tyrosine has been researched along with heme in 278 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 51 (18.35) | 18.7374 |
| 1990's | 47 (16.91) | 18.2507 |
| 2000's | 96 (34.53) | 29.6817 |
| 2010's | 75 (26.98) | 24.3611 |
| 2020's | 9 (3.24) | 2.80 |
| Authors | Studies |
|---|---|
| Morgan, WT; Muller-Eberhard, U; Sutor, RP | 1 |
| Tsong, TY | 1 |
| Hrkal, Z; Kodícĕk, M; Suttnar, J; Vodrázka, Z | 1 |
| Keller, RM; Wüthrich, K | 1 |
| Erecińska, M; Vanderkool, JM | 1 |
| Kulmacz, RJ; Palmer, G; Tsai, AL | 1 |
| Frauenhoff, MM; Scott, RA | 1 |
| Davies, AM; Greenwood, C; Guillemette, JG; Mauk, AG; Moore, GR; Smith, M; Thurgood, AG | 1 |
| Eling, TE; Kulmacz, RJ; Marnett, LJ; Smith, WL; Tsai, A | 1 |
| Boynton, SB; Carter, BE; Connor, E; Fowler, B; Roth, KS; Wyss, PA | 1 |
| Bloomer, JR; Freese, D; Glock, M; Pascual-Leone, A; Payne, W; Rank, JM; Sharp, H | 1 |
| Halvorsen, S; Kvittingen, EA; Steen-Johnsen, J; Søvik, O | 1 |
| Carter, BE; Moses, LC; Roth, KS; Spencer, PD | 1 |
| Di Primo, C; Douzou, P; Hui Bon Hoa, G; Sligar, S | 1 |
| Bain, MD; Bingham, P; Chalmers, RA; Jones, M; Purkiss, P; Stacey, TE | 1 |
| Garber, EA; Luntz, TL; Margoliash, E; Schejter, A | 1 |
| La Mar, GN; Lecomte, JT; Smit, JD; Winterhalter, KH | 1 |
| Dalvit, C; Wright, PE | 1 |
| Fisher, MT; Sligar, SG | 1 |
| DeGroot, LJ; Hati, RN | 1 |
| Dickerson, RE | 1 |
| Winfield, ME | 1 |
| Hayashi, A; Imai, K; Morimoto, H; Suzuki, T; Watari, H | 1 |
| Byckova, V; Labie, D; Travers, F; Wajcman, H | 1 |
| Babul, G; Rysavy, R; Stellwagen, E | 1 |
| Morgan, WT; Riehm, JP | 1 |
| de Prailauné, S; Nunez, J; Pommier, J | 1 |
| Bucci, E | 1 |
| Antonini, E; Bonaventura, C; Bonaventura, J; Bossa, F; Brunori, M; Giardina, B; Wyman, J | 1 |
| Ho, C; Ladner, JE; Perutz, MF; Simon, SR | 1 |
| Perutz, MF | 1 |
| Danner, DJ; Morrison, M | 1 |
| Nagai, M; Sugita, Y; Yoneyama, Y | 1 |
| Salhany, JM | 1 |
| Gibson, QH; Olson, JS | 1 |
| Huntley, TE; Strittmatter, P | 1 |
| Folin, M; Galiazzo, G; Gennari, G; Jori, G | 1 |
| Billups, C; Horwitz, J; Kay, E; Shannon, LM; Strickland, EH; Wilchek, M | 1 |
| Antonini, E; Forlani, L; Phelps, C | 1 |
| McKellar, JR; Weightman, JA; Williams, RJ | 1 |
| Gilmore, RA; Sherman, F; Stewart, JW | 1 |
| Jackson, HF; Lea, CH; Parr, LJ | 1 |
| McGowan, EB; Stellwagen, E | 2 |
| Guerritore, D; Zito, R | 1 |
| Bucci, E; Fronticelli, C; Ragatz, B | 1 |
| Efron, ML; Shahidi, NT | 1 |
| Horwitz, J; Kay, E; Shannon, LM; Strickland, EH | 1 |
| Stellwagen, E | 1 |
| Herskovits, TT | 1 |
| Johnson, BP; Li, TK | 1 |
| Galiazzo, G; Jori, G; Scoffone, E | 1 |
| Shichi, H | 1 |
| Baudras, A; Di Franco, A; Iwatsubo, M; Labeyrie, F | 1 |
| Stellwagen, E; Van Rooyan, S | 1 |
| Krogmann, DW; Markley, JL; Ulrich, EL | 1 |
| Grenier, A; Meister, A; New, MI; Rifkind, AB; Sassa, S; Starkman, H; Steinherz, PG; Stoner, E; Wellner, D; Wellner, VP | 1 |
| Bernhardt, R; Jänig, GR; Makower, A; Rabe, H; Ruckpaul, K | 1 |
| Kappas, A; Sassa, S | 1 |
| Eads, JC; Jordan, T; Spiro, TG | 1 |
| Friedman, AE; Goodin, DB; Hartmann, C; Miller, VP; Ortiz de Montellano, PR | 1 |
| Babcock, GT; Garavito, RM; Hoganson, CW; Hsi, LC; Smith, WL | 1 |
| Joshi, AA; McDonald, MJ | 1 |
| Giardina, B; Martorana, GE; Miggiano, AG; Minotti, G; Mordente, A; Petiti, T; Santini, SA | 1 |
| Coggins, JR; Kelly, SM; Lindsay, JG; Malarkey, K; McKnight, J; Miles, JS; Munro, AW; Price, NC; Thomson, AJ | 1 |
| Bersch, B; Bianco, P; Blanchard, L; Dolla, A; Forest, E; Guerlesquin, F; Marion, D; Wall, J | 1 |
| Bogumil, R; Brayer, GD; Luo, Y; Mauk, AG; Maurus, R; Smith, M; Tang, HL | 1 |
| Berghuis, AM; Brayer, GD; Guillemette, JG; Smith, M | 1 |
| Chen, DY; Vergères, G; Waskell, L; Wu, FF | 1 |
| Adachi, S; Egawa, T; Ishimori, K; Kitagawa, T; Makino, R; Morishima, I; Nagano, S; Watanabe, Y | 1 |
| Boynton, S; Chu, J; Roth, KS; Wyss, PA | 1 |
| Barnard, ML; Diep, D; Gurdian, S; Ladd, M; Turrens, JF | 1 |
| Beri, R; Chandra, R | 1 |
| Friedman, JM; Goldberg, DE; Huang, J; Huang, S; Kloek, AP | 1 |
| Adak, S; Banerjee, RK; Mazumder, A | 1 |
| Delepelaire, P; Delepierre, M; Ghigo, JM; Wolff, N | 1 |
| Arese, M; Bellelli, A; Brunori, M; Cutruzzolà, F; Grasso, S | 1 |
| Mortuza, GB; Whitford, D | 1 |
| Chance, MR; Friedman, JM; Goldberg, DE; Huang, S; Kloek, AP; Miller, LM; Peterson, ES; Vidugiris, G; Wang, J; Wittenberg, JB | 1 |
| Horiuchi, Y; LaFleur, GJ; Wessel, GM | 1 |
| Dohse, B; Mathis, P; Oesterhelt, D; Ortega, JM | 1 |
| Blackledge, M; Dolla, A; Guerlesquin, F; Marion, D; Sebban-Kreuzer, C | 1 |
| Fei, MJ; Inoue, N; Libeu, CP; Mizushima, T; Nakashima, R; Shinzawa-Itoh, K; Tomizaki, T; Tsukihara, T; Yamaguchi, H; Yamashita, E; Yao, M; Yaono, R; Yoshikawa, S | 1 |
| Hasegawa, J; Igarashi, Y; Kobayashi, Y; Kodama, T; Kyogoku, Y; Sambongi, Y; Yamazaki, K; Yamazaki, T; Yoshida, T; Yu, Y | 1 |
| Lukat-Rodgers, GS; Rexine, JL; Rodgers, KR | 1 |
| Das, TK; Gennis, RB; Pecoraro, C; Rousseau, DL; Tomson, FL | 1 |
| Behr, J; Grzybek, S; Hellwig, P; Ludwig, B; Mäntele, W; Michel, H | 1 |
| Minetti, M; Pietraforte, D; Scorza, G | 1 |
| Hildebrand, DP; Liu, Y; Loehr, TM; Mauk, AG; Moënne-Loccoz, P; Ortiz de Montellano, PR; Wilks, A | 1 |
| Ullrich, V; Yesilkaya, A; Zou, M | 1 |
| Bambai, B; Koehn, JA; Kulmacz, RJ; Marshall, PJ; Palmer, G; Tsai, Al; Wu, G | 1 |
| Buse, G; Hellwig, P; Mäntele, W; Soulimane, T | 1 |
| Kitagawa, T; Nagai, M; Nagatomo, S; Tsuneshige, A; Yonetani, T | 1 |
| Quaroni, L; Smith, WE | 1 |
| Balabanli, B; Kamisaki, Y; Martin, E; Murad, F | 1 |
| Couture, M; Das, TK; Guertin, M; Lee, HC; Peisach, J; Rousseau, DL; Wittenberg, BA; Wittenberg, JB | 1 |
| Couture, M; Guertin, M; Ouellet, Y; Rousseau, DL; Yeh, SR | 1 |
| Ahmad, F; Ahmad, R; Sinha, A; Yadav, S | 1 |
| Arvai, AS; Bourne, Y; Putnam, CD; Tainer, JA | 1 |
| Behr, J; Hellwig, P; Mäntele, W; Michel, H | 1 |
| Das, TK; Ferguson-Miller, S; Gennis, RB; Lee, HM; Mills, D; Rousseau, DL | 1 |
| Adak, S; Stuehr, DJ; Wang, Q | 1 |
| Goodwin, DC; Marnett, LJ; Rowlinson, SW | 1 |
| Bendall, DS; Carrell, CJ; Cramer, WA; Howe, CJ; Ponamarev, MV; Schlarb, BG; Smith, JL | 1 |
| Pereira, MM; Teixeira, M; Verkhovskaya, ML; Verkhovsky, MI | 1 |
| Kitagawa, T; Mogi, T; Uchida, T | 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 |
| Daiber, A; Jung, C; Schmidt, P; Schöneich, C; Ullrich, V | 1 |
| Aki, M; Jin, Y; Kitagawa, T; Li, R; Nagai, M; Nagatomo, S; Sakai, H | 1 |
| Asokan, A; Auclair, K; Espiritu, B; La Mar, GN; Ortiz De Montellano, PR; Yeh, DC | 1 |
| Das, TK; Gennis, RB; Gordon, M; Rousseau, DL; Tomson, FL | 1 |
| Abraham, BD; Boutaud, O; Brash, AR; Dawson, JH; Gaffney, BJ; Shriner, A; Sono, M | 1 |
| Ascenzi, P; Bolognesi, M; Dewilde, S; Kiger, L; Marden, MC; Milani, M; Moens, L; Pesce, A; Van Hauwaert, ML; Vanfleteren, J | 1 |
| Marino, G; Minetti, M; Pietraforte, D; Salzano, AM; Scorza, G | 1 |
| Ludwig, B; Pfitzner, U; Pinakoulaki, E; Varotsis, C | 1 |
| Boffi, A; Draghi, F; Miele, AE; Vallone, B | 1 |
| Enemark, JH; Feng, C; Hazzard, JT; Hurley, JK; Rajagopalan, KV; Tollin, G; Wilson, HL | 1 |
| Allen, JW; Ferguson, SJ; Fülöp, V; Gordon, EH; Hajdu, J; Higham, CW; Löfqvist, M; Richter, CD; Sjögren, T | 1 |
| English, AM; Tsaprailis, G | 1 |
| Adak, S; Dawson, JH; Goodin, DB; Ikeda-Saito, M; Perera, R; Pond, AE; Sono, M; Stuehr, DJ; Tomita, T; Voegtle, HL | 1 |
| Bhaskar, B; Farmer, PJ; Immoos, CE; Poulos, TL; Shimizu, H; Sulc, F | 1 |
| Bian, K; Gao, Z; Murad, F; Weisbrodt, N | 1 |
| Ascenzi, P; Bolognesi, M; Guertin, M; Milani, M; Ouellet, H; Savard, PY | 1 |
| Lardinois, OM; Ortiz de Montellano, PR | 1 |
| Conover, RC; Daldal, F; Johnson, MK; Knaff, DB; Li, J; Osyczka, A; Qin, H | 1 |
| Girotto, S; Magliozzo, RS; Yu, S; Zhao, X | 1 |
| Abeysinghe, RD; Ball, T; Cukier, RI; Hsi, LC; Micielli, R; Mills, DA; Rieke, CJ; Seibold, SA; Smith, WL | 1 |
| HERMANS, J | 1 |
| BRESLOW, E | 1 |
| Debarbieux, L; Delepelaire, P; Izadi, N; Létoffé, S; Wandersman, C | 1 |
| Didik, J; Gebicka, L | 1 |
| Akutsu, H; Cusanovich, MA; Higuchi, Y; Ogata, H; Ohmura, T; Ozawa, K; Takayama, Y; Tomimoto, Y; Yasukawa, F | 1 |
| Rothery, RA; Weiner, JH; Zhao, Z | 1 |
| Cao, C; Huang, ZX; Wang, YF; Wang, YH; Wang, ZQ; Wu, H; Zhang, Q | 1 |
| Bigotti, MG; Brunori, M; Cutruzzolà, F; Musto, R; Travaglini-Allocatelli, C | 1 |
| Detweiler, CD; Guo, Q; Mason, RP | 1 |
| Hirota, S; Suzuki, M; Watanabe, Y | 1 |
| Chishiro, T; Liu, JG; Naruta, Y; Tachi, Y; Tani, F | 1 |
| Chen, Z; Ost, TW; Schelvis, JP | 1 |
| Aznar, C; Britt, RD; Brynda, M; Kim, SH; Michalczyk, R; Silks, LA; Unkefer, CJ; Woodruff, WH | 1 |
| Di Mascio, P; Dyszy, FH; Nantes, IL; Nascimento, OR; Prado, FM; Rinaldi, TA; Tersariol, IL | 1 |
| Célier, C; Grosclaude, J; Marden, MC; Pato, C; Rezaei, H | 1 |
| Bamm, VV; Shaklai, M; Shaklai, N; Tsemakhovich, VA | 1 |
| Proshlyakov, DA | 1 |
| Allen, JW; Cartron, ML; Ferguson, SJ; Richardson, DJ; Zajicek, RS | 1 |
| Herold, S; Kalinga, S; Matsui, T; Watanabe, Y | 1 |
| Jin, Y; Kitagawa, T; Nagai, M; Nagai, Y; Nagatomo, S | 1 |
| Bertrand, T; Brown, KA; Eady, NA; Jamart-Grégoire, B; Jones, JN; Nagy, JM; Raven, EL | 1 |
| Erickson, J; Londer, YY; Long, WC; Pessanha, M; Pokkuluri, PR; Salgueiro, CA; Schiffer, M | 1 |
| Akutsu, H; Harada, E; Kobayashi, R; Ozawa, K; Takayama, Y | 1 |
| Mehvar, R; Vuppugalla, R | 1 |
| Anderson, VE; Nukuna, BN; Sun, G | 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 |
| Olson, JS; Phillips, GN; Zhang, W | 1 |
| Cadilla, CL; Cruz, A; De Jesús, W; Garriga, JL; Granell, L; Leon, R; Lewis, A; Pietri, R | 1 |
| De la Rosa, MA; Díaz-Moreno, I; Díaz-Quintana, A; Ubbink, M | 1 |
| Andersson, KK; Barra, AL; Harbitz, E; Kolberg, M; Nordlander, E; Ryabova, ES; Rydberg, P; Ryde, U | 1 |
| Friedrich, J; Reif, M; Scharnagl, C | 1 |
| Ghiladi, RA; Knudsen, GM; Medzihradszky, KF; Ortiz de Montellano, PR | 1 |
| Abergel, C; Bruschi, M; Giudici-Orticoni, MT; Leroy, G; Lojou, E; Malarte, G | 1 |
| Cheesman, MR; Ferguson, SJ; Gordon, EH; Zajicek, RS | 1 |
| Hollenberg, PF; Lin, HL; Waskell, L; Zhang, H | 1 |
| Casella, L; Monzani, E; Nicolis, S; Pennati, A; Perani, E; Sanangelantoni, AM | 1 |
| Barra, AL; Böttger, LH; Contzen, J; Galander, M; Jung, C; Lendzian, F; Richter, M; Schünemann, V; Trautwein, AX | 1 |
| Mizutani, Y; Sato, A | 1 |
| Abraham, NG; Botros, FT; Goodman, AI; Schwartzman, ML; Stier, CT | 1 |
| Barbar, EJ; Deeb, RS; Gross, SS; Hajjar, DP; Hao, G; Lainé, M; Qiu, JH; Resnick, B; Upmacis, RK | 1 |
| Das, TK; Dewilde, S; Friedman, JM; Moens, L; Rousseau, DL | 1 |
| Bolognesi, M; Couture, M; Guertin, M; Milani, M; Ouellet, Y | 1 |
| Deeb, RS; Hajjar, DP; Upmacis, RK | 1 |
| Barry, BA; Einarsdóttir, O | 1 |
| Liao, WQ; Neuzil, J; Witting, PK | 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 |
| Giner, RM; Máñez, S; Olmos, A; Recio, MC; Ríos, JL | 2 |
| Czjzek, M; Delepierre, M; Izadi-Pruneyre, N; Lecroisey, A; Létoffé, S; Wandersman, C | 1 |
| Kulmacz, RJ; Palmer, G; Rogge, CE; Tsai, AL; Wang, JS; Wu, G | 1 |
| Liu, JG; Naruta, Y; Tani, F | 1 |
| Raghothama, S; Rai, J; Sahal, D | 1 |
| Abraham, NG; Botros, FT; Goodman, AI; Navar, LG; Olszanecki, R; Prieto-Carrasquero, MC | 1 |
| Bolognesi, M; Couture, M; Guertin, M; LaBarre, M; Milani, M; Ouellet, H | 1 |
| Hollenberg, PF; Lin, HL; Myshkin, E; Waskell, L | 1 |
| Kondo, R; Nonaka, D; Sasaki, S; Tsutsumi, Y; Wariishi, H | 1 |
| Basran, J; Bottrill, AR; Cooper, CE; Efimov, I; Mistry, SC; Pipirou, Z; Raven, EL; Svistunenko, DA | 1 |
| Bhakta, MN; Block, DR; Lansky, IB; Lukat-Rodgers, GS; Rodgers, KR; Wilks, A | 1 |
| Aono, S; El-Mashtoly, SF; Gu, Y; Kitagawa, T; Yoshimura, H; Yoshioka, S | 1 |
| Bigotti, MG; Cutruzzola, F; Hider, RC; Reeder, BJ; Wilson, MT | 1 |
| Abriata, LA; Cassina, A; Castro, L; Marín, M; Radi, R; Souza, JM; Tórtora, V; Vila, AJ | 1 |
| Ferguson, SJ; Harvat, EM; Redfield, C; Stevens, JM | 1 |
| Centola, F; Cutruzzolà, F; Goldfarb, D; Pecht, I; Radoul, M; Rinaldo, S | 1 |
| Cedervall, PE; Hooper, AB; Wilmot, CM | 1 |
| Cheung, C; Deeb, RS; Gross, SS; Hajjar, DP; Lamon, BD; Nuriel, T; Upmacis, RK | 1 |
| Deng, S; Derbyshire, ER; Marletta, MA | 1 |
| Balla, G; Balla, J; Csonka, T; Eaton, JW; Galajda, Z; Jeney, V; Méhes, G; Nagy, E; Smith, A; Soares, MP; Szentmiklósi, J; Varga, Z; Vercellotti, GM | 1 |
| Buschmann, S; Ermler, U; Langer, JD; Michel, H; Warkentin, E; Xie, H | 1 |
| Abu Tarboush, N; Davidson, VL; Feng, M; Jensen, LM; Tachikawa, H; Wilmot, CM | 1 |
| Brandman, R; Meitzler, JL; Ortiz de Montellano, PR | 1 |
| Angeles-Boza, AM; Huff, GS; Mukherjee, A; Roth, JP | 1 |
| Cain, K; Challiss, RA; Chernova, T; Forsythe, ID; Jukes-Jones, R; Mistry, R; Richards, P; Smith, AG; Steinert, JR | 1 |
| Arroyo Mañez, P; Boechi, L; Estrin, DA; Lu, C; Luque, FJ; Martí, MA; Poole, RK; Shepherd, M; Wilson, JL; Yeh, SR | 1 |
| Bennati, M; Brodhun, F; Denysenkov, V; Feussner, I; Fielding, AJ; Koch, C; Pievo, R | 1 |
| Castro, L; Demicheli, V; Kagan, VE; Kapralov, AA; Klein-Seetharaman, J; Maeda, A; Mylnikov, D; Peterson, J; Radi, R; Samhan-Arias, A; Tortora, V; Tyurina, YY; Vladimirov, YA; Weitz, AA; Yanamala, N | 1 |
| Ducsay, CA; Myers, DA | 1 |
| Egawa, T; Gerfen, GJ; Rousseau, DL; Shinzawa-Itoh, K; Yeh, SR; Yoshikawa, S; Yu, MA | 1 |
| Angeles-Boza, AM; Brinkley, DW; Cramer, CJ; Doncheva, IS; Huff, GS; Mukherjee, A; Roth, JP | 1 |
| Grigg, JC; Mao, CX; Murphy, ME | 1 |
| Colabroy, KL; Connor, KL; Gerratana, B | 1 |
| De la Rosa, MA; Díaz-Moreno, I; Díaz-Quintana, A; García-Heredia, JM; Teixeira, M | 1 |
| Donald, LJ; Jha, V; Loewen, PC | 1 |
| Cerdán, ME; Flötenmeyer, M; Meyer, F; Moussian, B; Shaik, KS; Vázquez, AV | 1 |
| Berry, RE; Cusanovich, MA; Fitch, JC; Kyndt, JA; Meyer, TE; Stewart, MC; Walker, FA; Whitley, K | 1 |
| Hu, C; Liu, X; Lu, Y; Wang, J; Yu, Y; Zhang, W | 1 |
| De La Rosa, MÁ; Díaz-Moreno, I; García-Heredia, JM; Hildebrandt, P; Ly, HK; Utesch, T | 1 |
| Alayash, AI; Buehler, PW; Bulow, L; Cooper, CE; Reeder, BJ; Schaer, DJ; Silkstone, G; Svistunenko, DA; Wilson, MT | 1 |
| López-Garriga, J; Ramos-Santana, BJ | 1 |
| Davidson, VL; Hedman, B; Jensen, LM; Meharenna, YT; Poulos, TL; Sarangi, R; Wilmot, CM | 1 |
| Abu Tarboush, N; Davidson, VL; Geng, J; Liu, A; Shin, S | 1 |
| Alcaraz, LA; Donaire, A; Gómez-Mingot, M; Heptinstall, J; Iniesta, J; Montiel, V; Piccioli, M | 1 |
| Hase, T; Hori, H; Nakanishi, N; Park, SY; Rahman, MM; Sakamoto, Y; Tsubaki, M | 1 |
| Awasabisah, D; Powell, DR; Richter-Addo, GB; Sharmah Gautam, KP; Shaw, MJ; Xu, N | 1 |
| Boffi, A; Bonamore, A; Bustamante, JP; Droghetti, E; Estrin, DA; Feis, A; Howes, BD; Nicoletti, FP; Sciamanna, N; Smulevich, G | 1 |
| Davidson, VL; Dornevil, K; Geng, J; Liu, A | 1 |
| Chiu, J; Hogg, PJ; Ng, JY; Wong, JW | 1 |
| Gao, Z; Huang, Y; Li, H; Shuai, Y | 1 |
| Goodwin, DC; Ndontsa, EN; Njuma, OJ | 1 |
| Chaloupkova, R; Damborsky, J; Janata, J; Kamenik, Z; Kutejova, E; Mareckova, M; Mojzes, P; Novak, P; Novotna, J; Olsovska, J; Spizek, J; Tichy, P | 1 |
| Didik, J; Domazou, AS; Gebicka, L; Gebicki, JL; Koppenol, WH; van der Meijden, B | 1 |
| Chibbar, R; Lane, N; Ndisang, JF | 1 |
| Donald, LJ; Hosseinzadeh, P; Ivancich, A; Karaduman, N; Loewen, PC; Lu, Y; Miner, KD; Pfister, TD | 1 |
| Li, J; Lu, N; Peng, YY; Tian, R | 2 |
| Auer, M; Furtmüller, PG; Nicolussi, A; Obinger, C; Schütz, G | 1 |
| Du, KJ; Lin, YW; Nie, CM; Shu, XG; Wen, GB | 1 |
| Sharma, V; Wikström, M | 2 |
| Gao, Z; Li, H; Wang, P; Zhao, J | 1 |
| Li, W; Lin, YW; Tan, X; Wen, GB; Xiang, Y; Yan, DJ | 1 |
| Abián, J; Bartesaghi, S; Becana, M; Calvo-Begueria, L; Pérez-Rontomé, C; Radi, R; Sainz, M; Staudinger, C; Wienkoop, S | 1 |
| Andrews, NW; Flannery, AR; Hamza, I; Miguel, DC; Renberg, RL; Samuel, TK; Yuan, X | 1 |
| Jarzęcki, AA; Kruft, BI; Magliozzo, RS | 1 |
| He, B; Li, W; Lin, YW; Nie, CM; Tan, X; Wen, GB; Xiang, Y; Yan, DJ; Yuan, H | 1 |
| Adrian, SA; Akbas, N; Allen, CE; Collins, DP; Dawson, JH; Dixon, DW; Draganova, EB; Lukat-Rodgers, GS; Rodgers, KR; Schmitt, MP | 1 |
| Costello, CE; Guo, Y; Hendrich, MP; Her, AS; Liu, P; Naowarojna, N; Pu, Y; Song, F; Song, H; Wang, S; Weitz, A; Wu, CH; Yan, W; Zhang, L; Zhang, YJ | 1 |
| Fan, CZ; Li, YT; Pan, ZF; Tang, WY; Wang, W | 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 |
| Huang, Q; Ke, Z | 2 |
| Du, KJ; Gao, SQ; Liao, F; Lin, YW; Tan, X; Wen, GB; You, Y; Yuan, H | 1 |
| Alvarez, LA; Bourke, B; Cean, A; Daff, S; Friedmacher, F; Ghişe, A; Gosemann, JH; Knaus, UG; Kovačič, L; Kubica, M; Pircalabioru, GG; Plettner, E; Puri, P; Rodríguez, J; Sărăndan, MB; von Kriegsheim, A | 1 |
| Chen, L; Feng, C; Li, W; Miao, Y; Zheng, H | 1 |
| Gao, SQ; He, B; Hu, S; Lin, YW; Wang, XJ; Wen, GB | 1 |
| Nakamura, H; Nakamura, K; Sato, S | 1 |
| Battista, T; Cervelli, M; Ciaccio, C; Coletta, M; Fiorucci, L; Howes, BD; Mariottini, P; Santucci, R; Smulevich, G; Tognaccini, L | 1 |
| Dobbek, H; Hildebrandt, P; Jeoung, JH; Kielb, P; Kozuch, J; Mroginski, MA; Utesch, T; Weidinger, I | 1 |
| Gao, W; Gao, Z; Li, H; Zhao, J | 1 |
| Ishimori, K; Kobayashi, N; Muneta, S; Uchida, T | 1 |
| Nagatoishi, S; Nakamura, N; Naoe, Y; Rahman, MM; Shiro, Y; Sugimoto, H; Tosha, T; Tsumoto, K | 1 |
| Nakamura, H; Nakamura, K; Sato, S; Tsushima, M | 1 |
| Alvarez, B; Bartesaghi, S; Campolo, N; Carballal, S; Ferrer-Sueta, G; Radi, R; Romero, N; Trujillo, M | 1 |
| Fita, I; Rovira, C; Wang, B | 1 |
| Gray, HB; Winkler, JR | 1 |
| English, AM; Kathiresan, M | 1 |
| Bülow, L; Cooper, CE; Eke, A; Eriksson, NL; Gretton, S; Mathe, D; Mozzarelli, A; Rajagopal, B; Reeder, BJ; Ronda, L; Shaik, T; Silkstone, GGA; Simons, M; Syrett, N; Welbourn, E | 1 |
| Gao, Z; Li, H; Ouyang, L; Wu, J; Yang, Z; Zhao, J; Zhu, L | 1 |
| Du, KJ; Gao, SQ; Liao, F; Lin, YW; Liu, C; Tan, X; Wei, CW; Yuan, H | 1 |
| Jose, A; Roveda, AC; Schaefer, AW; Solomon, EI | 1 |
| López-Garriga, J; Marchany-Rivera, D; Rodriguez-Perez, JD; Smith, CA | 1 |
| Deniz, E; Heit, S; Klein, M; Lancaster, CRD; Mäntele, W; Wille, G | 1 |
| Imhof, D; Krämer, OH; Mustafa, AM; Schmalohr, BF | 1 |
| Cerda, JF; Cruz-Balberdy, A; Flanders, KG; Frankenfield, K; Lopez-Garriga, J; Marchany-Rivera, D | 1 |
| Britt, RD; Chakarawet, K; Dwaraknath, S; Ledray, AP; Lu, Y; Merchen, C; Rao, G; Sponholtz, MR; Van Stappen, C | 1 |
| Gray, HB; Ravanfar, R; Sheng, Y; Winkler, JR | 1 |
| Jordan, S; Li, B; Liu, A; Traore, E; Usai, R; Wang, Y; Wu, Y; Xie, ZR | 1 |
| André, E; Bernad, S; Derrien, V | 1 |
| Aller, P; Alonso Mori, R; Batyuk, A; Bhowmick, A; Bogacz, I; Brewster, AS; Butryn, A; Chatterjee, R; Dasgupta, M; Davis, I; Dornevil, K; Fuller, F; Kern, JF; Kim, IS; Liu, A; Makita, H; Mendez, D; Nguyen, RC; Orville, AM; Paley, DW; Sauter, NK; Simon, PS; Wang, Y; Yachandra, VK; Yano, J; Zhou, T | 1 |
11 review(s) available for tyrosine and heme
| Article | Year |
|---|---|
Tyrosyl radicals and their role in hydroperoxide-dependent activation and inactivation of prostaglandin endoperoxide synthase.
Topics: Animals; Cyclooxygenase Inhibitors; Enzyme Activation; Free Radicals; Heme; Humans; Hydrogen Peroxide; Prostaglandin-Endoperoxide Synthases; Tyrosine | 1992 |
Structure and function of hemoglobin.
Topics: Amino Acid Sequence; Heme; Hemoglobins; Models, Chemical; Tryptophan; Tyrosine | 1969 |
Chemistry and biology of heme. Effect of metal salts, organometals, and metalloporphyrins on heme synthesis and catabolism, with special reference to clinical implications and interactions with cytochrome P-450.
Topics: Amino Acid Metabolism, Inborn Errors; Animals; Catalysis; Cytochrome P-450 Enzyme System; Drug Interactions; Heme; Humans; Hyperbilirubinemia; Infant, Newborn; Lead Poisoning; Leukemia, Erythroblastic, Acute; Metalloporphyrins; Metals; Organometallic Compounds; Tyrosine | 1993 |
Peroxynitrite inactivates prostacyclin synthase by heme-thiolate-catalyzed tyrosine nitration.
Topics: Animals; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Epoprostenol; Heme; Humans; Intramolecular Oxidoreductases; Nitrates; Nitric Oxide; Sulfhydryl Compounds; Superoxides; Tyrosine; Vascular Resistance | 1999 |
UV optical absorption by protein radicals in cytochrome c oxidase.
Topics: Animals; Carbon Monoxide; Cattle; Copper; Electron Transport Complex IV; Free Radicals; Heme; Hydrogen-Ion Concentration; In Vitro Techniques; Myocardium; Oxygen; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine | 2004 |
Oxidative alterations of cyclooxygenase during atherogenesis.
Topics: Animals; Arachidonic Acid; Atherosclerosis; Cyclooxygenase Inhibitors; Cysteine; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Enzyme Activation; Heme; Humans; Intramolecular Oxidoreductases; MAP Kinase Signaling System; Nitric Oxide; Nitrogen Oxides; Oxidation-Reduction; Peroxynitrous Acid; Prostaglandin-Endoperoxide Synthases; Tyrosine | 2006 |
eNOS activation and NO function: differential control of steroidogenesis by nitric oxide and its adaptation with hypoxia.
Topics: Adrenal Glands; Animals; Cyclic GMP; Cysteine; Enzyme Activation; Female; Guanylate Cyclase; Heme; Humans; Hypoxia; Male; Models, Biological; Nitric Oxide; Nitric Oxide Synthase Type III; Ovary; Pregnancy; Protein Processing, Post-Translational; Steroids; Testis; Tyrosine | 2011 |
Catalase in peroxidase clothing: Interdependent cooperation of two cofactors in the catalytic versatility of KatG.
Topics: Antitubercular Agents; Archaea; Bacteria; Bacterial Proteins; Catalase; Coenzymes; Heme; Isoniazid; Methionine; Models, Molecular; Mycobacterium tuberculosis; Peroxidase; Prodrugs; Tryptophan; Tyrosine | 2014 |
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 |
[Development and Application of Catalytic Tyrosine Modification].
Topics: Catalysis; Heme; Hemeproteins; Luminescence; Luminol; Peroxidase; Tyrosine | 2018 |
Biochemistry of Peroxynitrite and Protein Tyrosine Nitration.
Topics: Carbon Dioxide; Coenzymes; Electron Transport Complex IV; Heme; Iron-Sulfur Proteins; Kinetics; Peroxidases; Peroxynitrous Acid; Proteins; Tyrosine | 2018 |
1 trial(s) available for tyrosine and heme
| Article | Year |
|---|---|
Hematin therapy for the neurologic crisis of tyrosinemia.
Topics: Amino Acid Metabolism, Inborn Errors; Amino Acids; Aminolevulinic Acid; Heme; Hemin; Heptanoates; Humans; Infant; Liver Transplantation; Male; Tyrosine | 1991 |
266 other study(ies) available for tyrosine and heme
| Article | Year |
|---|---|
The aromatic and heme chromophores of rabbit hemopexin. Difference absorption and fluorescence spectra.
Topics: Animals; Apoproteins; Binding Sites; Heme; Hemopexin; Hydrogen Bonding; Hydrogen-Ion Concentration; Protein Binding; Protein Conformation; Rabbits; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tyrosine | 1976 |
Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group.
Topics: Cytochrome c Group; Energy Transfer; Fluorescence; Guanidines; Heme; Hydrogen-Ion Concentration; Kinetics; Protein Conformation; Temperature; Tryptophan; Tyrosine; Urea | 1976 |
On the molecular conformation of human haemopexin. I. Reactivity of the tyrosine and tryptophan side chains.
Topics: Circular Dichroism; Heme; Hemopexin; Humans; Hydrogen-Ion Concentration; Kinetics; Protein Conformation; Spectrophotometry; Tryptophan; Tyrosine | 1977 |
1H NMR studies at 360 MHz of the aromatic amino acid residues in ferrocytochrome c-552 from Euglena gracilis.
Topics: Animals; Binding Sites; Cytochrome c Group; Euglena gracilis; Heme; Iron; Magnetic Resonance Spectroscopy; Protein Binding; Protein Conformation; Tryptophan; Tyrosine | 1977 |
Modification of cytochrome c: modification of aromatic amino acids, photoaffinity labels, and metal substitution.
Topics: Affinity Labels; Amino Acids; Animals; Cations, Divalent; Chemical Phenomena; Chemistry; Cytochrome c Group; Formates; Heme; Horses; Myocardium; Photochemistry; Porphyrins; Tryptophan; Tyrosine | 1978 |
Prostaglandin H synthase. Kinetics of tyrosyl radical formation and of cyclooxygenase catalysis.
Topics: Animals; Arachidonic Acid; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Kinetics; Lipid Peroxides; Male; Microsomes; Prostaglandin-Endoperoxide Synthases; Seminal Vesicles; Sheep; Time Factors; Tyrosine | 1992 |
The role of tyrosine 67 in the cytochrome c heme crevice structure studied by semisynthesis.
Topics: Animals; Cytochrome c Group; Electrochemistry; Electron Transport Complex IV; Heme; Horses; Isomerism; Ligands; Oxidation-Reduction; Peptide Mapping; Peptides; Protein Binding; Protein Conformation; Spectrophotometry, Ultraviolet; Titrimetry; Tyrosine | 1992 |
NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted.
Topics: Amino Acids; Cytochrome c Group; Cytochromes c; Heme; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Tryptophan; Tyrosine | 1991 |
Renal heme metabolism in hereditary tyrosinemia: use of succinylacetone in rat renal tubules.
Topics: Amino Acid Metabolism, Inborn Errors; Animals; Cytochrome P-450 Enzyme System; Cytosol; Ferrochelatase; Heme; Heme Oxygenase (Decyclizing); Heptanoates; Kidney Cortex; Kidney Tubules; Male; Models, Biological; Porphyrins; Rats; Rats, Inbred Strains; Tyrosine | 1991 |
Hereditary tyrosinemia of chronic course without rickets and renal tubular dysfunction.
Topics: Adolescent; Amino Acid Metabolism, Inborn Errors; Amino Acids; Child; Child, Preschool; Chronic Kidney Disease-Mineral and Bone Disorder; Female; Heme; Heptanoates; Humans; Hydrolases; Male; Porphobilinogen Synthase; Thrombocytopenia; Tyrosine | 1990 |
On rat renal aminolevulinate transport and metabolism in experimental Fanconi syndrome.
Topics: Amino Acid Metabolism, Inborn Errors; Aminolevulinic Acid; Animals; Biological Transport, Active; Fanconi Syndrome; Heme; Heptanoates; In Vitro Techniques; Kidney Tubules; Male; Maleates; Microvilli; Porphobilinogen Synthase; Rats; Rats, Inbred Strains; Tyrosine | 1990 |
Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation.
Topics: Camphor; Camphor 5-Monooxygenase; Cations, Monovalent; Chemical Phenomena; Chemistry, Physical; Cytochrome P-450 Enzyme System; Heme; Hydrogen Bonding; Mixed Function Oxygenases; Mutation; Thermodynamics; Tyrosine | 1990 |
Dietary treatment eliminates succinylacetone from the urine of a patient with tyrosinaemia type 1.
Topics: Amino Acid Metabolism, Inborn Errors; Female; Heme; Heptanoates; Heptanoic Acids; Humans; Infant; Methionine; Phenylalanine; Tyrosine | 1990 |
Structural significance of an internal water molecule studied by site-directed mutagenesis of tyrosine-67 in rat cytochrome c.
Topics: Animals; Cytochrome c Group; DNA Mutational Analysis; Heme; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Models, Molecular; Phenylalanine; Protein Conformation; Rats; Recombinant Proteins; Structure-Activity Relationship; Thermodynamics; Tyrosine; Urea; Water | 1989 |
Structural and electronic properties of the liver fluke heme cavity by nuclear magnetic resonance and optical spectroscopy. Evidence for a distal tyrosine residue in a normally functioning hemoglobin.
Topics: Amino Acids; Animals; Dicrocoelium; Heme; Hemoglobins; Magnetic Resonance Spectroscopy; Methemoglobin; Propionates; Protons; Tyrosine | 1989 |
Assignment of resonances in the 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques.
Topics: Amino Acid Sequence; Animals; Heme; Macromolecular Substances; Magnetic Resonance Spectroscopy; Myoglobin; Tryptophan; Tyrosine; Whales | 1987 |
Tyrosine motions in relation to the ferric spin equilibrium of cytochrome P-450cam.
Topics: Cytochrome P-450 Enzyme System; Heme; Kinetics; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Pseudomonas; Spectrophotometry; Tyrosine | 1985 |
Studies on the mechanism of iodination supported by thyroidal NADPH-cytochrome c reductase.
Topics: Animals; Carbon Radioisotopes; Cattle; Coloring Agents; Cytochrome c Group; Depression, Chemical; Ferricyanides; Formates; Guaiacol; Heme; In Vitro Techniques; Iodides; Iodine Radioisotopes; Isoproterenol; NADH, NADPH Oxidoreductases; NADP; Potassium; Pyrogallol; Temperature; Thyroid Gland; Trypsin; Tyrosine; Vitamin K | 1973 |
Redox state and chain folding in cytochrome c.
Topics: Amino Acid Sequence; Amino Acids; Animals; Binding Sites; Biological Evolution; Cytochrome c Group; Fishes; Heme; Horses; Iron; Models, Structural; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Porphyrins; Protein Binding; Protein Conformation; Species Specificity; Tryptophan; Tyrosine | 1974 |
Electron transfer within and between haemoprotein molecules.
Topics: Amino Acid Oxidoreductases; Amino Acids; Blood Proteins; Cytochromes; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; In Vitro Techniques; Iron; Myoglobin; Oxidation-Reduction; Tryptophan; Tyrosine | 1965 |
Properties of hemoglobin M, Milwaukee-I variant and its unique characteristic.
Topics: Amino Acid Sequence; Amino Acids; Australia; Blood; Boston; Chemical Phenomena; Chemistry; Cyanides; Drug Stability; Electron Spin Resonance Spectroscopy; Glutamates; Heme; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Iron; Oxidation-Reduction; Oxygen; Peptides; Protein Denaturation; Saskatchewan; Spectrophotometry; Temperature; Tyrosine; Wisconsin | 1969 |
Hemoglobin M Saskatoon: further data on biophysics and oxygen equilibrium.
Topics: Amino Acids; Biophysical Phenomena; Biophysics; Chromatography, Gel; Chromatography, Ion Exchange; Electron Spin Resonance Spectroscopy; Electrophoresis; Erythrocytes; Ferricyanides; Glycerophosphates; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Hydrolysis; Macromolecular Substances; Oxidation-Reduction; Oxygen; Peptides; Protein Binding; Saskatchewan; Spectrophotometry; Trypsin; Tyrosine | 1971 |
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 |
Proteins of the thermophilic fungus Humicola lanuginosa. II. Some physicochemical properties of a cytochrome c.
Topics: Animals; Circular Dichroism; Cytochrome c Group; Fungal Proteins; Heme; Horses; Hydrogen-Ion Concentration; Mitosporic Fungi; Myocardium; Optical Rotatory Dispersion; Peptides; Solvents; Spectrophotometry, Ultraviolet; Tyrosine; Urea | 1973 |
[Thyroid particulate peroxidase].
Topics: Acrylamides; Animals; Cattle; Chromatography, DEAE-Cellulose; Chromatography, Gel; Electrophoresis; Heme; Iodine; Molecular Weight; Monoiodotyrosine; Peroxidases; Protein Conformation; Protein Hydrolysates; Swine; Thyroid Gland; Trypsin; Tyrosine; Ultracentrifugation | 1972 |
The reversible titration of tyrosyl residues in human deoxyhemoglobin.
Topics: Acetylation; Amino Acids; Carboxyhemoglobin; Dithionite; Heme; Hemoglobins; Humans; Hydrogen-Ion Concentration; Imidazoles; Protein Binding; Protein Conformation; Spectrophotometry; Thermodynamics; Tyrosine; Ultracentrifugation | 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 |
Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin.
Topics: Arginine; Australia; Chemical Phenomena; Chemistry; Circular Dichroism; Globins; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Inositol; Macromolecular Substances; Magnetic Resonance Spectroscopy; Magnetics; Mutation; Organophosphorus Compounds; Oxygen; Oxyhemoglobins; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet; Succinimides; Tryptophan; Tyrosine; X-Ray Diffraction | 1974 |
Isolation of the thyroid peroxidase complex.
Topics: Animals; Antigens; Chemical Precipitation; Chlorides; Chromatography, Gel; Detergents; Electrophoresis, Disc; Guaiacol; Heme; Immune Sera; Immunodiffusion; Iodine; Kinetics; Methods; Molecular Weight; Peroxidases; Proteins; Rabbits; Spectrophotometry; Sulfuric Acids; Swine; Thyroid Gland; Trypsin; Tyrosine; Ultracentrifugation; Ultraviolet Rays; Zinc | 1971 |
Oxygen equilibrium and circular dichroism of hemoglobin-Rainer ( 2 2 1 45Tyr leads to Cys).
Topics: Amino Acid Sequence; Amino Acids; Chromatography, Ion Exchange; Circular Dichroism; Cysteine; Disulfides; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Oxygen; Peptides; Protein Conformation; Spectrophotometry; Sulfhydryl Compounds; Tyrosine; Ultraviolet Rays | 1972 |
The deoxygenation kinetics of hemoglobin Rainier ( 2 145 tyr change to cys).
Topics: Cysteine; Disulfides; Drug Stability; Glycerophosphates; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Kinetics; Oxygen; Peptides; Protein Binding; Protein Conformation; Tyrosine | 1972 |
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 |
The reactivity of the tyrosyl residues of cytochrome b 5 .
Topics: 1-Propanol; Acetates; Acylation; Anhydrides; Animals; Apoproteins; Cattle; Chemical Phenomena; Chemistry; Chromatography, Ion Exchange; Circular Dichroism; Cytochromes; Heme; Hydrogen-Ion Concentration; Iodine; Mathematics; Peptides; Protein Conformation; Rabbits; Spectrometry, Fluorescence; Spectrophotometry; Trypsin; Tyrosine; Ultraviolet Rays; Urea | 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 |
Near-ultraviolet absorption bands of tryptophan. Studies using horseradish peroxidase isoenzymes, bovine and horse heart cytochrome c, and N-stearyl-L-tryptophan n-hexyl ester.
Topics: Animals; Cattle; Chemical Phenomena; Chemistry; Cold Temperature; Cyclohexanes; Cytochromes; Energy Transfer; Esters; Glycerol; Heme; Horses; Hydrogen-Ion Concentration; Indoles; Isoenzymes; Myocardium; Peroxidases; Phenylalanine; Plants; Spectrophotometry; Stearic Acids; Tryptophan; Tyrosine; 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 |
Electrical conductivity of some organic materials containing metals.
Topics: Cobalt; Copper; Cytochromes; Electric Conductivity; Electron Transport; Heme; Iron; Organometallic Compounds; Proteins; Tryptophan; Tyrosine | 1971 |
Amino acid replacements resulting from super-suppression of nonsense mutants of iso-1-cytochrome c from yeast.
Topics: Amino Acid Sequence; Amino Acids; Chromosomes; Cytochromes; Electrophoresis; Genetic Code; Heme; Mutation; RNA, Transfer; Saccharomyces; Spectrophotometry; Suppression, Genetic; Tyrosine | 1971 |
Chemical and organoleptic changes in poultry meat resulting from the growth of psychrophylic spoilage bacteria at 1 degree C. 3. Glutamine, glutathione, tyrosine, ammonia, lactic acid, creatine, carbohydrate, haem pigment and hydrogen sulphide.
Topics: Ammonia; Animals; Carbohydrates; Chickens; Creatine; Food Microbiology; Food Preservation; Glutamine; Glutathione; Heme; Lactates; Meat; Muscles; Myoglobin; Poultry; Pseudomonas; Sulfides; Tyrosine | 1969 |
Reactivity of individual tyrosyl residues of horse heart ferricytochrome c toward iodination.
Topics: Amino Acids; Animals; Chemical Phenomena; Chemistry; Chromatography, Gel; Chromatography, Ion Exchange; Cyanides; Cytochromes; Diiodotyrosine; Heme; Horses; Hydrogen-Ion Concentration; Iodine; Iron; Myocardium; Peptides; Spectrophotometry; Trypsin; Tyrosine | 1970 |
Structural location of the tyrosyl and tryptophanyl residues of tuna heart cytochrome c.
Topics: Amino Acid Sequence; Animals; Chemical Phenomena; Chemistry; Cytochromes; Diiodotyrosine; Fishes; Heme; Hydrogen-Ion Concentration; Iodine; Iron; Monoiodotyrosine; Myocardium; Oxidation-Reduction; Solvents; Spectrophotometry; Tryptophan; Tyrosine; Ultraviolet Rays | 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 |
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 |
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 |
Peroxidase isoenzymes from horseradish roots. 3. Circular dichroism of isoenzymes and apoisoenzymes.
Topics: Binding Sites; Heme; Isoenzymes; Peroxidases; Phenylalanine; Plants; Spectrophotometry; Spectrum Analysis; Tryptophan; Tyrosine; Ultraviolet Rays | 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 |
Solvent perturbation studies of heme proteins and other colored proteins.
Topics: Animals; Catalase; Cattle; Cetacea; Cytochromes; Deuterium; Glycerol; Glycols; Heme; Hemoglobins; Horses; Hydrogen-Ion Concentration; Liver; Myoglobin; Optical Rotatory Dispersion; Solvents; Spectrum Analysis; Sucrose; Tryptophan; Tyrosine; Ultraviolet Rays; Urea; Water | 1969 |
Optical rotatory dispersion of human hemoglobins A, F, S, C, and M.
Topics: Chemical Phenomena; Chemistry; Fetal Hemoglobin; Genes; Heme; Hemoglobin C; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Methemoglobin; Optical Rotatory Dispersion; Oxidation-Reduction; Spectrophotometry; Temperature; Tryptophan; Tyrosine | 1969 |
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 |
Fluorometric and spectrophotometric study of heme binding on the apoprotein from a cytochrome b-2-derivative.
Topics: Coenzymes; Cytochromes; Flavins; Fluorometry; Heme; L-Lactate Dehydrogenase; Protein Binding; Spectrophotometry; Trypsin; Tryptophan; Tyrosine; Urea | 1967 |
The structural environment of the tryptophanyl residue of horse heart ferricytochrome c.
Topics: Amino Acids; Animals; Cytochromes; Heme; Horses; Hydrogen-Ion Concentration; Methionine; Myocardium; Oxidation-Reduction; Spectrophotometry; Tryptophan; Tyrosine; Viscosity | 1967 |
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 |
Biochemical studies of a patient with hereditary hepatorenal tyrosinemia: evidence of glutathione deficiency.
Topics: Erythrocytes; Fanconi Syndrome; Female; Glutathione; Heme; Humans; Infant; Liver; Liver Diseases; Mass Spectrometry; Mixed Function Oxygenases; Phosphates; Pyrroles; Rickets; Syndrome; Tyrosine | 1984 |
Chemical modification of cytochrome P-450 LM2. Characterization of tyrosine as axial heme iron ligand trans to thiolate.
Topics: Acetylation; Animals; Binding Sites; Cytochrome P-450 Enzyme System; Heme; Imidazoles; Kinetics; Ligands; Male; Microsomes, Liver; Phenobarbital; Protein Binding; Rabbits; Tyrosine | 1984 |
Hereditary tyrosinemia and the heme biosynthetic pathway. Profound inhibition of delta-aminolevulinic acid dehydratase activity by succinylacetone.
Topics: Amino Acid Metabolism, Inborn Errors; Animals; Cattle; Chick Embryo; Erythrocytes; Heme; Heptanoates; Heptanoic Acids; Humans; In Vitro Techniques; Liver; Mice; Mice, Inbred BALB C; Porphobilinogen Synthase; Species Specificity; Tyrosine | 1983 |
Secondary and tertiary structure of the A-state of cytochrome c from resonance Raman spectroscopy.
Topics: Animals; Crystallography, X-Ray; Cytochrome c Group; Heme; Horses; Hydrogen Bonding; Iron; Models, Molecular; Molecular Structure; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrum Analysis, Raman; Thermodynamics; Tryptophan; Tyrosine | 1995 |
Horseradish peroxidase Phe172-->Tyr mutant. Sequential formation of compound I with a porphyrin radical cation and a protein radical.
Topics: Animals; Baculoviridae; Base Sequence; Binding Sites; Cations; Cells, Cultured; Electron Spin Resonance Spectroscopy; Free Radicals; Guaiacol; Heme; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Spectrophotometry; Spodoptera; Sulfides; Tyrosine | 1995 |
An examination of the source of the tyrosyl radical in ovine prostaglandin endoperoxide synthase-1.
Topics: Amino Acid Sequence; Animals; Antibodies; Base Sequence; Binding Sites; Blotting, Western; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Peptides; Point Mutation; Prostaglandin-Endoperoxide Synthases; Recombinant Proteins; Sheep; Tyrosine | 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 |
The interaction of short chain coenzyme Q analogs with different redox states of myoglobin.
Topics: Acetylation; Aerobiosis; Animals; Heme; Horses; In Vitro Techniques; Myoglobin; Oxidation-Reduction; Oxygen Consumption; Spectrometry, Fluorescence; Tyrosine; Ubiquinone | 1994 |
The role of tryptophan 97 of cytochrome P450 BM3 from Bacillus megaterium in catalytic function. Evidence against the 'covalent switching' hypothesis of P-450 electron transfer.
Topics: Alanine; Bacillus megaterium; Bacterial Proteins; Base Sequence; Catalysis; Circular Dichroism; Cytochrome P-450 Enzyme System; DNA Primers; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli; Heme; Mixed Function Oxygenases; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; NADPH-Ferrihemoprotein Reductase; Phenylalanine; Protein Structure, Secondary; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine | 1994 |
Effects of the Tyr64 substitution on the stability of cytochrome c553, a low oxidoreduction-potential cytochrome from Desulfovibrio vulgaris Hildenborough.
Topics: Base Sequence; Cytochrome c Group; Desulfovibrio vulgaris; Drug Stability; Electrochemistry; Heme; Hydrogen Bonding; Hydrogen-Ion Concentration; Mass Spectrometry; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Spectrophotometry; Structure-Activity Relationship; Tyrosine | 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 |
Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment.
Topics: Cytochrome c Group; Electron Transport; Escherichia coli; Heme; Hydrogen Bonding; Mutagenesis, Site-Directed; Oxidation-Reduction; Peptides; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Tyrosine | 1994 |
The function of tyrosine 74 of cytochrome b5.
Topics: Animals; Cytochromes b5; Heme; Hot Temperature; In Vitro Techniques; Lysine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Conformation; Rats; Recombinant Proteins; Structure-Activity Relationship; Thermodynamics; Tyrosine; Urea | 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 |
Tissue distribution of succinylacetone in the rat in vivo: a possible basis for neurotoxicity in hereditary infantile tyrosinemia.
Topics: Animals; Animals, Newborn; Brain; Heme; Heptanoates; Kidney; Liver; Male; Nervous System Diseases; Porphobilinogen Synthase; Porphyrins; Rats; Rats, Sprague-Dawley; Tissue Distribution; Tyrosine | 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 |
Hydrogen bonding of tyrosine B10 to heme-bound oxygen in Ascaris hemoglobin. Direct evidence from UV resonance Raman spectroscopy.
Topics: Animals; Ascaris; Heme; Hemoglobins; Hydrogen Bonding; Oxygen; Spectrum Analysis, Raman; Tyrosine | 1996 |
Probing the active site residues in aromatic donor oxidation in horseradish peroxidase: involvement of an arginine and a tyrosine residue in aromatic donor binding.
Topics: Arginine; Binding Sites; Carbon Radioisotopes; Circular Dichroism; Cyclohexanones; Diacetyl; Enzyme Inhibitors; Heme; Horseradish Peroxidase; Kinetics; Models, Structural; Phenylglyoxal; Protein Structure, Secondary; Spectrophotometry; Tetranitromethane; Thermodynamics; Tyrosine | 1996 |
Spectroscopic studies of the C-terminal secretion signal of the Serratia marcescens haem acquisition protein (HasA) in various membrane-mimetic environments.
Topics: Amino Acid Sequence; ATP-Binding Cassette Transporters; Bacterial Proteins; Carrier Proteins; Circular Dichroism; Erwinia; Heme; Membrane Proteins; Membranes, Artificial; Metalloendopeptidases; Molecular Sequence Data; Protein Sorting Signals; Protein Structure, Secondary; Recombinant Fusion Proteins; Sequence Alignment; Serratia marcescens; Spectrometry, Fluorescence; Tyrosine | 1997 |
Mutagenesis of nitrite reductase from Pseudomonas aeruginosa: tyrosine-10 in the c heme domain is not involved in catalysis.
Topics: Amino Acid Sequence; Catalysis; Heme; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitrite Reductases; Pseudomonas aeruginosa; Pseudomonas putida; Sequence Homology, Amino Acid; Tyrosine | 1997 |
Mutagenesis of residues 27 and 78 modulates heme orientation in cytochrome b5.
Topics: Amino Acid Sequence; Animals; Cattle; Crystallography, X-Ray; Cytochromes b5; Heme; Magnetic Resonance Spectroscopy; Microsomes; Molecular Sequence Data; Mutagenesis, Site-Directed; Nicotiana; Phenylalanine; Plants, Toxic; Rats; Tyrosine | 1997 |
A comparison of functional and structural consequences of the tyrosine B10 and glutamine E7 motifs in two invertebrate hemoglobins (Ascaris suum and Lucina pectinata).
Topics: Amino Acid Substitution; Animals; Ascaris suum; Binding Sites; Bivalvia; Carbon Monoxide; Carboxyhemoglobin; Glutamic Acid; Heme; Hemoglobins; Kinetics; Oxyhemoglobins; Protein Conformation; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Thermodynamics; Tyrosine | 1997 |
Sea urchin ovoperoxidase: oocyte-specific member of a heme-dependent peroxidase superfamily that functions in the block to polyspermy.
Topics: Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; DNA Primers; DNA, Complementary; Female; Fertilization; Heme; Male; Molecular Sequence Data; Oocytes; Peroxidases; Protein Processing, Post-Translational; Sea Urchins; Sequence Homology, Amino Acid; Substrate Specificity; Tyrosine | 1998 |
Low-temperature electron transfer from cytochrome to the special pair in Rhodopseudomonas viridis: role of the L162 residue.
Topics: Amino Acid Sequence; Binding Sites; Cold Temperature; Cytochrome c Group; Electron Transport; Freezing; Heme; Kinetics; Models, Molecular; Oxidation-Reduction; Point Mutation; Protein Conformation; Recombinant Proteins; Rhodopseudomonas; Spectrophotometry; Thermodynamics; Tyrosine | 1998 |
Tyrosine 64 of cytochrome c553 is required for electron exchange with formate dehydrogenase in Desulfovibrio vulgaris Hildenborough.
Topics: Amino Acid Substitution; Arginine; Cytochrome c Group; Desulfovibrio vulgaris; Electron Transport; Formate Dehydrogenases; Heme; Hydrogen Bonding; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Static Electricity; Tyrosine | 1998 |
Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase.
Topics: Animals; Aspartic Acid; Azides; Binding Sites; Carbon Monoxide; Cattle; Copper; Crystallography, X-Ray; Electron Transport Complex IV; Heme; Hydrogen Bonding; Hydrogen Peroxide; Hydrogen-Ion Concentration; Ligands; Metals; Models, Chemical; Models, Molecular; Myocardium; Oxidation-Reduction; Oxygen; Protein Conformation; Proton Pumps; Tyrosine | 1998 |
Solution structure of thermostable cytochrome c-552 from Hydrogenobacter thermophilus determined by 1H-NMR spectroscopy.
Topics: Amino Acid Sequence; Arginine; Bacteria, Aerobic; Bacterial Proteins; Crystallography, X-Ray; Cytochrome c Group; Heme; Hydrogen Bonding; Lysine; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Peptides; Protein Conformation; Protein Folding; Protons; Pseudomonas aeruginosa; Sequence Homology, Amino Acid; Solutions; Thermodynamics; Tyrosine | 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 |
The post-translational modification in cytochrome c oxidase is required to establish a functional environment of the catalytic site.
Topics: Binding Sites; Catalysis; Electron Transport Complex IV; Heme; Ligands; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Protein Processing, Post-Translational; Rhodobacter sphaeroides; Spectrum Analysis, Raman; Tyrosine | 1998 |
Electrochemical and ultraviolet/visible/infrared spectroscopic analysis of heme a and a3 redox reactions in the cytochrome c oxidase from Paracoccus denitrificans: separation of heme a and a3 contributions and assignment of vibrational modes.
Topics: Arginine; Aspartic Acid; Electrochemistry; Electron Transport Complex IV; Glutamic Acid; Heme; Molecular Conformation; Oxidation-Reduction; Paracoccus denitrificans; Porphyrins; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Tyrosine | 1999 |
Peroxynitrite induces long-lived tyrosyl radical(s) in oxyhemoglobin of red blood cells through a reaction involving CO2 and a ferryl species.
Topics: Carbon Dioxide; Electron Spin Resonance Spectroscopy; Erythrocytes; Ferric Compounds; Free Radicals; Heme; Hemoglobins; Humans; Hydrogen Peroxide; Iron; Methemoglobin; Metmyoglobin; Nitrates; Oxidants; Oxygen; Oxyhemoglobins; Tyrosine | 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 |
Rapid kinetics of tyrosyl radical formation and heme redox state changes in prostaglandin H synthase-1 and -2.
Topics: Animals; Apoenzymes; Cyclooxygenase 1; Cyclooxygenase 2; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Humans; Isoenzymes; Kinetics; Male; Membrane Proteins; Oxidation-Reduction; Prostaglandin-Endoperoxide Synthases; Protein Conformation; Recombinant Proteins; Seminal Vesicles; Sheep; Tyrosine | 1999 |
Electrochemical, FTIR, and UV/VIS spectroscopic properties of the ba(3) oxidase from Thermus thermophilus.
Topics: Arginine; Aspartic Acid; Buffers; Cytochrome b Group; Deuterium Oxide; Electrochemistry; Electron Transport Complex IV; Glutamic Acid; Heme; Lysine; Oxidation-Reduction; Peptides; Phosphates; Porphyrins; Potentiometry; Propionates; Protein Conformation; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Thermus thermophilus; Tyrosine; Water | 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 |
Nitration of internal tyrosine of cytochrome c probed by resonance Raman scattering.
Topics: Animals; Cytochrome c Group; Heme; Horses; Hydrogen-Ion Concentration; Spectrum Analysis, Raman; Tyrosine | 1999 |
Requirements for heme and thiols for the nonenzymatic modification of nitrotyrosine.
Topics: Chromatography, High Pressure Liquid; Electrochemistry; Heme; Sulfhydryl Compounds; Tyrosine | 1999 |
Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: evidence for ligation of tyrosine-63 (B10) to the heme.
Topics: Amino Acid Substitution; Animals; Chlamydomonas; Chloroplasts; Electron Spin Resonance Spectroscopy; Ferric Compounds; Heme; Hemoglobins; Hydrogen-Ion Concentration; Ligands; Mutagenesis, Site-Directed; Spectrum Analysis, Raman; Tyrosine | 1999 |
A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis. Stabilization of heme ligands by a distal tyrosine residue.
Topics: Carbon Monoxide; Heme; Hemoglobins; Hydrogen; Hydroxides; Ligands; Models, Chemical; Mycobacterium tuberculosis; Oxygen; Recombinant Proteins; Spectrum Analysis, Raman; Tyrosine | 2000 |
A possible origin of differences between calorimetric and equilibrium estimates of stability parameters of proteins.
Topics: Biochemistry; Calorimetry; Cytochrome c Group; Heme; Hot Temperature; Hydrogen-Ion Concentration; Models, Chemical; Muramidase; Myoglobin; Protein Conformation; Protein Denaturation; Proteins; Ribonuclease, Pancreatic; Thermodynamics; Tryptophan; Tyrosine | 2000 |
Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism.
Topics: Amino Acid Sequence; Amitrole; Binding Sites; Catalase; Catalysis; Crystallization; Crystallography, X-Ray; Cyanides; Electrons; Enzyme Inhibitors; Heme; Humans; Hydrogen Bonding; Hydrogen Peroxide; Models, Chemical; Models, Molecular; Molecular Sequence Data; NADP; Protein Conformation; Substrate Specificity; Tyrosine; Water | 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 |
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 |
Molecular basis for hyperactivity in tryptophan 409 mutants of neuronal NO synthase.
Topics: Amino Acid Substitution; Animals; Catalysis; Heme; Kinetics; Models, Chemical; Mutagenesis, Site-Directed; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Rats; Recombinant Proteins; Spectrophotometry; Tryptophan; Tyrosine | 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 |
Tryptophan-heme pi-electrostatic interactions in cytochrome f of oxygenic photosynthesis.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Chlamydomonas reinhardtii; Chloroplasts; Cyanobacteria; Cytochromes; Cytochromes f; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Photosynthesis; Static Electricity; Tryptophan; Tyrosine | 2000 |
The caa(3) terminal oxidase of Rhodothermus marinus lacking the key glutamate of the D-channel is a proton pump.
Topics: Amino Acid Sequence; Copper; Cytochrome c Group; Electron Transport Complex IV; Glutamic Acid; Gram-Negative Aerobic Bacteria; Heme; Liposomes; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Protein Conformation; Proteolipids; Proton Pumps; Sequence Alignment; Sequence Homology, Amino Acid; Tyrosine | 2000 |
Resonance raman studies of oxo intermediates in the reaction of pulsed cytochrome bo with hydrogen peroxide.
Topics: Bacterial Proteins; Carbon Monoxide; Cytochrome b Group; Cytochromes; Deuterium Oxide; Escherichia coli; Escherichia coli Proteins; Free Radicals; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Iron; Oxygen Isotopes; Spectrum Analysis, Raman; Tyrosine | 2000 |
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 |
Autocatalytic nitration of P450CAM by peroxynitrite.
Topics: Binding Sites; Blotting, Western; Camphor 5-Monooxygenase; Carbon Monoxide; Catalysis; Cytochrome P-450 Enzyme System; Heme; Hydroxylation; Intramolecular Oxidoreductases; Kinetics; Ligands; Mass Spectrometry; Models, Molecular; Nitrates; Nitrogen; Phenol; Protein Binding; Protein Conformation; Protons; Spectrophotometry; Time Factors; Tyrosine | 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 |
Solution 1H NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase. comparison to the crystal structure of the water-ligated form.
Topics: Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Cyanides; Heme; Heme Oxygenase (Decyclizing); Humans; Hydrogen; Hydrogen Bonding; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; Tyrosine; Water | 2001 |
pH-dependent structural changes at the Heme-Copper binuclear center of cytochrome c oxidase.
Topics: Animals; Binding Sites; Catalytic Domain; Cattle; Copper; Electron Transport Complex IV; Heme; Hydrogen-Ion Concentration; Models, Molecular; Protein Conformation; Rhodobacter sphaeroides; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Temperature; Tyrosine | 2001 |
Characterization of the coral allene oxide synthase active site with UV-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopy: evidence for tyrosinate ligation to the ferric enzyme heme iron.
Topics: Animals; Azides; Binding Sites; Catalase; Cattle; Circular Dichroism; Cnidaria; Cyanides; Electron Spin Resonance Spectroscopy; Ferric Compounds; Ferrous Compounds; Fluorides; Free Radicals; Heme; Intramolecular Oxidoreductases; Iron; Ligands; Peracetic Acid; Spectrophotometry, Ultraviolet; Tyrosine | 2001 |
Very high resolution structure of a trematode hemoglobin displaying a TyrB10-TyrE7 heme distal residue pair and high oxygen affinity.
Topics: Amino Acid Sequence; Animals; Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Heme; Hydrogen Bonding; Iron; Kinetics; Ligands; Methemoglobin; Models, Molecular; Molecular Sequence Data; Oxygen; Paramphistomatidae; Protein Structure, Quaternary; Protein Structure, Secondary; Sequence Alignment; Thermodynamics; Tyrosine | 2001 |
Mechanism of peroxynitrite interaction with ferric hemoglobin and identification of nitrated tyrosine residues. CO(2) inhibits heme-catalyzed scavenging and isomerization.
Topics: Carbon Dioxide; Carboxyhemoglobin; Electron Spin Resonance Spectroscopy; Ferric Compounds; Free Radical Scavengers; Heme; Humans; In Vitro Techniques; Isomerism; Methemoglobin; Peroxynitrous Acid; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry; Spin Labels; Tyrosine | 2001 |
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 |
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 |
Role of conserved tyrosine 343 in intramolecular electron transfer in human sulfite oxidase.
Topics: Amino Acid Substitution; Animals; Binding Sites; Chickens; Conserved Sequence; Electron Transport; Heme; Humans; Hydrogen-Ion Concentration; Hydroxides; Kinetics; Molybdenum; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Photolysis; Recombinant Proteins; Spectrophotometry; Tyrosine | 2003 |
Structure and kinetic properties of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with the d1 heme active site ligand tyrosine 25 replaced by serine.
Topics: Binding Sites; Cytochromes; Electron Transport Complex IV; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Heme; Kinetics; Ligands; Mutagenesis; Nitrite Reductases; Paracoccus; Protein Structure, Tertiary; Serine; Spectrometry, Mass, Electrospray Ionization; Tyrosine | 2003 |
Different pathways of radical translocation in yeast cytochrome c peroxidase and its W191F mutant on reaction with H(2)O(2) suggest an antioxidant role.
Topics: Amino Acid Substitution; Antioxidants; Cross-Linking Reagents; Cytochrome c Group; Cytochrome-c Peroxidase; Dimerization; Free Radicals; Fungal Proteins; Heme; Hydrogen Peroxide; Models, Molecular; Nitroso Compounds; Oxidation-Reduction; Oxygen; Recombinant Proteins; Saccharomyces cerevisiae; Spectrometry, Mass, Electrospray Ionization; Spin Labels; Tyrosine | 2003 |
Spectroscopic characterization of five- and six-coordinate ferrous-NO heme complexes. Evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide synthase.
Topics: Circular Dichroism; Cysteine; Electron Spin Resonance Spectroscopy; Ferric Compounds; Ferrous Compounds; Heme; Humans; Iron-Sulfur Proteins; Ligands; Mutagenesis, Site-Directed; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Phenylalanine; Protein Structure, Tertiary; Solvents; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine | 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 |
The nature of heme/iron-induced protein tyrosine nitration.
Topics: Animals; Brain; Heme; Hemeproteins; Hydrogen Peroxide; Kidney; Kinetics; Liver; Male; Mice; Muscle, Skeletal; Myocardium; Nitrates; Organ Specificity; Peroxidase; Sodium Nitrite; Tyrosine | 2003 |
A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O.
Topics: Amino Acid Sequence; Bacterial Proteins; Crystallography, X-Ray; Heme; Hemoglobins; Hydrogen Bonding; Models, Molecular; Protein Conformation; Protein Structure, Secondary; Truncated Hemoglobins; Tyrosine | 2003 |
Intra- and intermolecular transfers of protein radicals in the reactions of sperm whale myoglobin with hydrogen peroxide.
Topics: Animals; Chromatography, Gel; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Dimerization; Electrons; Electrophoresis, Polyacrylamide Gel; Free Radicals; Heme; Hydrogen Peroxide; Iron; Models, Chemical; Mutagenesis, Site-Directed; Mutation; Myoglobin; Time Factors; Tyrosine; Ultraviolet Rays; Whales | 2003 |
Role of acidic and aromatic amino acids in Rhodobacter capsulatus cytochrome c1. A site-directed mutagenesis study.
Topics: Amino Acids; Animals; Cattle; Chickens; Cytochromes c1; Electron Spin Resonance Spectroscopy; Heme; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Photosynthesis; Protein Binding; Rhodobacter capsulatus; Tyrosine; Yeasts | 2003 |
Rapid formation of compound II and a tyrosyl radical in the Y229F mutant of Mycobacterium tuberculosis catalase-peroxidase disrupts catalase but not peroxidase function.
Topics: Bacterial Proteins; Catalase; Electron Spin Resonance Spectroscopy; Escherichia coli; Free Radicals; Gene Expression; Heme; Iron; Mutagenesis; Mycobacterium tuberculosis; Peroxidase; Peroxidases; Structure-Activity Relationship; Transfection; Tyrosine | 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 |
Normal and abnormal tyrosine side-chains in various heme proteins.
Topics: Blood Proteins; Heme; Hemeproteins; Tyrosine | 1962 |
CHANGES IN SIDE CHAIN REACTIVITY ACCOMPANYING THE BINDING OF HEME TO SPERM WHALE APOMYOGLOBIN.
Topics: Acetates; Animals; Apoproteins; Cetacea; Chemical Phenomena; Chemistry; Heme; Hydrogen-Ion Concentration; Imidazoles; Myoglobin; Research; Spectrophotometry; Sperm Whale; Tyrosine | 1964 |
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 |
Mechanism of peroxynitrite interaction with cytochrome c.
Topics: Amino Acids; Bicarbonates; Cytochromes c; Heme; Hydrogen Peroxide; Kinetics; Oxidation-Reduction; Peroxynitrous Acid; Protein Conformation; Spectrophotometry; Tyrosine | 2003 |
Role of the aromatic ring of Tyr43 in tetraheme cytochrome c(3) from Desulfovibrio vulgaris Miyazaki F.
Topics: Amino Acid Substitution; Computer Simulation; Cytochrome c Group; Desulfovibrio vulgaris; Enzyme Activation; Enzyme Stability; Heme; Hydrocarbons, Aromatic; Lasers; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Photolysis; Protein Conformation; Recombinant Proteins; Structure-Activity Relationship; Tyrosine | 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 |
Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins.
Topics: Amino Acid Substitution; Animals; Aplysia; Apoproteins; Evolution, Molecular; Globins; Heme; Mutagenesis, Site-Directed; Myoglobin; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence; Thermodynamics; Tryptophan; Tyrosine; Urea; Whales | 2004 |
Protein radical formation during lactoperoxidase-mediated oxidation of the suicide substrate glutathione: immunochemical detection of a lactoperoxidase radical-derived 5,5-dimethyl-1-pyrroline N-oxide nitrone adduct.
Topics: Amino Acids; Ascorbic Acid; Azides; Blotting, Western; Catalase; Cyclic N-Oxides; Cysteine; Dose-Response Relationship, Drug; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Free Radicals; Glutathione; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Immunochemistry; Iodides; Lactoperoxidase; Models, Chemical; Nitrites; Nitrogen Oxides; Oxygen; Oxygen Consumption; Phenol; Spin Labels; Thiocyanates; Time Factors; Tyrosine | 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 |
Phe393 mutants of cytochrome P450 BM3 with modified heme redox potentials have altered heme vinyl and propionate conformations.
Topics: Amino Acid Substitution; Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Ferric Compounds; Ferrous Compounds; Heme; Iron-Sulfur Proteins; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Phenylalanine; Propionates; Protein Conformation; Protein Structure, Tertiary; Spectrum Analysis, Raman; Substrate Specificity; Tryptophan; Tyrosine; Vinyl Compounds | 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 |
Protonation of two adjacent tyrosine residues influences the reduction of cytochrome c by diphenylacetaldehyde: a possible mechanism to select the reducer agent of heme iron.
Topics: Aldehydes; Benzophenones; Biphenyl Compounds; Chromatography, High Pressure Liquid; Circular Dichroism; Cytochromes c; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Hydrogen-Ion Concentration; Iodine; Iron; Mass Spectrometry; Oxidation-Reduction; Oxygen Consumption; Protons; Reducing Agents; Tyrosine | 2004 |
Heme as an optical probe of a conformational transition of ovine recPrP.
Topics: Animals; Carbon Monoxide; Fluorescent Dyes; Heme; Peptides; Prions; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Sheep; Spectrometry, Fluorescence; Temperature; Tryptophan; Tyrosine | 2004 |
Haptoglobin phenotypes differ in their ability to inhibit heme transfer from hemoglobin to LDL.
Topics: Alkadienes; Alleles; Antioxidants; Biological Transport; Haptoglobins; Heme; Hemoglobins; Humans; Kinetics; Lipoproteins, LDL; Methemoglobin; Oxidation-Reduction; Phenotype; Spectrophotometry, Ultraviolet; Tyrosine | 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 |
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 |
Crystal structure of Mycobacterium tuberculosis catalase-peroxidase.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalysis; Crystallography, X-Ray; Heme; Models, Molecular; Molecular Sequence Data; Mutation; Mycobacterium tuberculosis; Peroxidases; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Tryptophan; Tyrosine | 2004 |
Redox characterization of Geobacter sulfurreducens cytochrome c7: physiological relevance of the conserved residue F15 probed by site-specific mutagenesis.
Topics: Amino Acid Substitution; Bacterial Proteins; Conserved Sequence; Cytochrome c Group; Desulfuromonas; Geobacter; Heme; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Phenylalanine; Protons; Spectrophotometry, Ultraviolet; Thermodynamics; Tyrosine | 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 |
Short-term inhibitory effects of nitric oxide on cytochrome P450-mediated drug metabolism: time dependency and reversibility profiles in isolated perfused rat livers.
Topics: Animals; Bile; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Cytochromes b5; Enzyme Inhibitors; Heme; In Vitro Techniques; Liver; Male; Microsomes, Liver; Nitric Oxide; Nitric Oxide Donors; Nitroprusside; Pharmaceutical Preparations; Proteins; Rats; Rats, Sprague-Dawley; Sulfhydryl Compounds; Time Factors; Tyrosine | 2004 |
Hydroxyl radical oxidation of cytochrome c by aerobic radiolysis.
Topics: Aerobiosis; Amino Acid Sequence; Animals; Cytochromes c; Dose-Response Relationship, Radiation; Electrons; Heme; Horses; Hydroxyl Radical; Hydroxylation; Intracellular Membranes; Methionine; Mitochondria, Heart; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Peptide Fragments; Phenylalanine; Protein Conformation; Pulse Radiolysis; Rats; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrophotometry, Ultraviolet; Tyrosine | 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 |
Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis.
Topics: Bacillus subtilis; Bacterial Proteins; Biophysics; Carbon Monoxide; Circular Dichroism; Heme; Hydrogen-Ion Concentration; Kinetics; Leucine; Ligands; Models, Molecular; Mutation; Oxygen; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Signal Transduction; Spectrophotometry; Spectrophotometry, Infrared; Spectroscopy, Fourier Transform Infrared; Temperature; Time Factors; Tryptophan; Tyrosine; Ultracentrifugation; Ultraviolet Rays | 2005 |
Tyrosine B10 and heme-ligand interactions of Lucina pectinata hemoglobin II: control of heme reactivity.
Topics: Animals; Heme; Hemoglobins; Hydrogen Peroxide; Hydrogen-Ion Concentration; Iron; Kinetics; Ligands; Models, Chemical; Mollusca; Mutation; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Tyrosine | 2005 |
Structure of the complex between plastocyanin and cytochrome f from the cyanobacterium Nostoc sp. PCC 7119 as determined by paramagnetic NMR. The balance between electrostatic and hydrophobic interactions within the transient complex determines the relati
Topics: Animals; Cytochromes f; Electrons; Heme; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Nostoc; Plasmodium; Plastocyanin; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Software; Static Electricity; Tyrosine | 2005 |
A comparative reactivity study of microperoxidases based on hemin, mesohemin and deuterohemin.
Topics: Benzothiazoles; Computational Biology; Dipeptides; Electrochemistry; Heme; Hemin; Hydrogen Peroxide; Kinetics; Magnetic Resonance Spectroscopy; Mesoporphyrins; Models, Biological; Oligopeptides; Peroxidases; Sulfonic Acids; Tyrosine | 2005 |
Local compressibilities of proteins: comparison of optical experiments and simulations for horse heart cytochrome-c.
Topics: Absorption; Algorithms; Animals; Computer Simulation; Cytochromes c; Glycerol; Heme; Horses; Models, Molecular; Myocardium; Porphyrins; Pressure; Proteins; Software; Solvents; Spectrophotometry; Stress, Mechanical; Temperature; Tensile Strength; Tyrosine; Water | 2005 |
The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalase; Catalysis; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Crystallography, X-Ray; Heme; Hydrogen Peroxide; Kinetics; Mass Spectrometry; Methionine; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mycobacterium tuberculosis; Peptides; Peracetic Acid; Plasmids; Protein Binding; Recombinant Proteins; Spectrophotometry; Time Factors; Trypsin; Tryptophan; Tyrosine; Ultraviolet Rays | 2005 |
Insight into molecular stability and physiological properties of the diheme cytochrome CYC41 from the acidophilic bacterium Acidithiobacillus ferrooxidans.
Topics: Acidithiobacillus; Azurin; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Electron Transport; Electron Transport Complex IV; Enzyme Stability; Escherichia coli; Heme; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Recombinant Proteins; Surface Plasmon Resonance; Tyrosine | 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 |
The highly conserved Glu149 and Tyr190 residues contribute to peroxynitrite-mediated nitrotyrosine formation and the catalytic activity of cytochrome P450 2B1.
Topics: Catalysis; Conserved Sequence; Cytochrome P-450 CYP2B1; Escherichia coli; Glutamine; Heme; Hydrogen Bonding; Iron; Kinetics; Models, Molecular; Molecular Sequence Data; Oxidoreductases; Peroxynitrous Acid; Plasmids; Temperature; Tyrosine | 2005 |
Easy oxidation and nitration of human myoglobin by nitrite and hydrogen peroxide.
Topics: Heme; Humans; Hydrogen Peroxide; Myoglobin; Nitrites; Oxidation-Reduction; Sulfinic Acids; Tyrosine | 2006 |
Spectroscopic characterization of the iron-oxo intermediate in cytochrome P450.
Topics: Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; Iron; Protein Structure, Tertiary; Tryptophan; Tyrosine | 2005 |
Picosecond structural dynamics of myoglobin following photodissociation of carbon monoxide as revealed by ultraviolet time-resolved resonance Raman spectroscopy.
Topics: Carbon Monoxide; Heme; Models, Molecular; Myoglobin; Photolysis; Spectrum Analysis, Raman; Time Factors; Tryptophan; Tyrosine; Ultraviolet Rays | 2005 |
Increase in heme oxygenase-1 levels ameliorates renovascular hypertension.
Topics: Aldosterone; Animals; Cyclooxygenase 1; Cyclooxygenase 2; Dinoprostone; Enzyme Activation; Enzyme Inhibitors; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Hypertension, Renal; Juxtaglomerular Apparatus; Kidney; Male; Metalloporphyrins; Organ Size; Protoporphyrins; Rats; Rats, Sprague-Dawley; Renin; Tyrosine | 2005 |
Heme catalyzes tyrosine 385 nitration and inactivation of prostaglandin H2 synthase-1 by peroxynitrite.
Topics: Amino Acid Sequence; Animals; Apoenzymes; Binding Sites; Catalysis; Chromatography, Ion Exchange; Cyclooxygenase 1; Electrophoresis, Polyacrylamide Gel; Free Radical Scavengers; Heme; Hemin; Holoenzymes; Hydroxyl Radical; Male; Models, Chemical; Molecular Sequence Data; Molsidomine; Peroxynitrous Acid; Seminal Vesicles; Sheep; Tyrosine | 2006 |
Multiple active site conformers in the carbon monoxide complexes of trematode hemoglobins.
Topics: Amino Acid Sequence; Animals; Binding Sites; Carbon Monoxide; Carboxyhemoglobin; Heme; Hemoglobins; Hydrogen Bonding; Iron; Models, Molecular; Molecular Sequence Data; Oxygen; Oxyhemoglobins; Protein Conformation; Sequence Homology, Amino Acid; Spectrum Analysis, Raman; Trematoda; Tyrosine | 2006 |
Ligand interactions in the distal heme pocket of Mycobacterium tuberculosis truncated hemoglobin N: roles of TyrB10 and GlnE11 residues.
Topics: Amino Acid Sequence; Amino Acid Substitution; Carboxyhemoglobin; Crystallography, X-Ray; Ferric Compounds; Ferrous Compounds; Glutamine; Heme; Hemeproteins; Leviviridae; Ligands; Mycobacterium tuberculosis; Oxyhemoglobins; Spectrum Analysis, Raman; Truncated Hemoglobins; Tyrosine | 2006 |
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 |
Expression of human myoglobin in H9c2 cells enhances toxicity to added hydrogen peroxide.
Topics: Amino Acid Sequence; Animals; Apoptosis; Cells, Cultured; Cross-Linking Reagents; Heme; Humans; Hydrogen Peroxide; Myocardial Reperfusion Injury; Myocytes, Cardiac; Myoglobin; Rats; Reactive Oxygen Species; Transfection; Tyrosine | 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 |
Protein tyrosine nitration induced by heme/hydrogen peroxide: inhibitory effect of hydroxycinnamoyl conjugates.
Topics: Asteraceae; Catalysis; Coumaric Acids; Heme; Hemeproteins; Humans; Hydrogen Peroxide; Hydrogen-Ion Concentration; Inhibitory Concentration 50; Leukocytes; Nitrates; Phytotherapy; Tyrosine | 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 |
Modulation of protein tyrosine nitration and inflammatory mediators by isoprenylhydroquinone glucoside.
Topics: 3T3 Cells; Animals; Blotting, Western; Cell Survival; Cell-Free System; Cells, Cultured; Fibroblasts; Glucosides; Heme; Humans; Hydrogen Peroxide; Hydroquinones; Inflammation Mediators; Interleukin-1beta; Lipopolysaccharides; Mice; Neutrophils; Nitrates; Nitric Oxide Synthase Type II; Nitrites; Peroxynitrous Acid; Reverse Transcriptase Polymerase Chain Reaction; Rhodamines; Serum Albumin, Bovine; Stimulation, Chemical; Tetradecanoylphorbol Acetate; Tumor Necrosis Factor-alpha; Tyrosine | 2007 |
Oxyferryl heme and not tyrosyl radical is the likely culprit in prostaglandin H synthase-1 peroxidase inactivation.
Topics: Animals; Cyclooxygenase Inhibitors; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; In Vitro Techniques; Kinetics; Leukotrienes; Lipid Peroxides; Male; Models, Biological; Prostaglandin-Endoperoxide Synthases; Sheep; Tyrosine | 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 |
Tyrosine-heme ligation in heme-peptide complex: design based on conserved motif of catalase.
Topics: Amino Acid Sequence; Catalase; Circular Dichroism; Conserved Sequence; Heme; Molecular Mimicry; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Peptides; Protein Binding; Spectrophotometry, Ultraviolet; Tyrosine | 2007 |
Induction of heme oxygenase-1 in renovascular hypertension is associated with inhibition of apoptosis.
Topics: Animals; Apoptosis; bcl-X Protein; Caspases; Gene Expression Regulation; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Hypertension, Renovascular; Kidney; Male; Proto-Oncogene Proteins c-bcl-2; Rats; Rats, Sprague-Dawley; Tyrosine | 2007 |
The roles of Tyr(CD1) and Trp(G8) in Mycobacterium tuberculosis truncated hemoglobin O in ligand binding and on the heme distal site architecture.
Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; DNA Primers; Heme; Hemoglobins; Hydrogen Bonding; Ligands; Mutagenesis; Spectrum Analysis, Raman; Truncated Hemoglobins; Tryptophan; Tyrosine | 2007 |
Peroxynitrite inactivation of human cytochrome P450s 2B6 and 2E1: heme modification and site-specific nitrotyrosine formation.
Topics: Amino Acid Sequence; Aryl Hydrocarbon Hydroxylases; Carbon Monoxide; Cytochrome P-450 CYP2B6; Cytochrome P-450 CYP2E1; Cytochrome P-450 CYP2E1 Inhibitors; Enzyme Inhibitors; Heme; Humans; Models, Molecular; Molecular Sequence Data; Oxidoreductases, N-Demethylating; Peroxynitrous Acid; tert-Butylhydroperoxide; Tyrosine | 2007 |
Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: potential oxidation sites for oxidative polymerization of lignin.
Topics: Cations; Cell Wall; Heme; Lignin; Models, Molecular; Molecular Sequence Data; Molecular Structure; Molecular Weight; Oxidation-Reduction; Peroxidases; Populus; Sequence Alignment; Substrate Specificity; Surface Properties; Tyrosine | 2008 |
The reactivity of heme in biological systems: autocatalytic formation of both tyrosine-heme and tryptophan-heme covalent links in a single protein architecture.
Topics: Amino Acid Sequence; Ascorbate Peroxidases; Catalysis; Chromatography, High Pressure Liquid; Electron Spin Resonance Spectroscopy; Glycine max; Heme; Hydrogen Peroxide; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Peroxidases; Recombinant Proteins; Tryptophan; Tyrosine | 2007 |
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 |
Protein conformation changes of HemAT-Bs upon ligand binding probed by ultraviolet resonance Raman spectroscopy.
Topics: Bacillus subtilis; Bacterial Proteins; Gene Expression Regulation, Bacterial; Heme; Heme-Binding Proteins; Hemeproteins; Hydrogen Bonding; Ligands; Models, Biological; Models, Molecular; Molecular Conformation; Mutation; Oxygen; Protein Conformation; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Tyrosine | 2008 |
Tyrosine as a redox-active center in electron transfer to ferryl heme in globins.
Topics: Animals; Ascorbic Acid; Electron Transport; Globins; Heme; Iron Chelating Agents; Kinetics; Metmyoglobin; Models, Molecular; Oxidation-Reduction; Reducing Agents; Tyrosine | 2008 |
Nitration of solvent-exposed tyrosine 74 on cytochrome c triggers heme iron-methionine 80 bond disruption. Nuclear magnetic resonance and optical spectroscopy studies.
Topics: Amino Acid Substitution; Animals; Apoptosis; Cardiolipins; Cytochromes c; Heme; Horses; Hydrogen-Ion Concentration; Iron; Mitochondrial Proteins; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Peroxynitrous Acid; Point Mutation; Protein Processing, Post-Translational; Tyrosine | 2009 |
Probing the heme-binding site of the cytochrome c maturation protein CcmE.
Topics: Amino Acid Substitution; Apoproteins; Bacterial Outer Membrane Proteins; Binding Sites; Cytochromes c; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Ligands; Magnetic Resonance Spectroscopy; Methionine; Mutant Proteins; Mutation; Oxidation-Reduction; Potentiometry; Protein Structure, Secondary; Tyrosine | 2009 |
Heme d1 nitrosyl complex of cd1 nitrite reductase studied by high-field-pulse electron paramagnetic resonance spectroscopy.
Topics: Bacterial Proteins; Crystallization; Cytochromes; Electron Spin Resonance Spectroscopy; Heme; Ligands; Nitric Oxide; Nitrite Reductases; Protein Binding; Protein Conformation; Pseudomonas aeruginosa; Tyrosine | 2009 |
Crystallization and preliminary X-ray crystallographic analysis of a new crystal form of hydroxylamine oxidoreductase from Nitrosomonas europaea.
Topics: Crystallization; Crystallography, X-Ray; Heme; Nitrosomonas europaea; Oxidoreductases; Protein Structure, Quaternary; Protein Subunits; Tyrosine | 2009 |
Physical evidence for substrate binding in preventing cyclooxygenase inactivation under nitrative stress.
Topics: Amino Acid Sequence; Animals; Arachidonic Acid; Catalytic Domain; Chromatography, High Pressure Liquid; Chromatography, Liquid; Cyclooxygenase 1; Cyclooxygenase Inhibitors; Electrochemistry; Enzyme Activation; Heme; Humans; Mice; Molecular Sequence Data; Peroxynitrous Acid; Prostaglandin-Endoperoxide Synthases; Protein Binding; Protein Multimerization; Protein Structure, Quaternary; Rats; Stress, Physiological; Substrate Specificity; Tandem Mass Spectrometry; Tyrosine | 2010 |
Incorporation of tyrosine and glutamine residues into the soluble guanylate cyclase heme distal pocket alters NO and O2 binding.
Topics: Amino Acid Sequence; Animals; Glutamine; Guanosine Triphosphate; Guanylate Cyclase; Heme; Kinetics; Molecular Sequence Data; Nitric Oxide; Oxygen; Porphyrins; Protein Binding; Rats; Receptors, Cytoplasmic and Nuclear; Sequence Homology, Amino Acid; Soluble Guanylyl Cyclase; Spectrophotometry; Tyrosine | 2010 |
Red cells, hemoglobin, heme, iron, and atherogenesis.
Topics: Aorta; Atherosclerosis; Cell Survival; Cells, Cultured; Endothelial Cells; Erythrocytes; Glutathione; Glutathione Peroxidase; Haptoglobins; Hematoma; Heme; Heme Oxygenase-1; Hemoglobins; Hemolysis; Hemopexin; Humans; Iron; Lipid Peroxidation; Lipoproteins, LDL; Methemoglobin; Oxidation-Reduction; Oxidative Stress; Tyrosine | 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 |
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 |
Perturbed heme binding is responsible for the blistering phenotype associated with mutations in the Caenorhabditis elegans dual oxidase 1 (DUOX1) peroxidase domain.
Topics: Amino Acid Substitution; Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Dual Oxidases; Heme; Humans; Models, Molecular; Mutation; NADPH Oxidases; Oxidoreductases; Protein Binding; Protein Structure, Tertiary; Tyrosine | 2010 |
Catalytic mechanism of a heme and tyrosyl radical-containing fatty acid α-(di)oxygenase.
Topics: Biocatalysis; Dioxygenases; Enzyme Activation; Fatty Acids; Free Radicals; Heme; Kinetics; Molecular Structure; Oxidation-Reduction; Oxygen; Tyrosine | 2011 |
Early failure of N-methyl-D-aspartate receptors and deficient spine formation induced by reduction of regulatory heme in neurons.
Topics: Adenosine Triphosphate; Animals; Base Sequence; DNA Primers; Female; Heme; Male; Mice; Mice, Inbred BALB C; Neurons; Oxidation-Reduction; Phosphorylation; Polymerase Chain Reaction; Receptors, N-Methyl-D-Aspartate; Tyrosine | 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 |
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 |
Topography of tyrosine residues and their involvement in peroxidation of polyunsaturated cardiolipin in cytochrome c/cardiolipin peroxidase complexes.
Topics: Animals; Cardiolipins; Computer Simulation; Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen Peroxide; Iron; Magnetic Resonance Spectroscopy; Mitochondrial Membranes; Mutation; Myocardium; Oxygen; Oxygenases; Peroxidase; Peroxidases; Phenylalanine; Tyrosine | 2011 |
Radical formation in cytochrome c oxidase.
Topics: Animals; Ascorbic Acid; Binding Sites; Biocatalysis; Cattle; Copper; Dithionite; Electron Spin Resonance Spectroscopy; Electron Transport; Electron Transport Complex IV; Free Radicals; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Models, Chemical; Models, Molecular; Oxidation-Reduction; Oxygen; Peroxides; Protein Binding; Protons; Tyrosine | 2011 |
Experimental and computational investigations of oxygen reactivity in a heme and tyrosyl radical-containing fatty acid α-(di)oxygenase.
Topics: Binding, Competitive; Diffusion; Dioxygenases; Electron Transport; Fatty Acids; Free Radicals; Heme; Kinetics; Models, Molecular; Oryza; Oxygen; Oxygen Isotopes; Protein Binding; Protein Conformation; Quantum Theory; Solvents; Stereoisomerism; Substrate Specificity; Tyrosine; Viscosity | 2011 |
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer.
Topics: Antigens, Bacterial; Binding Sites; Carrier Proteins; Cation Transport Proteins; Crystallography, X-Ray; Heme; Iron; Kinetics; Models, Chemical; Models, Molecular; Mutation; Myoglobin; Protein Binding; Protoporphyrins; Staphylococcus aureus; Tyrosine | 2011 |
A heme peroxidase with a functional role as an L-tyrosine hydroxylase in the biosynthesis of anthramycin.
Topics: Anthramycin; Cloning, Molecular; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Hydrogen Peroxide; Kinetics; Levodopa; Models, Chemical; Oxygen; Peroxidases; Spectrophotometry, Ultraviolet; Streptomyces; Tyrosine; Tyrosine 3-Monooxygenase | 2011 |
Nitration of tyrosines 46 and 48 induces the specific degradation of cytochrome c upon change of the heme iron state to high-spin.
Topics: Amino Acid Sequence; Animals; Arabidopsis Proteins; Cytochromes c; Heme; Horses; Humans; Iron; Models, Molecular; Molecular Sequence Data; Nitrates; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; Reactive Nitrogen Species; Reactive Oxygen Species; Sequence Alignment; Tyrosine | 2011 |
Mutation of Phe413 to Tyr in catalase KatE from Escherichia coli leads to side chain damage and main chain cleavage.
Topics: Arginine; Catalase; Crystallography, X-Ray; Escherichia coli; Genetic Variation; Heme; Hydrogen Peroxide; Kinetics; Mass Spectrometry; Models, Molecular; Molecular Conformation; Mutation; Oxygen; Phenylalanine; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tyrosine | 2012 |
δ-Aminolevulinate synthase is required for apical transcellular barrier formation in the skin of the Drosophila larva.
Topics: 5-Aminolevulinate Synthetase; Animals; Chitin; Drosophila; Epidermis; Heme; Larva; Tyrosine; Water | 2012 |
Tyrosine triad at the interface between the Rieske iron-sulfur protein, cytochrome c1 and cytochrome c2 in the bc1 complex of Rhodobacter capsulatus.
Topics: Amino Acid Sequence; Animals; Biocatalysis; Cytochromes c1; Cytochromes c2; Electron Transport Complex III; Electrophoresis, Polyacrylamide Gel; Heme; Models, Molecular; Molecular Sequence Data; Mutation; Rhodobacter capsulatus; Sequence Alignment; Spectrum Analysis; Tyrosine | 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 |
Perturbation of the redox site structure of cytochrome c variants upon tyrosine nitration.
Topics: Cytochromes c; Fatty Acids; Heme; Humans; Iron; Kinetics; Lysine; Methionine; Mutation; Nitro Compounds; Oxidation-Reduction; Phenylalanine; Protein Stability; Protein Structure, Quaternary; Recombinant Proteins; Silver Compounds; Static Electricity; Sulfhydryl Compounds; Tyrosine; Water | 2012 |
Haptoglobin binding stabilizes hemoglobin ferryl iron and the globin radical on tyrosine β145.
Topics: Electron Spin Resonance Spectroscopy; Free Radicals; Haptoglobins; Heme; Hemoglobins; Humans; Hydrogen-Ion Concentration; Iron; Lipid Peroxidation; Oxidation-Reduction; Protein Binding; Protein Stability; Tyrosine | 2013 |
Tyrosine B10 triggers a heme propionate hydrogen bonding network loop with glutamine E7 moiety.
Topics: Animals; Glutamine; Heme; Hemoglobins; Hydrogen Bonding; Ligands; Mutation; Nuclear Magnetic Resonance, Biomolecular; Propionates; Tyrosine | 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 |
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 |
Electrochemical nitration of myoglobin at tyrosine 103: structure and stability.
Topics: Animals; Circular Dichroism; Electrochemical Techniques; Heme; Horses; Humans; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Muscle, Skeletal; Myoglobin; Nuclear Magnetic Resonance, Biomolecular; Protein Stability; Protein Structure, Secondary; Protein Structure, Tertiary; Tyrosine | 2013 |
Roles of conserved Arg(72) and Tyr(71) in the ascorbate-specific transmembrane electron transfer catalyzed by Zea mays cytochrome b561.
Topics: Arginine; Ascorbic Acid; Binding Sites; Biocatalysis; Cytochrome b Group; Electron Transport; Heme; Lysine; Mutagenesis, Site-Directed; Tyrosine; Zea mays | 2013 |
Stable ruthenium nitrosyl porphyrins with axial O-bonded ligands; preparation and redox behavior.
Topics: Crystallography, X-Ray; Electrochemistry; Heme; Ligands; Models, Chemical; Molecular Structure; Oxidation-Reduction; Porphyrins; Ruthenium; Spectroscopy, Fourier Transform Infrared; Tyrosine | 2013 |
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin.
Topics: Actinomycetales; Catalytic Domain; Cyanides; Heme; Hemoglobins; Hydrogen Bonding; Hydrogen-Ion Concentration; Hydroxides; Molecular Dynamics Simulation; Protein Binding; Spectrum Analysis, Raman; Tyrosine; Water | 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 |
Tyrosine nitration moderates the peptidase activity of human methionyl aminopeptidase 2.
Topics: Amino Acid Sequence; Aminopeptidases; Binding Sites; Crystallography, X-Ray; Enzyme Activation; Glycoproteins; Heme; Humans; Methionyl Aminopeptidases; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Tyrosine | 2013 |
Tyrosine residues play an important role in heme detoxification by serum albumin.
Topics: Heme; Humans; Nitrates; Peroxidases; Protein Carbonylation; Serum Albumin; Tyrosine | 2014 |
Lincomycin biosynthesis involves a tyrosine hydroxylating heme protein of an unusual enzyme family.
Topics: Anti-Bacterial Agents; Bacterial Proteins; Chromatography, High Pressure Liquid; Circular Dichroism; Dihydroxyphenylalanine; Escherichia coli; Gene Expression; Heme; Hemeproteins; Hydroxylation; Iron; Lincomycin; Multigene Family; Recombinant Proteins; Streptomyces; Tyrosine; Tyrosine 3-Monooxygenase | 2013 |
The kinetics of the reaction of nitrogen dioxide with iron(II)- and iron(III) cytochrome c.
Topics: Amino Acids; Cytochromes c; Heme; Humans; Hydrogen-Ion Concentration; Iron; Kinetics; Nitrogen Dioxide; Oxidation-Reduction; Pulse Radiolysis; Tryptophan; Tyrosine | 2014 |
Heme oxygenase suppresses markers of heart failure and ameliorates cardiomyopathy in L-NAME-induced hypertension.
Topics: Adiponectin; Aldosterone; Animals; Antioxidants; Arginine; Atrial Natriuretic Factor; Biomarkers; Blood Pressure; Cardiomyopathies; Cardiotonic Agents; Chemokine CCL2; Chemokine CCL3; Cyclic GMP; Dinoprost; Endothelin-1; Enzyme Induction; Extracellular Matrix Proteins; Heart Failure; Heme; Heme Oxygenase (Decyclizing); Hypertension; Interleukin-1beta; Interleukin-6; Male; NG-Nitroarginine Methyl Ester; Rats; Rats, Sprague-Dawley; Tumor Necrosis Factor-alpha; Tyrosine | 2014 |
Identifying the elusive sites of tyrosyl radicals in cytochrome c peroxidase: implications for oxidation of substrates bound at a site remote from the heme.
Topics: Amino Acid Substitution; Binding Sites; Biocatalysis; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Electron Transport; Expectorants; Guaiacol; Heme; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins; Oxidation-Reduction; Protein Conformation; Recombinant Fusion Proteins; Saccharomyces cerevisiae Proteins; Surface Properties; Tryptophan; Tyrosine | 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 |
Key roles for tyrosine 10 in aβ-heme complexes and its relevance to oxidative stress.
Topics: Amyloid beta-Peptides; Heme; Humans; Oxidative Stress; Peroxidases; Tyrosine | 2015 |
How covalent heme to protein bonds influence the formation and reactivity of redox intermediates of a bacterial peroxidase.
Topics: Bromides; Catalysis; Cyanides; Electrons; Escherichia coli; Heme; Horseradish Peroxidase; Hydrogen Peroxide; Iodides; Iron; Lactoperoxidase; Models, Chemical; Oxidation-Reduction; Oxygen; Peroxidase; Peroxidases; Protein Binding; Protein Processing, Post-Translational; Spectrophotometry; Thiocyanates; Tyrosine | 2014 |
Computational insight into nitration of human myoglobin.
Topics: Catalytic Domain; Heme; Humans; Molecular Dynamics Simulation; Myoglobin; Nitrites; Protein Conformation; Protein Processing, Post-Translational; Tryptophan; Tyrosine | 2014 |
A structural and functional perspective on the evolution of the heme-copper oxidases.
Topics: Evolution, Molecular; Heme; Models, Molecular; Oxidoreductases; Protein Conformation; Tyrosine | 2014 |
Nitration of Y10 in Aβ1-40: is it a compensatory reaction against oxidative/nitrative stress and Aβ aggregation?
Topics: Amyloid beta-Peptides; Cell Line, Tumor; Cell Survival; Heme; Humans; Hydrogen Peroxide; Nitrites; Oxidative Stress; Peptide Fragments; Peroxidases; Protein Processing, Post-Translational; Tyrosine | 2015 |
A novel tyrosine-heme C−O covalent linkage in F43Y myoglobin: a new post-translational modification of heme proteins.
Topics: Amino Acid Substitution; Animals; Crystallography, X-Ray; Heme; Hydrogen Peroxide; Models, Molecular; Myoglobin; Oxidation-Reduction; Phenylalanine; Protein Conformation; Protein Processing, Post-Translational; Solutions; Spectrophotometry; Tyrosine; Whales | 2015 |
Leghemoglobin is nitrated in functional legume nodules in a tyrosine residue within the heme cavity by a nitrite/peroxide-dependent mechanism.
Topics: Glycine max; Heme; Hydrogen Peroxide; Leghemoglobin; Nitrates; Nitric Oxide; Nitrites; Nitrogen Dioxide; Oxidative Stress; Peroxynitrous Acid; Phaseolus; Protein Processing, Post-Translational; Tyrosine | 2015 |
The Heme Transport Capacity of LHR1 Determines the Extent of Virulence in Leishmania amazonensis.
Topics: Amino Acid Sequence; Animals; Biological Transport; Caenorhabditis elegans; Female; Genes, Reporter; Heme; Humans; Leishmania mexicana; Macrophages; Membrane Proteins; Mice; Mice, Inbred C57BL; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Protozoan Proteins; Saccharomyces cerevisiae; Sequence Alignment; Tyrosine; Virulence | 2015 |
Density Functional Theory Insights into the Role of the Methionine-Tyrosine-Tryptophan Adduct Radical in the KatG Catalase Reaction: O2 Release from the Oxyheme Intermediate.
Topics: Bacterial Proteins; Carbon; Catalase; Catalysis; Electrons; Heme; Hydrogen; Hydrogen Bonding; Methionine; Models, Chemical; Mycobacterium tuberculosis; Nitrogen; Oxygen; Quantum Theory; Tryptophan; Tyrosine | 2015 |
How a novel tyrosine-heme cross-link fine-tunes the structure and functions of heme proteins: a direct comparitive study of L29H/F43Y myoglobin.
Topics: Cross-Linking Reagents; Heme; Hemeproteins; Models, Molecular; Myoglobin; Protein Conformation; Tyrosine | 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 |
Endoperoxide formation by an α-ketoglutarate-dependent mononuclear non-haem iron enzyme.
Topics: Aspergillus fumigatus; Binding Sites; Biocatalysis; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Heme; Hydroxylation; Indoles; Iron; Ketoglutaric Acids; Oxygen; Prostaglandin Endoperoxides; Tyrosine | 2015 |
[Research on Early Diagnosis of Gastric Cancer by the Surface Enhanced Raman Spectroscopy of Human Hemoglobin].
Topics: Asparagine; Early Detection of Cancer; Heme; Hemoglobins; Humans; Methemoglobin; Multivariate Analysis; Oxyhemoglobins; Phenylalanine; Principal Component Analysis; Spectrum Analysis, Raman; Stomach Neoplasms; Tyrosine | 2015 |
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 |
Effect of protein structure and/or conformation on the dityrosine cross-linking induced by haem-hydrogen peroxide.
Topics: Cross-Linking Reagents; Dimerization; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Heme; Hemin; Humans; Hydrogen Peroxide; Oxidation-Reduction; Oxidative Stress; Protein Aggregates; Protein Conformation; Spectrum Analysis, Raman; Tyrosine | 2016 |
Haem-assisted dityrosine-cross-linking of fibrinogen under non-thermal plasma exposure: one important mechanism of facilitated blood coagulation.
Topics: Blood Cells; Blood Coagulation; Coordination Complexes; Cross-Linking Reagents; Fibrinogen; Heme; Hemin; Humans; Iron; Plasma Gases; Primary Cell Culture; Tyrosine | 2016 |
Distinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobin.
Topics: Crystallography, X-Ray; Heme; Hydrogen Bonding; Hydrogen Peroxide; Ligands; Models, Molecular; Mutation; Myoglobin; Protein Conformation; Protein Unfolding; Spectrum Analysis; Structure-Activity Relationship; Tyrosine | 2016 |
NADPH oxidase-derived H2O2 subverts pathogen signaling by oxidative phosphotyrosine conversion to PB-DOPA.
Topics: Campylobacter jejuni; Cell Line; Dihydroxyphenylalanine; Drug Resistance, Bacterial; Heme; Host-Pathogen Interactions; Humans; Hydrogen Peroxide; Immune System; Klebsiella pneumoniae; Listeria monocytogenes; NADPH Oxidases; Oxidation-Reduction; Oxidative Phosphorylation; Oxygen; Peroxidase; Phosphotyrosine; Reactive Oxygen Species; Salmonella enterica; Tyrosine | 2016 |
Role of a Conserved Tyrosine Residue in the FMN-Heme Interdomain Electron Transfer in Inducible Nitric Oxide Synthase.
Topics: Deuterium; Electron Transport; Heme; Hydrogen-Ion Concentration; Kinetics; Lasers; Nitric Oxide Synthase Type II; Protein Domains; Solvents; Tyrosine | 2016 |
Stabilization of cytochrome b
Topics: Animals; Catalytic Domain; Cattle; Circular Dichroism; Computer Simulation; Conserved Sequence; Crystallography, X-Ray; Cytochromes b5; Heme; Kinetics; Models, Molecular; Mutant Proteins; Protein Denaturation; Protein Stability; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Temperature; Tyrosine | 2017 |
Horseradish-Peroxidase-Catalyzed Tyrosine Click Reaction.
Topics: Binding Sites; Catalysis; Click Chemistry; Heme; Horseradish Peroxidase; Hydrogen Peroxide; Models, Molecular; Molecular Structure; Tyrosine | 2017 |
The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket.
Topics: Alanine; Circular Dichroism; Cytochromes c; Heme; Histamine; Humans; Kinetics; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Binding; Recombinant Proteins; Structure-Activity Relationship; Tyrosine | 2017 |
Switchable Redox Chemistry of the Hexameric Tyrosine-Coordinated Heme Protein.
Topics: Catalytic Domain; Heme; Hemeproteins; Models, Molecular; Oxidation-Reduction; Protein Conformation; Protein Multimerization; Rhodobacteraceae; Tyrosine | 2017 |
Triosephosphate isomerase tyrosine nitration induced by heme-NaNO
Topics: Acetophenones; Anthracenes; Antioxidants; Circular Dichroism; Flavonoids; Heme; Hydrogen Peroxide; Indicators and Reagents; Kinetics; Molsidomine; Oxidants; Oxidation-Reduction; Peroxynitrous Acid; Phytochemicals; Protein Processing, Post-Translational; Protein Structure, Secondary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sodium Nitrite; Triose-Phosphate Isomerase; Tyrosine | 2017 |
The Iron Chaperone Protein CyaY from Vibrio cholerae Is a Heme-Binding Protein.
Topics: Amino Acid Motifs; Bacterial Proteins; Binding Sites; Cloning, Molecular; Cysteine; Escherichia coli; Gene Expression; Heme; Hemeproteins; Ion Transport; Iron; Kinetics; Models, Molecular; Molecular Chaperones; Mutation; Protein Binding; Protein Interaction Domains and Motifs; Protein Multimerization; Protein Structure, Secondary; Recombinant Proteins; Tyrosine; Vibrio cholerae | 2017 |
Structural basis for binding and transfer of heme in bacterial heme-acquisition systems.
Topics: Amino Acid Motifs; Arginine; Binding Sites; Burkholderia cenocepacia; Chloroflexi; Cloning, Molecular; Crystallography, X-Ray; Escherichia coli; Gene Expression; Heme; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Iron; Models, Molecular; Periplasm; Periplasmic Binding Proteins; Plasmids; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Recombinant Proteins; Tyrosine | 2017 |
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 |
Living with Oxygen.
Topics: Catalytic Domain; Coordination Complexes; Cysteine; Cytochrome P-450 Enzyme System; Heme; Metals, Heavy; Methionine; Oxidation-Reduction; Oxygen; Protein Structural Elements; Tryptophan; Tyrosine | 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 |
Engineering tyrosine residues into hemoglobin enhances heme reduction, decreases oxidative stress and increases vascular retention of a hemoglobin based blood substitute.
Topics: Animals; Ascorbic Acid; Blood Substitutes; Electron Transport; HEK293 Cells; Heme; Hemoglobins; Humans; Iron; Methemoglobin; Mice; Mice, Nude; Oxidation-Reduction; Oxidative Stress; Oxygen; Oxyhemoglobins; Tyrosine | 2019 |
Nitration of hIAPP promotes its toxic oligomer formation and exacerbates its toxicity towards INS-1 cells.
Topics: Animals; Cell Line, Tumor; Heme; Hydrogen Peroxide; Islet Amyloid Polypeptide; Nitrites; Protein Binding; Protein Multimerization; Protein Processing, Post-Translational; Rats; Tyrosine | 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 |
Geometric and Electronic Structure Contributions to O-O Cleavage and the Resultant Intermediate Generated in Heme-Copper Oxidases.
Topics: Catalytic Domain; Copper; Density Functional Theory; Heme; Iron; Kinetics; Models, Chemical; Molecular Structure; Oxidation-Reduction; Oxidoreductases; Oxygen; Protons; Tyrosine | 2019 |
Lucina pectinata oxyhemoglobin (II-III) heterodimer pH susceptibility.
Topics: Animals; Bivalvia; Crystallography, X-Ray; Dimerization; Glutamine; Heme; Hemeproteins; Hemoglobins; Hydrogen Bonding; Hydrogen Sulfide; Hydrogen-Ion Concentration; Ligands; Oxygen; Oxyhemoglobins; Protein Conformation; Tyrosine | 2020 |
Proton-Coupled Electron Transport in Two Distinct CYBASC Paralogs of
Topics: Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Cytochrome b Group; Electron Transport; Heme; Lysine; Sequence Alignment; Tyrosine | 2020 |
Structural Insights into the Interaction of Heme with Protein Tyrosine Kinase JAK2*.
Topics: Heme; Humans; Janus Kinase 2; Leukemia, Myeloid; Phosphorylation; Protein Conformation; Signal Transduction; Tumor Cells, Cultured; Tyrosine | 2021 |
Fluoride binding to characteristic heme-pocket centers: Insights into ligand stability.
Topics: Animals; Bivalvia; Cyanides; Fluorides; Heme; Hemoglobins; Horses; Hydrogen Bonding; Hydrogen Sulfide; Hydrogen-Ion Concentration; Ligands; Myoglobin; Oxygen; Tyrosine | 2021 |
Tryptophan Can Promote Oxygen Reduction to Water in a Biosynthetic Model of Heme Copper Oxidases.
Topics: Heme; Hydrogen Peroxide; Oxidation-Reduction; Oxidoreductases; Oxygen; Tryptophan; Tyrosine; Water | 2023 |
Tryptophan-96 in cytochrome P450 BM3 plays a key role in enzyme survival.
Topics: Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Heme; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Tryptophan; Tyrosine | 2023 |
Structural and spectroscopic characterization of RufO indicates a new biological role in rufomycin biosynthesis.
Topics: Actinobacteria; Amino Acids; Cytochrome P-450 Enzyme System; Heme; Molecular Docking Simulation; Nitrates; Oligopeptides; Tyrosine | 2023 |
Peroxidase activity of rice (Oryza sativa) hemoglobin: distinct role of tyrosines 112 and 151.
Topics: Antioxidants; Guaiacol; Heme; Hemoglobins; Hydrogen Peroxide; Oryza; Peroxidases; Tyrosine | 2023 |
In Situ Structural Observation of a Substrate- and Peroxide-Bound High-Spin Ferric-Hydroperoxo Intermediate in the P450 Enzyme CYP121.
Topics: Carbon; Cytochrome P-450 Enzyme System; Heme; Iron; Ligands; Peracetic Acid; Peroxides; Tyrosine | 2023 |