra, AD; Pesce, A | 1 |
| Bhakta, MN; Block, DR; Lansky, IB; Lukat-Rodgers, GS; Rodgers, KR; Wilks, A | 1 |
| Caillet-Saguy, C; Czjzek, M; Delepierre, M; Guigliarelli, B; Izadi-Pruneyre, N; Lecroisey, A; Lukat-Rodgers, GS; Piccioli, M; Rodgers, KR; Turano, P | 1 |
| Cammack, R; Gareta, EG; Marritt, SJ; McKie, AT; Oakhill, JS | 1 |
| Ibrahim, M; Spiro, TG; Xu, C | 1 |
| Halder, P; Hargrove, MS; Smagghe, BJ | 1 |
| Heimdal, J; Rydberg, P; Ryde, U | 1 |
| Mayer, JM; Warren, JJ | 1 |
| Bhaskaran, S; Esquerra, RM; Goldbeck, RA; Jensen, RA; Kliger, DS; Lintner, BW; Mendoza, JL; Pillsbury, ML | 1 |
| Davis, RB; Lecomte, JT | 1 |
| Arcovito, A; Brunori, M; D'Angelo, P; Della Longa, S; Mancini, G; Moschetti, T; Vallone, B | 1 |
| Berry, EA; Walker, FA | 1 |
| Bocian, DF; Carragher, B; Cho, SH; Diers, JR; Finn, MG; Kuzelka, J; Lander, GC; Potter, C; Prasuhn, DE; Quispe, JD; Strable, E; Udit, AK | 1 |
| Fufezan, C; Gunner, MR; Zhang, J | 1 |
| Bandi, S; Bowler, BE | 3 |
| da Silva, GF; Kamensky, Y; Kulmacz, RJ; Liu, W; Palmer, G; Rogge, CE; Shinkarev, VP; Tsai, AL | 1 |
| Chowdhury, R; Ehrismann, D; Hardy, AP; Hewitson, KS; Holmes, SL; McDonough, MA; Schofield, CJ | 1 |
| Fufezan, C; Koder, RL; Negron, C | 1 |
| Hori, H; Kiyota, K; Nakanishi, N; Park, SY; Takeuchi, F; Tsubaki, M; Uno, T | 1 |
| Dreher, C; Hellwig, P; Hielscher, R; Prodöhl, A; Schneider, D | 1 |
| Ehlerding, A; Hvelplund, P; Kadhane, U; Kirketerp, MB; Lykkegaard, MK; Nielsen, SB; Panja, S; Wyer, JA; Zettergren, H | 1 |
| Capece, L; Estrin, DA; Marti, MA | 1 |
| Gandra, EA; Moura, VP; Santini, TD; Seixas, FA | 1 |
| Dawson, JH; Goodin, DB; Osborne, RL; Terentis, AC; Vetter, SW | 1 |
| Aitken, SM; Belew, MS; Quazi, FI; Willmore, WG | 1 |
| Leitgeb, S; Nidetzky, B | 1 |
| Bowman, SE; Bren, KL | 2 |
| Munegumi, T; Tai, H; Yamamoto, Y | 1 |
| Alam, M; Ascenzi, P; Bolli, A; Bolognesi, M; Coletta, M; Desmet, F; Dewilde, S; Gourlay, L; Moens, L; Nardini, M; Pesce, A; Sisinni, L; Thijs, L; Van Doorslaer, S; Wan, X | 1 |
| Bowler, BE; Kurchan, E; Roder, H; Tzul, FO | 1 |
| Mogi, T | 2 |
| Brøndsted Nielsen, S; Ehlerding, A; Kadhane, U; Kirketerp, MB; Lykkegaard, MK; Wyer, JA; Zettergren, H | 1 |
| de Visser, SP; Straganz, GD | 1 |
| Kobayashi, K; Mogi, T; Tagawa, S | 1 |
| Anderson, JL; Dutton, PL; Koder, RL; Moser, CC; Reddy, KS; Solomon, LA | 1 |
| Frawley, ER; Kranz, RG | 1 |
| Merchant, SS | 1 |
| Banerjee, S; Calisto, BM; Carpena, X; Fita, I; Furtmüller, PG; Obinger, C; Rovira, C; Schroettner, K; Soudi, M; Stampler, J; Vidossich, P | 1 |
| Falzone, CJ; Lecomte, JT; Majumdar, A; Pond, MP; Vuletich, DA | 1 |
| Gorres, KL; Pua, KH; Raines, RT | 1 |
| Ford, PC; Heinecke, J; Richter-Addo, GB; Tan, H; Yi, J | 1 |
| Arcovito, A; Boffi, A; Bonamore, A; D'Angelo, P; Hazemann, JL | 1 |
| Ai, YJ; Fang, WH; Luo, Y; Zhang, F | 1 |
| Moiseeva, SA; Postnikova, GB; Shekhovtsova, EA | 1 |
| Airola, MV; Crane, BR; Kabir, M; Patel, BA; Rousseau, DL; Sudhamsu, J; Yeh, SR | 1 |
| Allen, JW; Chan, W; Ferguson, SJ; Goddard, AD; Mavridou, DA; Rao, F; Richardson, DJ; Stevens, JM | 1 |
| Herzik, MA; Marletta, MA; Olea, C; Tran, R; Winter, MB; Yoon, J | 1 |
| Bowler, BE; Tzul, FO | 1 |
| Furutani, Y; Hoshino, T; Ikezaki, A; Imai, K; Kandori, H; Komatsu, T; Nakamura, M; Neya, S; Ode, H; Suzuki, M | 1 |
| Buschmann, S; Ermler, U; Langer, JD; Michel, H; Warkentin, E; Xie, H | 1 |
| Desmet, F; Dewilde, S; El Mkami, H; Moens, L; Smith, G; Thijs, L; Van Doorslaer, S | 1 |
| Liao, LF; Lin, YW; Ying, TL | 1 |
| Asher, WB; Bren, KL | 2 |
| Kern, M; Kranz, RG; Scheithauer, J; Simon, J | 1 |
| Behera, RK; Goyal, S; Mazumdar, S | 1 |
| Lewis-Ballester, A; López-Garriga, J; Pietri, R; Ramos-Santana, B; Román-Morales, E; Vinogradov, SN | 1 |
| Atkins, WM; Bowman, MK; Cheesman, MJ; Primak, A; Rettie, AE; Roberts, AG | 1 |
| Brøndsted Nielsen, S; Wyer, JA | 1 |
| Bernhardt, PV; Hanson, GR; Kappler, U; Rapson, TD | 1 |
| Abu Tarboush, N; Davidson, VL; Feng, M; Jensen, LM; Tachikawa, H; Wilmot, CM | 1 |
| Ascenzi, P; Coletta, M; Polticelli, F; Santucci, R | 1 |
| Franzen, S; Ghiladi, RA; Reeder, BJ; Svistunenko, DA; Thompson, MK | 1 |
| Asard, H; Bérczi, A; Desmet, F; Van Doorslaer, S; Zimányi, L | 1 |
| Adney, EM; Lecomte, JT; Nothnagel, HJ; Pond, MP; Preimesberger, MR; Winer, BY | 1 |
| Dewilde, S; Ioanitescu, AI; Moens, L; Van Doorslaer, S | 1 |
| DiCarlo, CM; Erman, JE; Vitello, LB | 1 |
| Boechi, L; Estrin, DA; Martì, MA; Mazzarella, L; Merlino, A; Sica, F; Vergara, A | 1 |
| Arroyo Mañez, P; Boechi, L; Estrin, DA; Lu, C; Luque, FJ; Martí, MA; Poole, RK; Shepherd, M; Wilson, JL; Yeh, SR | 1 |
| Burstyn, JN; Freeman, KM; Kraus, JP; Majtan, T; Smith, AT; Su, Y | 1 |
| Cheesman, MR; Johnston, AW; Le Brun, NE; Singleton, C; Todd, JD; White, GF | 1 |
| Howes, BD; Mazzarella, L; Merlino, A; Prisco, Gd; Smulevich, G; Verde, C; Vergara, A | 1 |
| Bennati, M; Brodhun, F; Denysenkov, V; Feussner, I; Fielding, AJ; Koch, C; Pievo, R | 1 |
| Catarino, T; Quintas, PO; Todorovic, S; Turner, DL | 1 |
| Dewilde, S; Geuens, E; Hoogewijs, D; Kiger, L; Lechauve, C; Marden, MC; Moens, L; Tilleman, L | 1 |
| Daskalakis, V; Pinakoulaki, E; Varotsis, C | 1 |
| Musayev, FN; Richter-Addo, GB; Safo, MK; Thomas, LM; Yi, J | 1 |
| He, C; Knipp, M; Neya, S | 1 |
| Enyenihi, AA; Lyutvinskiy, Y; Yang, H; Ytterberg, AJ; Zubarev, RA | 1 |
| Kaila, VR; Sharma, V; Wikström, M | 1 |
| Battistuzzi, G; Bellei, M; Furtmüller, PG; Gruber, C; Obinger, C; Soudi, M; Stampler, J | 1 |
| Agnew, CR; Brady, RL; Burton, NM; Kelly, SL; Lamb, DC; Warrilow, AG | 1 |
| Bretsnyder, EC; Kranz, RG; Rodgers, KR; San Francisco, B | 1 |
| Ishimori, K; Kitagawa, T; Sagami, I; Shimizu, T; Uchida, T | 1 |
| Hu, C; Liu, X; Lu, Y; Wang, J; Yu, Y; Zhang, W | 1 |
| Arora, DP; Boon, EM; Dai, Z; Farquhar, ER | 1 |
| Bhakta, MN; Fleming, KG; O'Neill, MJ; Wilks, A | 1 |
| Lutz, S; Meuwly, M | 1 |
| Alfonso-Prieto, M; Rovira, C; Vidossich, P | 1 |
| Cui, FC; Liu, JY; Liu, W; Pan, XL | 1 |
| Aono, S; Ishikawa, H; Mizutani, Y; Yoshida, Y | 1 |
| Fontaine, M; Joseph, P; Li, S; Steinke, L; Suman, SP | 1 |
| Dornevil, K; Geng, J; Liu, A | 1 |
| Lecomte, JT; Majumdar, A; Pond, MP | 1 |
| Ghirardi, ML; Gilles-Gonzalez, MA; Murthy, UM; Posewitz, MC; Wecker, MS | 1 |
| de Serrano, V; Dumarieh, R; Franzen, S; Ghiladi, RA; Thompson, M; Zhao, J | 1 |
| Davidson, VL; Hedman, B; Jensen, LM; Meharenna, YT; Poulos, TL; Sarangi, R; Wilmot, CM | 1 |
| Anderson, BJ; Belchik, SM; Lipton, MS; Merkley, ED; Monroe, ME; Park, J; Shi, L; Smith, RD | 1 |
| da Silva, GF; Kamensky, YA; Palmer, G; Shinkarev, VP | 1 |
| Balakrishnan, G; Hu, Y; Spiro, TG | 1 |
| Abu Tarboush, N; Davidson, VL; Geng, J; Liu, A; Shin, S | 1 |
| Bernad, S; Bocahut, A; Derrien, V; Guittet, E; Lescop, E; Sacquin-Mora, S; Sebban, P | 1 |
| Bretsnyder, EC; Kranz, RG; San Francisco, B | 1 |
| Bowler, BE; Khan, MK | 1 |
| Badyal, SK; Guimero, A; Gumiero, A; Leeks, T; Moody, PC; Raven, EL | 1 |
| Andersen, EM; Khajo, A; Koder, RL; Magliozzo, RS; Zhang, L | 1 |
| Gilles-Gonzalez, MA; Gondim, AC; Gonzalez, G; Sousa, EH; Tuckerman, JR | 1 |
| Andrew, CR; Lamarre, I; Martin, JL; Negrerie, M; Yoo, BK | 1 |
| Bielecki, M; Olczak, M; Olczak, T; Smalley, JW; Wojaczyński, J; Wójtowicz, H | 1 |
| Neya, S | 1 |
| Bidon-Chanal, A; Guallar, V; Lucas, F; Luque, FJ; Spyrakis, F; Viappiani, C | 1 |
| Huang, MJ; Liao, MS; Watts, JD | 1 |
| Davidson, VL; Dornevil, K; Geng, J; Liu, A | 1 |
| Budiman, K; Daskalakis, V; Kitagawa, T; Ludwig, B; Ohta, T; Pinakoulaki, E; Richter, OM; Varotsis, C | 1 |
| Alvarez, B; Ballou, DP; Banerjee, R; Carballal, S; Cuevasanta, E; Gherasim, C; Kabil, O; Marmisolle, I | 1 |
| Franzen, S; Jiang, S; Swartz, P; Wright, I | 1 |
| Bergquist, BB; Bowler, BE; Cherney, MM; Junior, CC | 1 |
| Benabbas, A; Champion, PM; Dawson, JH; Denisov, I; Du, J; Sligar, SG; Sun, Y; Ye, X; Zeng, W | 1 |
| Koszelak-Rosenblum, M; Malkowski, MG; Zhu, G | 1 |
| Amendola, EJ; Castorino, JD; Cerda, JF; Fritz, AL; Guzman, CX; Houchins, DN; Roeder, MH | 1 |
| Ishikawa, H; Mizuno, M; Mizutani, Y; Shibayama, N; Yamada, K | 1 |
| Hargis, JC; Vankayala, SL; Woodcock, HL | 1 |
| Hirota, S; Imai, K; Ishigami, I; Matsuo, T; Nagao, S; Neya, S; Nishimura, R; Ogura, T; Shibata, T; Shoji, O; Suzuki, A; Tai, H; Watanabe, Y; Yamamoto, Y | 1 |
| Kranz, RG; San Francisco, B; Sutherland, MC | 1 |
| Adak, S; Bose, M; Mukherjee, S; Roy, J; Saha, R; Sen Santara, S | 1 |
| Bali, S; Ferguson, SJ; Lea, SM; Raux-Deery, E; Rollauer, S; Roversi, P; Warren, MJ | 1 |
| Her, AS; Huo, Y; Liu, P; Raso, F; Song, H; Zhen, Z | 1 |
| Hough, MA; Reeder, BJ | 1 |
| Basran, J; Blakeley, MP; Casadei, CM; Concilio, MG; Fielding, AJ; Gumiero, A; Metcalfe, CL; Moody, PC; Murphy, EJ; Ostermann, A; Raven, EL; Schrader, TE; Teixeira, SC | 1 |
| Bu, W; Im, S; Meagher, J; Pearl, NM; Rwere, F; Shaik, S; Stuckey, J; Sun, C; Tarasev, M; Usharani, D; Waskell, L; Yang, Y; Zhang, H | 1 |
| Bhagi-Damodaran, A; Lu, Y; Marshall, NM; Petrik, ID; Robinson, H | 1 |
| Arai, H; Haufschildt, K; Heinz, DW; Kriegler, TM; Layer, G; Neumann, A; Schmelz, S; Streif, J | 1 |
| Aono, S; Ishikawa, H; Mizutani, Y; Nakatani, K | 1 |
| Babbitt, SE; Bretsnyder, EC; Kranz, RG; Lukat-Rodgers, GS; Mendez, DL; Rodgers, KR; San Francisco, B | 1 |
| Li, J; Lu, N; Peng, YY; Tian, R | 1 |
| Herzik, MA; Jonnalagadda, R; Kuriyan, J; Marletta, MA | 1 |
| Johnson, EA; Lecomte, JTJ; Preimesberger, MR; Rice, SL | 1 |
| Che, EN; Fedosov, SN; Ortiz de Orué Lucana, D; Torda, AE; Wedderhoff, I | 1 |
| Blumberger, J; Breuer, M; Butt, JN; Rosso, KM | 1 |
| Bhat, R; Dey, SG; Kundu, S; Mukhi, N; Salhotra, S; Seal, M; Uppal, S; Zaidi, FK | 1 |
| Bren, KL; Elliott, SJ; Levin, BD; Sullivan, KK; Walsh, KA | 1 |
| Frizzell, S; Gladwin, MT; Ragireddy, V; Sparacino-Watkins, CE; Tejero, J | 1 |
| Lamarre, I; Martin, JL; Negrerie, M; Rappaport, F; Yoo, BK | 1 |
| Bhardwaj, J; Goyal, M; Prakash, K; Puri, SK; Siddiqui, AJ; Soni, A | 1 |
| de Roos, A; Edens, L; Kliphuis, A; Schaap, A; Schouten, O; Shi, J; Vink, C; Vonk, B; Zheng, C | 1 |
| Bosch, J; Boucher, LE; Lecomte, JT; Preimesberger, MR; Rice, SL; Schlessman, JL | 1 |
| English, AM; Peslherbe, GH; Shadrina, MS | 1 |
| Arnold, FH; Buller, AR; Chio, L; Heel, T; McIntosh, JA | 1 |
| Hoshino, T; Kawaguchi, AT; Nagai, M; Nagatomo, S; Neya, S; Yoneda, T | 1 |
| Adrian, SA; Akbas, N; Allen, CE; Collins, DP; Dawson, JH; Dixon, DW; Draganova, EB; Lukat-Rodgers, GS; Rodgers, KR; Schmitt, MP | 1 |
| Lecomte, JT; Majumdar, A; Preimesberger, MR; Que, L; Rice, SL | 1 |
| Borek, A; Cieluch, E; Kuleta, P; Osyczka, A; Pintscher, S; Sarewicz, M | 1 |
| Sharma, V; Wikström, M | 1 |
| Brewitz, HH; Galler, K; Goradia, N; Hagelueken, G; Imhof, D; Kühl, T; Neugebauer, U; Ohlenschläger, O; Popp, J; Schiemann, O; Schubert, E; Syllwasschy, B | 1 |
| Arnold, FH; Cahn, JK; Dodani, SC; Kiss, G; Pande, VS; Su, Y | 1 |
| Gao, SQ; Lin, YW; Nie, CM; Tan, X; Wen, GB; Wu, LB; You, Y; Yuan, H | 1 |
| Asghari, SM; Esmaeili, S; Khodarahmi, R; Kooshk, MR | 1 |
| Fojtikova, V; Kavan, D; Man, P; Martínek, V; Martinkova, M; Shimizu, T; Stranava, M; Vaněk, O | 1 |
| Amartely, H; Dvir, H; Kornitzer, D; Nasser, L; Pinsky, M; Weissman, Z | 1 |
| Ashrafi-Kooshk, MR; Khodarahmi, R | 1 |
| Barr, I; Burstyn, JN; Guo, F; Hines, JP; Jacob, JP; Lukat-Rodgers, GS; Rodgers, KR; Smith, AT | 1 |
| Becker, AJ; Imhof, D; Kühl, T; Ohlenschläger, O; Silbermann, K; Wißbrock, A | 1 |
| Bernad, S; Butcher, D; Derrien, V; Miksovska, J; Sebban, P | 1 |
| Banerjee, R; Filipovic, MR; Kumutima, J; Lehnert, N; Lewis, BE; Ruetz, M; Stemmler, TL | 1 |
| Hayashi, T; Morita, Y; Oohora, K; Tang, N | 1 |
| Ädelroth, P; Bhagi-Damodaran, A; Kahle, M; Lu, Y; Shi, Y; Zhang, Y | 1 |
| Dojun, N; Ishimori, K; Sekine, Y; Uchida, T | 1 |
| Majumdar, S; Meneghini, LM; Poulos, TL; Tripathi, S; Weiss, GA; Woodworth, MA | 1 |
| Beattie, AD; Benaragama, I; Meesapyodsuk, D; Qiu, X | 1 |
| Dey, SG; Ghosh, C; Mukherjee, S; Seal, M | 1 |
| Church, JS; Dunn, CJ; Harmer, JR; Liu, JW; Musameh, M; Noble, CJ; Rapson, TD; Riley, MJ; Sriskantha, A; Sutherland, TD; Warden, AC; Woodhead, A | 1 |
| Chang, S; Ishikawa, H; Mizuno, M; Mizutani, Y | 1 |
| Lecomte, JTJ; Majumdar, A; Nye, DB; Preimesberger, MR | 1 |
| Fita, I; Rovira, C; Wang, B | 1 |
| Dereven'kov, IA; Hannibal, L; Koifman, OI; Makarov, SV; Makarova, AS; Molodtsov, PA | 1 |
| Bhagi-Damodaran, A; Dwaraknath, S; Harnden, KA; Hosseinzadeh, P; Lu, Y; Mirts, EN; Moënne-Loccoz, P; Reed, JH; Sandoval, BA; Shi, Y; Sponholtz, MR; Wang, S; Zhang, Y; Zhu, Q | 1 |
| Marconi, RT; Miller, DP; Oliver, LD; Sarkar, J | 1 |
| English, AM; Kathiresan, M | 1 |
| Lecomte, JTJ; Nye, DB | 1 |
| Hori, H; Ikushiro, H; Kamiya, N; Miyahara, I; Nagami, A; Sawai, T; Shimeno, Y; Takai, T; Yano, T | 1 |
| Fukuda, Y; Inoue, T; Kim, J | 1 |
| Shibata, T; Shimayama, C; Uchida, K; Yoshitake, J | 1 |
| Matsui, T; Song, JW | 1 |
| Du, KJ; Gao, SQ; Liao, F; Lin, YW; Liu, C; Tan, X; Wei, CW; Yuan, H | 1 |
| Li, J; Ma, F; Peng, Q; Sun, CJ; Sun, HL; Wang, Z; Wu, Q; Xiao, H; Xu, W; Zhao, J | 1 |
| Fernandes, TM; Morgado, L; Salgueiro, CA; Turner, DL | 1 |
| Dojun, N; Ishimori, K; Muranishi, K; Uchida, T | 1 |
| Ichiyanagi, K; Ohki, M; Park, SY; Sato-Tomita, A; Shibayama, N | 1 |
| Abbasnezhad, A; Abd El-Ghafar, OA; Abhilash, L; Abouzid, KAM; Achberger, AM; Ackerman, S; Akhatayeva, Z; Akin, D; Al-Kaysi, RO; Alakhdar, AA; Alame, M; Aleksic Sabo, V; Alinezhadbalalami, N; Allen, JD; Alonso, JM; Alqatani, S; Alsayed, B; Álvarez Larraondo, M; Alvarez, M; Amini, SB; An, Z; Anasir, MI; Anderson, GH; Andremont, A; Andrés, S; Angel, S; Anigboro, AA; Anini, Y; Antonides, CFJ; Arafa, K; Arafa, RK; Aryal, UK; Asbaghi, O; Assefa, MK; Atyah, M; Avwioroko, OJ; Ayora-Talavera, G; Azpilikueta, A; Azyazov, VN; Ba, YF; Bachmann, KF; Badoual, J; Bae, SJ; Baek, SH; Bahrami, B; Bai, J; Baid-Agrawal, S; Bailey, MR; Baillie, JK; Balani, N; Balcar, VJ; Banica, T; Banks, L; Barb, J; Bardeen, CJ; Barrett, HE; Bartnikowski, N; Bashir, R; Battaglia, M; Bautista-Hernández, V; Becker, B; Beekman, FJ; Benidir, M; Benjelloun, M; Bentley, RF; Bergé, J; Berger, D; Bernsen, MR; Berraondo, P; Bhattacharya, R; Bhayani, SB; Bi, W; Bi, X; Bi, YL; Bi, Z; Bian, K; Biesecker, LG; Billadeau, DD; Blaszczyk, R; Blum, JL; Boachie, R; Boelte, K; Bogers, AJJC; Boileau, I; Bonduelle, C; Bonny, O; Bonsu, JM; Boos, LA; Borges-Argáez, R; Bouchard, PA; Boudot, C; Bourgeade-Delmas, S; Boutet-Robinet, E; Boyle, AJ; Branigan, D; Briones, S; Broniowska, KA; Brossas, JY; Brown, WA; Brzezinska, J; Buitron, G; Burnier, M; Bursulaya, B; Burton, PR; Bush, AA; Busuttil, RW; Cabello-Aguilar, S; Cáceres-Farfán, M; Cacheux, V; Caffrey, PJ; Cai, B; Cai, Q; Cai, S; Cai, Y; Calders, P; Cammarota, G; Campbell, DA; Cancelli, C; Cao, Q; Cao, WH; Cao, X; Capet, M; Capoluongo, E; Carey, ME; Carnero, M; Carrasco, LI; Carreno, J; Carrillo-Reyes, J; Casini, I; Cassar, M; Catalan, G; Cattamanchi, A; Cazares-Granillo, M; Celie, B; Cen, YK; Cena, H; Cerbo, RM; Ceron, E; Cetina-Montejo, L; Chaâbane-Banaoues, R; Chabanet, C; Chace-Donahue, F; Chalfun-Júnior, A; Chan-Balan, R; Chang, CS; Chen, CS; Chen, D; Chen, J; Chen, L; Chen, PN; Chen, Q; Chen, S; Chen, W; Chen, WP; Chen, X; Chen, Z; Cheng, H; Cheng, J; Cheng, Q; Cheng, T; Chi, T; Chianelli, D; Chieppa, M; Child, CJ; Cho, JH; Cho, JY; Chogtu, B; Choi, GH; Choi, J; Choi, M; Choi, NG; Cholu, CO; Chow, ES; Chowdhury, AH; Chu, PC; Chu, Q; Chu, S; Chua, H; Chung, T; Chunyan, L; Church, JS; Civardi, E; Cobiella, J; Colinge, J; Collado, CJ; Collins, TJ; Cong, LM; Conkrite, KL; Cope, SJ; Corbett, JA; Cornet, M; Cornillot, E; Corvaisier, S; Costes-Martineau, V; Courtioux, B; Coussens, M; Covino, M; Criado, A; Cui, J; Cui, Y; Cunitz, BW; Curry, AE; Cussó, L; D'Urzo, AD; D'Urzo, KA; Dabbous, S; Dahlgren, RA; Dai, H; Dai, T; Dai, W; Dalinghaus, M; Dang, S; Davalos, RV; Davidson, H; de Andrea, CE; De Angelis, M; de Blois, E; de Carvalho, PA; De Clercq, E; De Giuseppe, R; de Jong, M; De Langhe, S; De Oliveira, L; de Souza Pinto Lemgruber, R; de Souza, LB; de Swart, J; De Wandele, I; de Woestijne, PCV; Delaney, S; Delorme, M; Delvenne, P; Deng, L; Deng, Z; Denkinger, CM; der Meulen, MHV; Deraeve, C; Desco, M; DeSilva, S; Destere, A; Dhali, A; Di Ciano, P; Dias-Santagata, D; Diskin, SJ; Djè, MK; Doddipatla, S; Doerr, AJ; Dokla, EME; Domiciano, D; Domingo, N; Dong, C; Dong, J; Dong, Q; Dong, S; Dong, X; Dong, Z; Douair, I; Douglas, TA; Doyle, SM; Drain, PK; Du, K; Du, L; Du, Q; Du, S; Duan, C; Duan, H; Duan, J; Duan, S; Duan, W; Dueluzeau, R; Dukic, L; Dunmire, BL; Duvauchelle, T; Dymek, B; Dzwonek, K; Earnest, A; Eckardt, KU; El Ghadraoui, L; El Massoudi, S; Elloumi, F; Elnour, IE; Embarak, S; Ende, M; England, K; Enikeev, D; Enyedy, I; Epple, R; Erickson, GE; Eriksson, J; Erndt-Marino, J; Errachidi, F; Etxeberria, I; Evan, AP; Fairlamb, AH; Falahi, E; Fan, CC; Fan, H; Fan, M; Fan, MZ; Fan, S; Fan, Y; Fang, CS; Fang, J; Fang, X; Fang, Z; Farmany, A; Farooqi, A; Farouk, HO; Fazelipour, S; Feng, D; Feng, J; Feng, JX; Feng, YL; Ferraz, SL; Ferreira, CR; Figenshau, RS; Finn, AV; Fiseha, T; Fleischer, AS; Fogleman, AD; Fontaine, O; Ford, CR; Fouladvand, F; Four, M; Fousteri, G; Francis, JR; Fraser, JF; Frazier, RP; Fu, H; Fu, P; Fu, YJ; Fujishima, A; Fuster, V; Gabilan, JC; Gagliani, N; Gai, QY; Galán-Arriola, C; Gale, P; Galimova, GR; Galkin, A; Gallo, A; Gallo, AA; Gang, DD; Ganschow, S; Gao, C; Gao, F; Gao, GP; Gao, H; Gao, K; Gao, M; Gao, MY; Gao, P; Gao, R; Gao, S; Gao, WJ; Gao, Y; Garbacz, P; García Ruiz, L; Garcia, EM; Garofoli, F; Gasbarrini, A; Gattinoni, L; Gaudig, M; Gbureck, U; Ge, X; Genko, N; Gentile, GL; George, MW; Gerety, GF; Gestwicki, JE; Geusens, PP; Ghassemi, M; Giardina, JD; Giebultowicz, JM; Gifford, CA; Gijsen, FJH; Gilfillan, R; Gilson, E; Gingl, K; Giuliano, C; Glybochko, P; Goessler, W; Gofflot, S; Golab, J; Goldstein, A; Golebiowski, A; Gómez, L; Gómez-Carballo, J; Gonçalves, PEO; Gonzales, R; Gonzalez-Cotto, M; González-Fernández, D; Gonzalez-Lopez de Turiso, F; Goodman, JM; Govinda Raju, S; Grimm, J; Gross, AJ; Gruenheid, S; Gu, C; Gu, FF; Gu, S; Gu, Z; Guest, RL; Gui, C; Gui, J; Guillem, A; Guo, G; Guo, L; Guo, Q; Guo, S; Guo, SW; Guo, W; Guo, Y; Guo, YG; Guo, Z; Guretzky, JA; Haenggi, M; Hahn, MS; Hakkola, J; Halim, AA; Hampel, D; Han, B; Han, BH; Han, D; Han, G; Han, J; Han, LZ; Han, R; Han, S; Han, X; Han, Z; Handley, MA; Hanke, I; Hannongbua, S; Hao, P; Happ, JT; Hara, M; Haraux, F; Hare, JL; Harper, JD; Hartley, AM; Harvey, E; Hashimoto, K; Hassan, HM; Hautajärvi, H; Hayton, TW; He, C; He, H; He, HJ; He, WP; He, Y; He, Z; Hedrick, V; Heffernan, JK; Hegrová, J; Heidarimoghadam, R; Helms, K; Hengphasatporn, K; Henry, D; Herrmann, TRW; Hesson, T; Himmelbauer, MK; Hindle, A; Hoffmann, R; Hogg, N; Hong, KB; Hong, SK; Honjol, Y; Hood, C; Hsi, RS; Hsu, JL; Hu, B; Hu, BC; Hu, D; Hu, H; Hu, J; Hu, K; Hu, M; Hu, MK; Hu, T; Hu, W; Hu, Y; Hu, Z; Hua, S; Huang, H; Huang, J; Huang, L; Huang, M; Huang, P; Huang, X; Huang, Y; Huang, Z; Hukkanen, J; Hung, MC; Huo, X; Hyötyläinen, T; Ianiro, G; Ibanez, B; Imran, M; Ireland, S; Irwin, MS; Ishiguro, H; Jackowski, K; Jackson, C; Jacob, SI; Jahromy, MH; Jakob, SM; Jang, J; Javvaji, PK; Jefferson, KK; Jena, P; Ji, H; Jiang, F; Jiang, GH; Jiang, H; Jiang, J; Jiang, X; Jiang, Z; Jiao, J; Jiménez, A; Jin, X; Jincai, W; Jintao, X; Jo, K; Jofra, T; Johari, Y; Johnson, ACM; Jones, JH; Josephine Fauci, A; Juhl, AK; Jun, S; Kaiser, RI; Kajioka, J; Kajiyama, H; Kalliyil, A; Kalthur, SG; Kamalanathan, M; Kamaldinov, T; Kanaani, L; Kang, D; Kang, J; Kang, S; Känsäkoski, P; Kaplan, DL; Karwan, M; Kasibhatla, S; Kaur, A; Kawazoe, Y; Ke, C; Keyser, J; Khalique, A; Khan, IT; Kharshoum, RM; Kher, R; Kherani, J; Ki, KK; Kikkawa, F; Kikkawa, R; Kim, BT; Kim, EH; Kim, GA; Kim, GD; Kim, HB; Kim, HG; Kim, JS; Kim, MJ; Kim, SI; Kim, SJ; Kim, Y; King, K; Kinyamu-Akunda, J; Kirkkala, T; Kjaer-Sorensen, K; Kleppinger, EL; Kloner, RA; Klopfenstein, TJ; Knappe, D; Knezevic, P; Kobos, LM; Kohli, M; Kolano, L; Kolodgie, FD; Kolte, AP; Koneru, B; Kong, D; Kong, F; Kong, X; Konggidinata, MI; Köpke, M; Koski, KG; Kotsis, F; Köttgen, A; Kouakou-Kouamé, CA; Kraemer, US; Krane, V; Krehbiel, CR; Krenning, BJ; Kretzschmar, D; Ku, KB; Kubota, Y; Kulich, P; Kumar, NG; Kupiec-Weglinski, JW; Lalani, SS; Lan, X; Landfeldt, E; Langenberg, E; Lapauw, B; Larkin, J; Lassoued, MA; Laukhtina, E; Laura Martinez, J; Laveillé, A; Lavela, P; Law, AD; Lazraq, A; Le Foll, B; Lee, BK; Lee, C; Lee, CS; Lee, EJ; Lee, EY; Lee, G; Lee, HY; Lee, JH; Lee, JJ; Lee, JO; Lee, JS; Lee, R; Lei, H; Lei, P; Lellouche, F; Lennerz, JK; Leong, W; Leslie, I; Lessem, E; Levin, M; Levinger, I; Li, C; Li, CW; Li, CX; Li, CY; Li, D; Li, H; Li, HM; Li, J; Li, L; Li, LM; Li, N; Li, S; Li, W; Li, X; Li, XX; Li, Y; Li, Z; Li, ZL; Li, ZX; Lian, Q; Liang, C; Liang, GH; Liang, H; Liang, J; Liang, X; Liao, CX; Liao, R; Ličbinský, R; Lim, YS; Lima, HK; Lin, JG; Lin, L; Lin, S; Lin, WP; Lin, Z; Liso, M; Liu, BX; Liu, C; Liu, H; Liu, J; Liu, M; Liu, Q; Liu, S; Liu, SF; Liu, SL; Liu, T; Liu, W; Liu, X; Liu, XB; Liu, Y; Liu, YY; Liu, Z; Liu, ZQ; Lobo, M; Loitzenbauer, M; López, F; Lopez, G; López, GJ; Lou, Z; Lu, IC; Lu, J; Lu, M; Lu, W; Lu, X; Lu, Y; Luhovyy, BL; Luna-Abanto, J; Luo, J; Luo, K; Luo, L; Luo, M; Luo, W; Luo, X; Luo, XM; Lv, Y; Lv, YQ; Lyu, HD; Lyu, J; Ma, C; Ma, G; Ma, L; Ma, Q; Ma, X; Ma, Y; Macha, SJ; MacLean, E; Mahalapbutr, P; Maina, T; Malfait, F; Malfertheiner, MV; Malzert-Fréon, A; Mansouri, E; Mao, C; Marcellin, E; Marchiori, PER; Marcotte, DJ; Maréchal, A; Maric, N; Maris, JM; Maron, L; Marti, CN; Martínez-Milla, J; Mateo, J; Mather, K; Mathison, CJN; Matthay, MA; Maxwell, CL; Mazier, D; Mazumder, D; Mazurkiewicz, M; Mazzucchelli, TG; McAuley, DF; Mccoy, K; McVicar, DW; Mebel, AM; Mech, A; Meester, EJ; Meiselbach, H; Melero, I; Ménard, G; Meng, X; Mengya, Y; Merle, G; Meunier, B; Mfarrej, B; Mi, K; Migueliz, I; Mikuška, P; Miladi, K; Miletich, R; Millar, JE; Mills, MR; Milne, R; Minute, L; Misiak, M; Mo, F; Modi, A; Mok, F; Molina, C; Mollen, CJ; Molteni, V; Montalto, M; Montet, D; Monti, MC; Moor, MB; Moravec, P; Morsiani, C; Murillo, E; Murugan, P; Muslem, R; Myers, RK; N'guessan, FK; Nabil, H; Nadal, J; Nadeem, M; Nafady, MM; Nafie, MS; Nair, HP; Nakano, R; Nance, J; Naren, N; Neil, CJ; Nelson, J; Nery, FC; Netsch, C; Nguyen, TH; Ni, L; Ni, YX; Nie, W; Nielsen, LK; Nigam, K; Nikolayev, AA; Nishiyama, M; Niu, LL; Niu, PP; Nock, BA; Noer, PR; Noll, G; Noll, S; Norenberg, JP; Nowicka, J; Nutho, B; O'Connor, M; Obonyo, NG; Ochiai, T; Ochoa, MC; Oh, BL; Oh, S; Olczak, J; Olivares, X; Ommurugan, B; Oosthuizen, MC; Operario, D; Orešič, M; Oshima, K; Otano, I; Ou, Y; Owen, TW; Oxvig, C; Pacey, V; Pai, M; Paik, H; Paiva, R; Palmieri, EM; Palpant, N; Pan, L; Pan, Q; Panahi, S; Pang, B; Pang, ZC; Pannecouque, C; Paris, L; Park, D; Park, DJ; Park, E; Park, EC; Park, IH; Park, JH; Park, JI; Park, S; Passmore, MR; Pattaranggoon, NC; Paun, M; Pedersen, S; Pedron, J; Peng, M; Peng, X; Penzhorn, BL; Pérez-Camargo, D; Perez-Maldonado, R; Pérez-Vicente, C; Pham, TD; Pickering, L; Pickersgill, NA; Pinault, E; Pinotsis, N; Plan, M; Pocino, K; Poh, CL; Pons, EDC; Popoff, MR; Porri, D; Pourmand, A; Pratviel, G; Prudente, DO; Qi, H; Qi, N; Qian, LY; Qiao, L; Qiao, Q; Qin, QP; Qiu, N; Qiu, SW; Qu, F; Quan, M; 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; Shao, J; Shao, ZH; Shasha, Y; Shaw, K; Sheeba, V; Shekar, K; Shen, G; Shen, H; Shen, XD; Shen, Y; Sherrell, PC; Shete, PB; Shi, AX; Shi, J; Shi, JH; Shi, S; Shi, X; Shigeta, Y; Shimbo, A; Shin, E; Sikka, N; Silhavy, TJ; Simanon, N; Simard, S; Simon, J; Simon, M; Simpson, SD; Simundic, AM; Since, M; Singh, B; Singhroy, DN; Sinisterra, OT; Smith, EH; Sobreira, TJP; Solanes, N; Somasundar, Y; Sommerer, C; Sonei, A; Song, B; Song, E; Song, J; Song, M; Song, Y; Soo Lee, M; Sorensen, MD; Sournia-Saquet, A; Spaepen, E; Spirk, D; Srivastava, S; Stancill, JS; Stanczak, PS; Starenki, D; Starr, F; Step, DL; Steubl, D; Stigliani, JL; Stráská, J; Sträter, N; Su, ZZ; Sudano, I; Suen, JY; Suh, HJ; Sui, ZY; Suico, JG; Suleiman, K; Sumon, K; Sun, HB; Sun, J; Sun, L; Sun, LL; Sun, M; Sun, Q; Sun, W; Sun, X; Sun, XF; Sun, Y; Sun, YB; Sun, YH; Sun, YN; Sun, Z; Sunada, K; Suzuki, S; Sylvan, JB; Takala, J; Talla, D; Tamir, Z; Tan, SJ; Tanda, S; Tang, H; Tang, J; Tang, LF; Tang, SJ; Tang, Y; Tao, FB; Tappel, R; Taratkin, M; Teijeira, Á; Tellew, JE; Thomas, AM; Thomas, SG; Thomson, SR; Tian, J; Tie, Y; Tirado, JL; Tolonen, A; Tosato, G; Tronnet, A; Tsai, S; Turtoi, A; Turtoi, E; Tvrdoňová, M; Tyagi, A; Tzou, DT; Uddin Ahmad, Z; Urias, E; Usawachintachit, M; Ustriyana, P; Utsumi, F; Vacca, M; Vaculovič, T; Vaidya, SS; Valentin, A; Valgepea, K; van den Berg, P; van den Bergh, JP; van der Heiden, K; van Gaalen, K; Van Gemert, W; van Haard, PMM; van Hest, JCM; Vecchiarelli, E; Večeřa, Z; Venkatesh, R; Verhaeghe, P; Verhagen, HJ; Vetter, JM; Vieira, D; Vilchez-Tschischke, JP; Villena-Gutierrez, R; Villoslada Terrones, V; Vital-Jacome, M; Voelkl, J; Vogel, K; Vogrin, S; Volke, D; von Bahr, V; Vysloužil, J; Wade, TL; Wagner-Gillespie, M; Walsh, SW; Wan, LJ; Wan, SP; Wang, AL; Wang, B; Wang, BY; Wang, C; Wang, D; Wang, F; Wang, H; Wang, HR; Wang, HY; Wang, J; Wang, JY; Wang, K; Wang, L; Wang, LF; Wang, P; Wang, Q; Wang, R; Wang, SF; Wang, SP; Wang, SR; Wang, T; Wang, W; Wang, WP; Wang, X; Wang, XJ; Wang, Y; Wang, YL; Wang, YN; Wáng, YXJ; Wang, Z; Wang, ZF; Wang, ZY; Waning, B; Warner, JM; Washington, SL; Watson, AK; Wei, B; Wei, C; Wei, F; Wei, X; Wei, Y; Wemhoff, AP; Wen, Z; Weng, TT; Wesdemiotis, C; Wheeler, DA; Wildner, M; Wilson, BK; Wirth, LJ; Wissler, M; Wu, F; Wu, G; Wu, J; Wu, KH; Wu, MC; Wu, P; Wu, PK; Wu, S; Wu, W; Wu, X; Wu, XP; Wu, Y; Wyatt, E; Wyllie, S; Xia, Y; Xiao, BH; Xiao, SZ; Xiao, W; Xiao, X; Xiao, Z; Xie, D; Xie, K; Xie, X; Xie, Y; Xie, YF; Xin, S; Xin, Z; Xing, Q; Xing, WQ; Xiong, D; Xiong, X; Xu, C; Xu, D; Xu, F; Xu, G; Xu, H; Xu, J; Xu, JY; Xu, L; Xu, N; Xu, W; Xu, X; Xu, Y; Xu, YM; Xue, H; Xue, J; Xue, Z; Yan, R; Yan, SQ; Yan, W; Yan, X; Yan, Z; Yang, C; Yang, D; Yang, F; Yang, FC; Yang, G; Yang, J; Yang, M; Yang, P; Yang, Q; Yang, R; Yang, S; Yang, SJ; Yang, TWW; Yang, X; Yang, Y; Yang, Z; Yao, C; Yao, L; Yao, LP; Yao, M; Yao, T; Yao, W; Yao, Y; Yaseen, T; Yazdani, V; Ye, J; Ye, S; Yerys, BE; Yi, HWL; Yi, JL; Yin, F; Yin, J; Yin, Y; Yin, Z; Yong, ZP; Yongli, S; Yoo, JS; Yoshikawa, N; You, Q; Yu, B; Yu, CQ; Yu, H; Yu, HG; Yu, J; Yu, L; Yu, Q; Yu, X; Yu, Y; Yu, YK; Yu, Z; Yuan, Q; Yuan, R; Yuan, W; Yuan, X; Yuan, Y; Zager, RA; Zagozdzon, A; Zaller, N; Zang, YP; Zappi, ME; Zelikoff, JT; Zeman, T; Zhai, X; Zhan, P; Zhang, B; Zhang, C; Zhang, G; Zhang, H; Zhang, HB; Zhang, J; Zhang, JS; Zhang, L; Zhang, M; Zhang, Q; Zhang, RX; Zhang, S; Zhang, T; Zhang, W; Zhang, WH; Zhang, X; Zhang, XX; Zhang, Y; Zhang, YQ; Zhang, YW; Zhang, Z; Zhang, ZH; Zhao, D; Zhao, FL; Zhao, K; Zhao, L; Zhao, M; Zhao, R; Zhao, S; Zhao, W; Zhao, WG; Zhao, X; Zhao, Y; Zheng, G; Zheng, J; Zheng, S; Zheng, W; Zheng, Y; Zheng, YG; Zhong, Z; Zhou, C; Zhou, D; Zhou, H; Zhou, HY; Zhou, L; Zhou, Q; Zhou, X; Zhou, Y; Zhou, YL; Zhou, Z; Zhu, J; Zhu, L; Zhu, N; Zhu, X; Zhu, XF; Zhu, Y; Zhu, Z | 1 |
| Olczak, T; Siemińska, K; Ślęzak, P; Smalley, JW; Śmiga, M | 1 |
| Demeler, B; Iranzo, O; Ivancich, A; Koebke, KJ; Kühl, T; Lojou, E; Pecoraro, VL; Schoepp-Cothenet, B | 1 |
| Harvey, JN; Roos, G | 1 |
| Ishimori, K; Omura, I; Uchida, T; Umetsu, S | 1 |
| Abbruzzetti, S; Barker, AJ; Becana, M; Bruno, S; Cerullo, G; Pérez-Rontomé, C; Viappiani, C; Villar, I | 1 |
| Chand, S; Perera, R; Pierce, BS; Ray, S; Samanta, S; Yadav, P | 1 |
| Capece, L; Estrin, DA; Julió Plana, L; Lecomte, JTJ; Martinez Grundman, JE; Schlessman, JL | 1 |
| Bari, SE; Bieza, SA; Diz, V; Estrin, DA; Murgida, DH; Oviedo Rouco, S | 1 |
| Kitagawa, T; Nagai, M; Nagatomo, S | 1 |
| Albetel, AN; Dailey, HA; Lanzilotta, WN; Medlock, AE; Najahi-Missaoui, W; Shiferaw, MT | 1 |
| Adamczyk, K; Blumberger, J; Butt, JN; Clarke, TA; Edwards, MJ; Hall, CR; Jeuken, LJC; Jiang, X; Meech, SR; Piper, SEH; Sazanovich, IV; Towrie, M; van Wonderen, JH; Wu, X; Zhang, H | 1 |
| De-Simone, SG; Lechuga, GC; Morel, CM; Napoleão-Pêgo, P; Provance, DW | 1 |
| Ayers, TN; Bocian, K; DeMartino, AW; Kaliszuk, SJ; Morgan, NI; Ragireddy, V; Sparacino-Watkins, CE; Tejero, J; Tong, Q | 1 |
| Cramer, WA; Zakharov, SD | 1 |
| Hirao, H; Liu, S; Xia, S | 1 |
| Davies, GJ; Diaz, DE; Franco-Cairo, JP; Walton, PH | 1 |
| Nolan, K; Wang, Y | 1 |
| Cain, MD; Du, D; Goldberg, DE; Klein, RS; Nguyen, ST; Russo, I; Wu, Q; Wychrij, D | 1 |
| Ahmad, MS; Chiorean, S; Daub, E; Gyamfi, H; Honek, JF; Poole, A; Su, Z; Suttisansanee, U; Taylor, RM; Urquhart, T; van der Ven, AM | 1 |
Reviews
24 review(s) available for histidine and heme
| Article | Year |
|---|---|
Structure and mechanism of haemoglobin.
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.
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.
Topics: Amino Acid Sequence; Animals; Bacteria; Cytochrome c Group; Heme; Histidine; Iron; Ligands; Methionine; Mitochondria; Phylogeny; Protein Binding; Protein Conformation | 1985 |
Inorganic nutrition.
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].
Topics: Globins; Heme; Histidine; Iron; Myoglobin; Oxygen; Protein Conformation; Rotation | 1995 |
The construction of metal centers in proteins by rational design.
Topics: Calcium; Enzymes; Heme; Histidine; Iron-Sulfur Proteins; Metals; Proteins | 1998 |
Studying the structure and regulation of soluble guanylyl cyclase.
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.
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.
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.
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.
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.
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.
Topics: Amino Acid Motifs; Catalysis; Heme; Histidine; Iron; Proteins | 2008 |
The chemistry and biochemistry of heme c: functional bases for covalent attachment.
Topics: Heme; Histidine; Models, Molecular; Molecular Structure | 2008 |
Cytochromes: Reactivity of the "dark side" of the heme.
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.
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.
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.
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.
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.
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.
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.
Topics: Amyloid beta-Peptides; Animals; Heme; Histidine; Humans; Peroxidases; Protein Aggregates; Protein Multimerization | 2017 |
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; 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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; 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YAP-Signaling Proteins; Yogurt; Young Adult; Zebrafish; Zebrafish Proteins; Ziziphus | 2016 |
The histidine brace: nature's copper alternative to haem?
Topics: Copper; Heme; Histidine; Oxidation-Reduction | 2023 |
Trials
1 trial(s) available for histidine and heme
Other Studies
721 other study(ies) available for histidine and heme
| Article | Year |
|---|---|
A proton magnetic resonance study of the distal histidine of soybean Leghemoglobin. Effects of nicotinate and other heme ligands.
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.
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.
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.
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.
Topics: Amino Acid Sequence; Cytochromes; Escherichia coli; Heme; Histidine; Ligands; Magnetic Resonance Spectroscopy; Methionine; Protein Conformation; X-Ray Diffraction | 1978 |
Structure of oxymyoglobin.
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.
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.
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.
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].
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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).
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Topics: Cyanides; Cytoskeletal Proteins; Erythrocyte Membrane; Glutathione; Heme; Hemin; Hemolysis; Histidine; Humans; Membrane Proteins | 1987 |
Cryogenic stabilization of myoglobin photoproducts.
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.
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.
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.
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.
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.
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.
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].
Topics: Alkylation; Beta-Globulins; Binding Sites; Heme; Histidine; Humans; Mucoproteins; Protein Binding; Serum Globulins | 1967 |
Electron paramagnetic resonance of nitric oxide cytochrome C.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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 ).
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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].
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.
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].
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.
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.
Topics: Animals; Cetacea; Chemical Phenomena; Chemistry; Heme; Histidine; Mollusca; Myoglobin; Peptides | 1970 |
Kinetics of the reaction of hybrid-heme hemoglobins with carbon monoxide.
Topics: Binding Sites; Carbon Monoxide; Chemical Phenomena; Chemistry; Deuterium; Heme; Hemoglobins; Histidine; Iron; Methemoglobin | 1970 |
The terminal groups of chlorocruorin.
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.
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)].
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.
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.
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.
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.
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.
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).
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.
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.
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.
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.
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.
Topics: Chemical Phenomena; Chemistry, Physical; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Oxidation-Reduction; Pyridines; Spectrophotometry | 1966 |
The stereochemistry of peroxidase catalysis.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Topics: Animals; Heme; Histidine; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Myoglobin; Protein Conformation; Whales | 1981 |
Structural changes at the heme induced by freezing hemoglobin.
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.
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.
Topics: Animals; Chironomidae; Diptera; Heme; Hemoglobins; Histidine; Larva; Magnetic Resonance Spectroscopy; Protein Conformation; Solutions | 1981 |
Resonance Raman spectroscopy of hemoglobin.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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].
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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?
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Topics: Animals; Bivalvia; Heme; Hemoglobins; Histidine; Hydrogen-Ion Concentration; Hydroxides; Oxidation-Reduction; Spectrum Analysis, Raman | 1999 |
The heme environment in barley hemoglobin.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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).
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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).
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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).
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].
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].
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.
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.
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.
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?
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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'.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Topics: Amino Acid Sequence; Bacterial Proteins; Cysteine; Heme; Hemeproteins; Histidine; Ligands; Trans-Activators | 2006 |
Drosophila nuclear receptor E75 is a thiolate hemoprotein.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Topics: Electrochemistry; Heme; Hemoglobins; Histidine; Iron; Kinetics; Ligands; Nitric Oxide; Oxidation-Reduction | 2008 |
Protonation of the proximal histidine ligand in heme peroxidases.
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.
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.
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.
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.
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.
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.
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.
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).
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).
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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?
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.
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.
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.
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.
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.
Topics: Biological Transport; Catalysis; Cell Membrane; Chloroplasts; Cytochromes c; Heme; Histidine | 2009 |
Essential role of proximal histidine-asparagine interaction in mammalian peroxidases.
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.
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.
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.
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.
Topics: Actinomycetales; Animals; Crystallography, X-Ray; Heme; Hemoglobins; Histidine; Horses; Iron; Myoglobin; Spectrophotometry, Infrared | 2010 |
Nonadiabatic histidine dissociation of hexacoordinate heme in neuroglobin protein.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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 .
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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''.
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.
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.
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.
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.
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?
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.
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.
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.
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.
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.
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.
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.
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.
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).
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.
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.
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.
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).
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.
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.
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).
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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).
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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
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.
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.
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.
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.
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.
Topics: Bacterial Proteins; Binding Sites; Heme; Hemoglobins; Histidine; Synechocystis; Truncated Hemoglobins | 2018 |
Heme-dependent Inactivation of 5-Aminolevulinate Synthase from Caulobacter crescentus.
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.
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.
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.
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.
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.
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.
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.
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.
Topics: Carbon Monoxide; Crystallography, X-Ray; Diffusion; Heme; Hemoglobins; Histidine; Humans; Ligands; Models, Molecular; Protein Conformation; Protein Subunits; Recombinant Fusion Proteins | 2020 |
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.
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
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.
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
Topics: Heme; Hemoglobins; Histidine; Medicago truncatula; Plant Proteins; Protein Binding | 2021 |
Abiological catalysis by myoglobin mutant with a genetically incorporated unnatural amino acid.
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.
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.
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.
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.
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.
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.
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.
Topics: Cytoglobin; Globins; Heme; Histidine; Lipids; Mutation; Nitric Oxide; Nitrite Reductases; Nitrites | 2022 |
Concerning the enigmatic cytochrome b-559 of oxygenic photosynthesis.
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.
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.
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.
Topics: Animals; Endothelial Cells; Heme; Hemeproteins; Histidine; Inflammation; Iron; Malaria, Cerebral; Malaria, Falciparum; Mice | 2023 |
Molecular Engineering of
Topics: Bacterial Proteins; Escherichia coli; Ferritins; Gold; Heme; Histidine; Metal Nanoparticles | 2023 |