heme has been researched along with cytochrome c-t in 498 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 35 (7.03) | 18.7374 |
| 1990's | 30 (6.02) | 18.2507 |
| 2000's | 173 (34.74) | 29.6817 |
| 2010's | 215 (43.17) | 24.3611 |
| 2020's | 45 (9.04) | 2.80 |
| Authors | Studies |
|---|---|
| Berghuis, AM; Brayer, GD | 1 |
| Di Bello, C; Gozzini, L; Vita, C | 1 |
| Brayer, GD; Murphy, ME; Nall, BT | 1 |
| Boyd, J; Gao, Y; Pielak, GJ; Williams, RJ | 1 |
| DiBello, C; Gozzini, L; Taniuchi, H | 1 |
| Davies, AM; Greenwood, C; Guillemette, JG; Mauk, AG; Moore, GR; Smith, M; Thurgood, AG | 1 |
| Arutiunian, AM; Dudchenko, AM; Evstigneeva, RP; Kulish, MA; Luk'ianova, LD; Lysko, AI; Mironov, AF; Zhuravleva, DV | 1 |
| Brayer, GD; Louie, GV | 2 |
| Bosshard, HR; Corradin, G; Saad, B | 1 |
| Moench, SJ; Satterlee, JD | 1 |
| Neupert, W; Nicholson, DW | 1 |
| Juillerat, MA; Taniuchi, H | 1 |
| Guarente, L; Pfeifer, K; Prezant, T | 1 |
| Brayer, GD; Hutcheon, WL; Louie, GV | 1 |
| Das, G; Hampsey, DM; Sherman, F | 1 |
| De Kruijff, B; Jordi, W; Zhou, LX | 1 |
| Cusanovich, MA; Das, G; Hazzard, JT; McLendon, G; Sherman, F; Tollin, G | 1 |
| Adam, G; Hartig, A; Mattes, E; Ruis, H; Schanz, M; Winkler, H | 1 |
| Dumont, ME; Ernst, JF; Sherman, F | 1 |
| Brayer, GD; Louie, GV; Pielak, GJ; Smith, M | 1 |
| Blázovits, A; Horváth, I; Kittel, A; Marton, A; Végh, M; Venekei, I; Vodnyánszky, L | 1 |
| Arif Kazmi, S; Mills, MA; Pitluk, ZW; Scott, RA | 1 |
| Arcangioli, B; Lescure, B | 1 |
| Kuramitsu, S; Matsubara, H; Miyazaki, T; Mukai, K; Wakabayashi, S | 1 |
| Bandlow, W; Magdolen, V; Oechsner, U; Schmalix, W | 1 |
| Enosawa, S; Ohashi, A | 2 |
| Laz, TM; Pietras, DF; Sherman, F | 1 |
| Basile, G; Di Bello, C; Taniuchi, H | 1 |
| Matner, RR; Sherman, F | 1 |
| Ammerer, G; Bilinski, T; Hamilton, B; Hartter, E; Hörtner, H; Ruis, H; Rytka, J | 1 |
| Nall, BT | 1 |
| Basile, G; Taniuchi, H; Taniuchi, M; Veloso, D | 1 |
| Alani, E; Gifford, P; Guarente, L; Lalonde, B | 1 |
| Juillerat, M; Taniuchi, H; Veloso, D | 1 |
| Banci, L; Bertini, I; Bren, KL; Gray, HB; Sompornpisut, P; Turano, P | 1 |
| Fetrow, JS; Fumo, G; Spitzer, JS | 1 |
| Barker, PD; Brayer, GD; Eltis, LD; Guillemette, JG; Lo, TP; Mauk, AG; Smith, M | 1 |
| Campbell, GA; Corin, AF; Dumont, ME | 1 |
| Bakker, G; Komar-Panicucci, S; McLendon, G; Qiao, T; Sherman, F; Weis, D | 1 |
| Heibel, G; Hildebrandt, P; Mauk, AG; Vanhecke, F | 1 |
| Bren, KL; Casimiro, DR; Gray, HB; Lu, Y; Richards, JH | 1 |
| Barker, PD; Eltis, LD; Guillemette, JG; Inglis, SC; Mauk, AG; Miller, CM; Northrup, SH; Thomasson, KA | 1 |
| Buse, G; Hildebrandt, P; Mauk, AG; Soulimane, T; Vanhecke, F | 1 |
| Ferguson, SJ; Norris, HAC; Page, MD; Pearce, DA | 1 |
| Erman, JE; Satterlee, JD; Sukits, SF | 1 |
| Künzler, P; Thöny-Meyer, L | 1 |
| Brennan, L; Turner, DL | 1 |
| Banci, L; Gori-Savellini, G; Turano, P | 1 |
| Hennecke, H; Schulz, H; Thöny-Meyer, L | 1 |
| Matsuura, K; Miki, K; Nagashima, KV; Osyczka, A; Shimada, K; Sogabe, S; Yoshida, M | 1 |
| Bonnard, G; Goldman, B; Kranz, R; Lill, R; Merchant, S | 1 |
| Appia-Ayme, C; Bengrine, A; Bonnefoy, V; Bruschi, M; Cavazza, C; Chippaux, M; Giudici-Orticoni, MT | 1 |
| Buse, G; Gerscher, S; Hildebrandt, P; Soulimane, T | 1 |
| Silkstone, G; Stanway, G; Wilson, MT | 1 |
| Djavadi-Ohaniance, L; Goldberg, ME; Guillou, Y; Schaeffer, F | 1 |
| Dawson, JH; Lu, Y; Pond, AE; Sigman, JA | 1 |
| Bowler, BE; Godbole, S; Hammack, B | 1 |
| Mauk, AG; Vazquez-Duhalt, R; Villegas, JA | 1 |
| Nall, BT; Pierce, MM | 1 |
| Döpner, S; Harris, TR; Hildebrand, DP; Hildebrandt, P; Mauk, AG; Rosell, FI | 1 |
| Thöny-Meyer, L | 2 |
| Engel, BJ; McLuckey, SA; Pan, P; Reid, GE; Wells, JM | 1 |
| Bowler, BE; Hammack, BN; Smith, CR | 1 |
| Ahuja, U; Ren, Q; Thöny-Meyer, L | 1 |
| Guillemette, JG; Lett, CM | 1 |
| Bai, Z; Qian, C; Tang, W; Wang, J; Yao, Y; Ye, K | 1 |
| Allen, JW; Ferguson, SJ; Hong, L; Tomlinson, EJ | 1 |
| Mauk, AG; Rosell, FI | 1 |
| Daltrop, O; Ferguson, SJ | 1 |
| Bowler, BE; Smith, CR; Wandschneider, E | 1 |
| Daltrop, O; Ferguson, SJ; Higham, CW; Stevens, JM | 1 |
| Feissner, R; Kranz, RG; Xiang, Y | 1 |
| Baptista, AM; Bento, I; Carrondo, MA; Matias, PM; Soares, CM; Teixeira, VH | 1 |
| Tang, W; Yao, Y | 1 |
| Atalick, S; Braun, M; Brettreich, M; Burghardt, S; Guldi, DM; Hatzimarinaki, M; Hirsch, A; Lanig, H; Prato, M; Ravanelli, E; van Eldik, R | 1 |
| Englander, SW; Liu, W; Rumbley, J; Wand, AJ | 1 |
| Bu, L; Straub, JE | 1 |
| Knapp, EW; Voigt, P | 1 |
| FROHWIRT, N; MARGOLIASH, E; WIENER, E | 1 |
| HARBURY, HA; LOACH, PA | 2 |
| GEORGE, P; SCHEJTER, A | 1 |
| KING, TE; TAKEMORI, S | 1 |
| GEORGE, P; HANANIA, GI | 1 |
| Cristian, L; Farid, RS; Piotrowiak, P | 1 |
| Bernard, DG; Dujardin, G; Gabilly, ST; Hamel, PP; Merchant, S | 1 |
| Didik, J; Gebicka, L | 1 |
| Ahuja, U; Thöny-Meyer, L | 3 |
| Bominaar, EL; Hill, BC; Pearce, LL; Peterson, J | 1 |
| Allen, JW; Barker, PD; Ferguson, SJ | 1 |
| Kawachi, R; Kume, T; Nagasawa, N; Nishio, T; Oku, T; Satoh, T; Suruga, K; Yamada, S | 1 |
| Baysse, C; Cornelis, P; Jahn, D; Layer, G; Matthijs, S; Schobert, M | 1 |
| Bondon, A; Chevance, S; de Certaines, JD; Le Rumeur, E; Simonneaux, G | 1 |
| Hirota, S; Suzuki, M; Watanabe, Y | 1 |
| Balogh, G; Cinege, G; Dusha, I; Kereszt, A; Kertész, S | 1 |
| Covian, R; Gutierrez-Cirlos, EB; Trumpower, BL | 1 |
| Benson, DR; Cowley, AB; Lukat-Rodgers, GS; Rodgers, KR | 1 |
| Daldal, F; Dutton, PL; Moser, CC; Osyczka, A | 1 |
| Di Mascio, P; Dyszy, FH; Nantes, IL; Nascimento, OR; Prado, FM; Rinaldi, TA; Tersariol, IL | 1 |
| Lukowska, E; Mahy, JP; Pezzotti, F; Ricoux, R | 1 |
| Bartunik, H; Bourenkov, G; Dias J, JM; Moura, I; Romão, MJ; Santos-Silva, T | 1 |
| Cusanovich, MA; de Smet, L; Frishman, D; Meyer, TE; Nealson, KH; Tsapin, AI; van Beeumen, JJ; Vandenberghe, I | 1 |
| Bowler, BE; Wandschneider, E | 1 |
| Aubier, M; Boczkowski, J; Dang, MC; El-Benna, J; Lanone, S; Ogier-Denis, E; Taillé, C | 1 |
| Acker, H; Berchner-Pfannschmidt, U; Bunn, HF; Cross, AR; Fandrey, J; Jackson, TA; Ladoux, A; Larade, K; Lukat-Rodgers, GS; Rodgers, KR; Xie, J; Zhu, H | 1 |
| Allen, JW; Cartron, ML; Ferguson, SJ; Richardson, DJ; Zajicek, RS | 1 |
| Fiorucci, L; Santoni, E; Santucci, R; Scatragli, S; Sinibaldi, F; Smulevich, G | 1 |
| Berka, V; Palmer, G; Tsai, AL; Wu, G; Yeh, HC | 1 |
| Ye, W; Zhang, L | 1 |
| DeMay, BS; Gao, YT; Jones, RJ; Mann, KJ; Salerno, JC; Salerno, KM; Smith, SM | 1 |
| Autenrieth, F; Baudry, J; Luthey-Schulten, Z; Tajkhorshid, E | 1 |
| Dohmae, N; Iizuka, T; Ishida, M; Isogai, Y; Oku, T; Shiro, Y | 1 |
| Burlat, B; Clarke, TA; Cole, JA; Dennison, V; Hemmings, AM; Richardson, DJ; Seward, HE | 1 |
| Braun, M; Thöny-Meyer, L | 1 |
| Ciaccio, C; Coletta, M; De Sanctis, G; Fasciglione, GF; Fiorucci, L; Gioia, M; Marini, S; Santucci, R; Sinibaldi, F | 1 |
| Hagen, SJ; Pabit, SA; Roder, H | 1 |
| Anderson, VE; Nukuna, BN; Sun, G | 1 |
| Daltrop, O; Ferguson, SJ; Harvat, EM; Hong, L; Kitagawa, T; Stevens, JM; Uchida, T | 1 |
| Cianetti, S; Kruglik, SG; Martin, JL; Négrerie, M; Vos, MH | 2 |
| Rousseau, DL; Yeh, SR; Zhong, S | 1 |
| Brown, SJ; Deng, Y; He, T; Huang, Y; Vanka, P; Wu, Y; Yang, G; Yao, H | 1 |
| Allen, JW; Daltrop, O; Ferguson, SJ; Stevens, JM | 1 |
| Hooker, BS; Lin, JT; Markillie, LM; Shi, L; Squier, TC | 1 |
| Hu, Z; Lelli, KM; Maines, MD; Miralem, T; Torno, MD | 1 |
| Brandolin, G; Dahout-Gonzalez, C; Dassa, EP; Dianoux, AC | 1 |
| Burkitt, M; Jones, C; Lawrence, A; Wardman, P | 1 |
| Brochsztain, S; Campos, IB; Figueiredo, KM; Marcon, RO; Nantes, IL | 1 |
| Allen, JW; Ferguson, SJ; Leach, N | 1 |
| E Ferapontova, E; Gorton, L | 1 |
| Friedrich, J; Reif, M; Scharnagl, C | 1 |
| Braun, M; Rubio, IG; Thöny-Meyer, L | 1 |
| Hoffman, BM; Lu, Y; Nocek, JM; Pfister, TD; Seifert, JL | 1 |
| Faraone-Mennella, J; Gray, HB; Winkler, JR | 1 |
| Igarashi, K; Matsumura, H; Nakamura, N; Nishino, T; Ohno, H; Samejima, M; Yoshida, M | 1 |
| Fujii, J; Ohba, Y; Sato, K; Suto, D; Yoshimura, T | 1 |
| Daltrop, O; Ferguson, SJ; Stevens, JM; Uchida, T | 1 |
| Weinkam, P; Wolynes, PG; Zong, C | 1 |
| Ferguson, SJ; Harvat, EM; Redfield, C; Stevens, JM | 2 |
| Battistuzzi, G; Bellei, M; Borsari, M; Di Rocco, G; Ranieri, A; Sola, M | 1 |
| Brecht, K; Heim, J; Simonen, M | 1 |
| Bhattacharya, J; Dasgupta, AK; Ghoshmoulick, R; Roy, S; Singha, S | 1 |
| Domanov, YA; Gorbenko, GP; Molotkovsky, JG | 1 |
| Bernard, DG; Guiard, B; Hamel, PP; Merchant, S; Quevillon-Cheruel, S | 1 |
| Bhambhani, A; Cheng, W; Duff, MR; Kumar, CV; McLendon, GL; Tan, WB; Webber, A | 1 |
| Cirpus, IE; de Been, M; den Camp, HJ; Jetten, MS; Kuenen, GJ; Le Paslier, D; Strous, M | 1 |
| Buckpitt, AR; Cortopassi, GA; Lonnerdal, B; Morin, D; Napoli, E; Puccio, H; Reutenauer, L; Ristow, M; Schoenfeld, RA; Taroni, F; Wong, A; Zhan, S | 1 |
| Bren, KL; Elliott, SJ; Kaur, R; Wen, X; Ye, T | 1 |
| Bokoch, MP; Perroud, TD; Zare, RN | 1 |
| Pradeep, T; Tom, RT | 1 |
| Gray, HB; Pletneva, EV; Winkler, JR | 1 |
| Ishimori, K; Kimura, T; Morishima, I; Sakamoto, K | 1 |
| Blizzard, ER; Feinberg, BA; Margoliash, E; Ryan, MD; Schejter, A; Zhang, C | 1 |
| Kagan, VE; Kapralov, AA; Kurnikov, IV; Osipov, AN; Potapovich, MV; Stoyanovsky, DA; Tyurin, VA; Vlasova, II | 1 |
| Mendes, SB; Runge, AF; Saavedra, SS | 1 |
| Carlsson, CF; Cho, BM; Jimenez, R | 1 |
| Daldal, F; Sanders, C; Turkarslan, S | 1 |
| Ball, EG; Spiro, MJ | 1 |
| Dawson, PE; Matsuda, S; Romesberg, FE; Sagle, LB; Zimmermann, J | 1 |
| Bhuyan, AK; Prabhu, NP; Rao, DK | 1 |
| Droghetti, E; Hildebrandt, P; Oellerich, S; Smulevich, G | 1 |
| Hiraishi, K; Kubo, Y; Sagara, T | 1 |
| Didonato, RJ; Ding, YH; Haveman, SA; Holmes, DE; Lovley, DR; Ward, JE | 1 |
| Cortopassi, G; Lu, C | 1 |
| Dragomir, I; Hagarman, A; Schweitzer-Stenner, R; Wallace, C | 1 |
| Goto, M; Kamiya, N; Naganawa, H; Naruta, Y; Shimojo, K; Tani, F | 1 |
| Jasaitis, A; Silkstone, G; Vos, MH; Wilson, MT | 1 |
| Archer, M; Oliveira, TF; Pereira, IA; Rodrigues, ML | 1 |
| Boscherini, F; Cordone, L; Francia, F; Giachini, L; Venturoli, G | 1 |
| Benson, DR; Cowley, AB | 1 |
| de Groot, MT; Evers, TH; Koper, MT; Merkx, M | 1 |
| Balakrishnan, G; Groves, JT; Hu, Y; Oyerinde, OF; Spiro, TG; Su, J | 1 |
| Banci, L; Furlan, S; Mealli, C; Penna, GL | 1 |
| Bren, KL; Patel, KM; Russell, BS; Wen, X | 1 |
| Hill, RT; Lyon, JL; Shear, JB; Stevenson, KJ | 1 |
| Akutsu, H; Takayama, Y | 1 |
| Christensen, O; Ferguson, SJ; Harvat, EM; Stevens, JM; Thöny-Meyer, L | 1 |
| Beeghley, CA; Graf, CB; Liang, Q; Miller, GT; Timkovich, R | 1 |
| Chaturvedi, S; Driscoll, WJ; Mueller, GP | 1 |
| Clarke, TA; Hartshorne, RS; Karas, M; Kern, M; Meyer, B; Richardson, DJ; Simon, J | 1 |
| Hagarman, A; Huang, Q; Laberge, M; Schweitzer-Stenner, R; Wallace, CJ | 1 |
| Clarke, TA; Cole, JA; Hemmings, AM; Richardson, DJ | 1 |
| Driscoll, WJ; Mueller, GP | 1 |
| Bruix, M; Londer, YY; Morgado, L; Pokkuluri, PR; Salgueiro, CA; Schiffer, M | 1 |
| Bowler, BE; Kurchan, E; Tzul, FO | 1 |
| Borloo, J; Brigé, A; De Smet, L; Devreese, B; Motte, B; Van Beeumen, J; Vergauwen, B | 1 |
| Black, KM; Wallace, CJ | 1 |
| Baddam, S; Bandi, S; Bowler, BE | 1 |
| Hickman, MJ; Winston, F | 1 |
| Coopersmith, CM; Courtois, MR; Deutschman, CS; Gruber, PJ; Levy, RJ; Piel, DA; Robertson, CM; Weinheimer, CJ | 1 |
| Kawano, S; Tai, H; Yamamoto, Y | 1 |
| Abel, CJ; Chen, E; Goldbeck, RA; Kliger, DS | 1 |
| Gurel, E; Mandaci, S; Ozturk, M; Watmough, NJ | 1 |
| Basova, LV; Bayir, H; Belikova, NA; Jiang, J; Kagan, VE; Kapralov, AA; Kurnikov, IV; Tyurin, VA; Tyurina, YY; Vladimirov, YA; Vlasova, II; Zhao, Q | 1 |
| Bonnard, G; Giegé, P; Grienenberger, JM | 1 |
| Borgia, A; Brunori, M; Gianni, S; Travaglini-Allocatelli, C | 1 |
| Antalík, M; Varhac, R | 1 |
| Ghourchian, H; Mogharrab, N; Shafiey, H | 1 |
| Covian, R; Rotsaert, FA; Trumpower, BL | 1 |
| Allen, JW; Ferguson, SJ; Ginger, ML; Jackson, AP; Rigden, DJ; Willis, AC | 1 |
| Deutschman, CS; Levy, RJ; Piel, DA | 1 |
| Einsle, O; Kern, M; Simon, J | 1 |
| Battistoni, A; de Rosny, E; Desbois, A; Kiger, L; Lechauve, C; Liebl, U; Marden, MC; Pilet, E; Vos, MH | 1 |
| Bandi, S; Bowler, BE | 2 |
| de Vitry, C; Ephritikhine, G; Kuras, R; Lezhneva, L | 1 |
| Bonnard, G; Corvest, V; Giegé, P; Hamel, P | 1 |
| Schweitzer-Stenner, R | 2 |
| Daldal, F; Kranz, RG; Lee, DW; Onder, O; Sanders, C; Turkarslan, S | 1 |
| Berenguer, J; Cava, F; Zafra, O | 1 |
| Rurek, M | 1 |
| Breuker, K; Elber, R; Gerber, RB; McLafferty, FW; Steinberg, MZ | 1 |
| Archer, M; Gomes, CM; Hjorleifsdottir, S; Hreggvidsson, GO; Melo, AM; Pereira, MM; Saraiva, LM; Stelter, M; Teixeira, M | 1 |
| Almeida, CC; Carita, JN; Lobo, SA; Saraiva, LM; Teixeira, M | 1 |
| Brennan, L; Chapman, SK; Paixão, VB; Reid, GA; Salgueiro, CA; Turner, DL | 1 |
| Hasegawa, J; Kobayashi, Y; Nakamura, S; Sambongi, Y; Sonoyama, T; Uchiyama, S | 1 |
| Abriata, LA; Cassina, A; Castro, L; Marín, M; Radi, R; Souza, JM; Tórtora, V; Vila, AJ | 1 |
| Gunner, MR; Zheng, Z | 1 |
| Braun, M; Ferguson, SJ; Mavridou, DA; Stevens, JM; Thöny-Meyer, L | 1 |
| Munegumi, T; Tai, H; Yamamoto, Y | 1 |
| Allen, JW; Barker, PD; Ferguson, SJ; Ginger, ML; Sawyer, EB | 1 |
| Bowler, BE; Kurchan, E; Roder, H; Tzul, FO | 1 |
| Guo, L; Link, JJ; Stevens, JA; Wang, L; Zang, C; Zhong, D | 1 |
| Allegrozzi, M; Lisdat, F; Möhwald, H; Turano, P; Wegerich, F | 1 |
| Collman, JP; Decréau, RA; Dey, A; Ghosh, S; Yang, Y | 1 |
| Chen, E; Goldbeck, RA; Kliger, DS | 1 |
| Merchant, SS | 1 |
| Fabián, M; Sedlák, E; Tomásková, N; Varhac, R | 1 |
| Barros, MP; Bechara, EJ; Dyszy, FH; Faria, PA; Mano, CM; Nantes, IL; Nascimento, OR; Prieto, T | 1 |
| Bonner, ER; Frawley, ER; Kranz, RG; Richard-Fogal, CL; San Francisco, B; Zhu, H | 1 |
| Hagarman, A; Kohli, A; Schweitzer-Stenner, R; Verbaro, D | 1 |
| Ahuja, U; Hederstedt, L; Kjelgaard, P; Schulz, BL; Thöny-Meyer, L | 1 |
| Fan, C; He, S; Huang, Q; Li, D; Peng, C; Song, S; Zuo, X | 1 |
| Bhuyan, AK | 2 |
| Duke, NE; Erickson, J; Johnson, G; Londer, YY; Orshonsky, V; Pokkuluri, PR; Schiffer, M; Yang, X | 1 |
| De Biase, PM; Doctorovich, F; Estrin, DA; Hildebrandt, P; Marti, MA; Murgida, DH; Paggi, DA | 1 |
| Hain, A; Hamza, I; Hausmann, A; Ihrig, J; Lill, R; Mühlenhoff, U; Richter, N | 1 |
| Allen, JW; Ferguson, SJ; Goddard, AD; Nomerotskaia, E; Rondelet, A; Stevens, JM | 1 |
| Battistuzzi, G; Borsari, M; Bortolotti, CA; Casalini, S; Di Rocco, G; Ranieri, A; Sola, M | 1 |
| Azai, C; Higuchi, M; Hirano, Y; Miki, K; Oh-Oka, H; Wang, ZY | 1 |
| Bonnard, G; Corvest, V; Hamel, PP; Meyer, EH | 1 |
| Khoroshyy, P; Rákhely, G; Tenger, K; Zimányi, L | 1 |
| Allen, JW; Barker, PD; Ferguson, SJ; Sawyer, EB; Stephens, E | 1 |
| Chandran, K; Liang, HL; Mortensen, J; Nilakantan, V; Rajesh, S | 1 |
| Daldal, F; Lee, DW; Sanders, C; Turkarslan, S | 1 |
| Husu, I; Kapetanaki, SM; Silkstone, G; Vos, MH; Wilson, MT | 1 |
| Ciampi, S; Gooding, JJ | 1 |
| Inoue, K; Izallalen, M; Kim, BC; Lovley, DR; Mester, T; Morgado, L; Qian, X; Salgueiro, CA | 1 |
| Allen, JW; Chan, W; Ferguson, SJ; Goddard, AD; Mavridou, DA; Rao, F; Richardson, DJ; Stevens, JM | 1 |
| Bowler, BE; Tzul, FO | 1 |
| Ankner, JF; Droubay, T; Johs, A; Liang, L; Shi, L | 1 |
| Bren, KL; Liptak, MD; Wen, X | 1 |
| Kranz, RG; Richard-Fogal, C | 1 |
| Corvest, V; Dreyfuss, BW; Gabilly, ST; Hamel, PP; Karamoko, M; Kropat, J; Merchant, SS; Page, MD | 1 |
| Bowman, SE; Bren, KL | 1 |
| Bernard, DG; Corvest, V; Guiard, B; Hamel, PP; Knaff, DB; Murrey, DA | 1 |
| Dahl, C; Grein, F; Hildebrandt, P; Pereira, IA; Schneider, L; Todorovic, S; Venceslau, SS | 1 |
| Abel, S; Marchi, M; Waks, M | 1 |
| Sedlák, E; Tomášková, N; Varinská, L | 1 |
| Battistuzzi, G; Borsari, M; Lombardi, A; Monari, S; Nastri, F; Pavone, V; Ranieri, A; Ringhieri, P; Sola, M | 1 |
| Fukumori, Y; Hino, T; Iwata, S; Matsumoto, Y; Murata, T; Nagano, S; Shiro, Y; Sugimoto, H | 1 |
| Nishidate, I; Sato, M; Yoshida, K | 1 |
| Londer, YY | 1 |
| Bischin, C; Cooper, CE; Damian, G; Deac, F; Rajagopal, BS; Silaghi-Dumitrescu, R; Worrall, JA | 1 |
| Duke, NE; Erickson, J; Londer, YY; Orshonsky, L; Orshonsky, V; Pessanha, M; Pokkuluri, PR; Salgueiro, CA; Schiffer, M; Yang, X; Zagyanskiy, Y | 1 |
| Fee, JA; Moënne-Loccoz, P | 1 |
| Kern, M; Simon, J | 1 |
| Bren, KL; Fagerlund, RD; Ledgerwood, EC; Liptak, MD; Wilbanks, SM | 1 |
| Gabilly, ST; Hamel, PP; Karamoko, M; Kropat, J; Merchant, SS; Nakamoto, SS; Page, MD | 1 |
| Kinoshita, M; Kodama, R; Oda, K; Sambongi, Y; Yamanaka, M; Yoshidome, T | 1 |
| Butt, JN; Clarke, TA; Lockwood, C; Richardson, DJ | 1 |
| Bertini, I; Cavallaro, G; Rosato, A | 1 |
| Fang, X; Pletnev, AA; Pletneva, EV; Pound, GJ | 1 |
| Lederer, F | 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 |
| Inoue, H; Nishihara, H; Sambongi, Y; Wakai, S | 1 |
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| Nesterova, AM; Remenshchikov, VE; Vladimirov, GK; Vladimirov, YA; Volkov, VV | 1 |
| Durham, B; Ferguson-Miller, S; Geren, L; Ma, L; Millett, F; Rajagukguk, R; Scharlau, M; Zhen, EY | 1 |
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| Alonso-Mori, R; Bergmann, U; Biasin, E; Chollet, M; Driel, TBV; Gaffney, KJ; Gee, LB; Glownia, JM; Hadt, RG; Hartsock, RW; Hedman, B; Hodgson, KO; Kjaer, KS; Kroll, T; Kunnus, K; Lim, H; Mara, MW; Nelson, S; Reinhard, ME; Sokaras, D; Solomon, EI; Weninger, C | 1 |
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31 review(s) available for heme and cytochrome c-t
| Article | Year |
|---|---|
Yeast iso-1-cytochrome c: genetic analysis of structural requirements.
Topics: Amino Acid Sequence; Base Sequence; Cytochrome c Group; Cytochromes c; Electron Transport; Eukaryotic Cells; Fungal Proteins; Heme; Molecular Sequence Data; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Homology, Nucleic Acid; Structure-Activity Relationship | 1988 |
Molecular mechanisms of cytochrome c biogenesis: three distinct systems.
Topics: Apoproteins; Biological Transport; Cell Membrane; Chloroplasts; Cytochrome c Group; Cytochromes c; Eukaryotic Cells; Evolution, Molecular; Heme; Mitochondria; Oxidation-Reduction; Prokaryotic Cells | 1998 |
Haem-polypeptide interactions during cytochrome c maturation.
Topics: Amino Acid Sequence; Apoproteins; Bacterial Outer Membrane Proteins; Bacterial Proteins; Cyanobacteria; Cytochrome c Group; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Membrane Proteins; Models, Chemical; Models, Molecular; Protein Processing, Post-Translational; Saccharomyces cerevisiae | 2000 |
Cytochrome c maturation: a complex pathway for a simple task?
Topics: Amino Acid Sequence; Apoproteins; Binding Sites; Cytochrome c Group; Cytochromes c; Escherichia coli; Heme; Protein Processing, Post-Translational | 2002 |
C-type cytochrome formation: chemical and biological enigmas.
Topics: Animals; Bacterial Proteins; Cytochromes c; Heme; Mitochondria; Models, Molecular; Molecular Structure | 2004 |
Activation of cytochrome c to a peroxidase compound I-type intermediate by H2O2: relevance to redox signalling in apoptosis.
Topics: Apoptosis; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Activation; Fluoresceins; Heme; Hydrogen Peroxide; Models, Chemical; Oxidation-Reduction; Oxidative Stress; Peroxidase | 2004 |
Covalent cofactor attachment to proteins: cytochrome c biogenesis.
Topics: Binding Sites; Coenzymes; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Proteins | 2005 |
Cytochrome c biogenesis in mitochondria.
Topics: ATP-Binding Cassette Transporters; Bacteria; Cytochromes c; Evolution, Molecular; Genome, Bacterial; Genome, Fungal; Genome, Plant; Heme; Lyases; Mitochondria; Plants | 2008 |
Order within a mosaic distribution of mitochondrial c-type cytochrome biogenesis systems?
Topics: Amino Acid Sequence; Animals; Bacterial Proteins; Computational Biology; Cysteine; Cytochromes c; Cytochromes c1; Eukaryotic Cells; Evolution, Molecular; Heme; Lyases; Mitochondria; Molecular Sequence Data; Molecular Structure; Phylogeny; Plant Proteins | 2008 |
Biochemical requirements for the maturation of mitochondrial c-type cytochromes.
Topics: Animals; Apoproteins; Cytochromes c; Heme; Humans; Mitochondria; Mitochondrial Proteins; Models, Biological; Oxidation-Reduction | 2009 |
Proteins involved in maturation pathways of plant mitochondrial and plastid c-type cytochromes.
Topics: Cytochromes c; Genes, Plant; Heme; Mitochondrial Proteins; Models, Biological; Models, Molecular; Molecular Structure; Oxidation-Reduction; Plant Proteins; Plants; Plastids; Protein Processing, Post-Translational | 2008 |
Probing early events in ferrous cytochrome c folding with time-resolved natural and magnetic circular dichroism spectroscopies.
Topics: Animals; Circular Dichroism; Cytochromes c; Equipment Design; Heme; Humans; Iron; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Time Factors; Ultraviolet Rays | 2009 |
Redox processes controlling the biogenesis of c-type cytochromes.
Topics: Amino Acid Motifs; Animals; Apoproteins; Bacteria; Cytochromes c; Heme; Mitochondria; Mitochondrial Proteins; Oxidation-Reduction; Plants; Plastids; Protein Processing, Post-Translational; Saccharomyces cerevisiae | 2010 |
Cytochrome c biogenesis: the Ccm system.
Topics: Archaea; Archaeal Proteins; Bacteria; Bacterial Outer Membrane Proteins; Bacterial Proteins; Cysteine; Cytochromes c; Heme; Mitochondria; Plant Proteins; Plants; Protein Processing, Post-Translational; Rhodophyta; Sulfides | 2010 |
Expression of recombinant cytochromes c in E. coli.
Topics: Cytochromes c; Enzyme Stability; Escherichia coli; Gene Expression; Heme; Multigene Family; Periplasm; Recombinant Proteins | 2011 |
Another look at the interaction between mitochondrial cytochrome c and flavocytochrome b (2).
Topics: Binding Sites; Catalysis; Cytochrome b Group; Cytochromes b5; Cytochromes c; Electron Transport; Flavin Mononucleotide; Flavins; Heme; Kinetics; Mitochondria; Models, Molecular; NADPH Oxidases; Osmolar Concentration; Oxidation-Reduction; Protein Binding; Protein Structure, Tertiary; Saccharomyces cerevisiae | 2011 |
The role of intramolecular interactions in the functional control of multiheme cytochromes c.
Topics: Bacterial Proteins; Cytochromes c; Electron Transport; Heme; Hydrogen-Ion Concentration; Models, Molecular; Oxidation-Reduction; Protein Conformation; Static Electricity; Thermodynamics | 2012 |
Spectroscopic analysis of protein Fe-NO complexes.
Topics: Animals; Bacterial Proteins; Cytochromes c; Heme; Iron; Myoglobin; Nitric Oxide; Spectrum Analysis; Trans-Activators | 2011 |
Cytochrome c maturation system on the negative side of bioenergetic membranes: CCB or System IV.
Topics: Amino Acid Sequence; Animals; Cell Membrane; Cytochromes c; Energy Metabolism; Heme; Humans; Molecular Sequence Data; Protein Processing, Post-Translational | 2011 |
Composition and function of cytochrome c biogenesis System II.
Topics: Animals; Bacteria; Chloroplasts; Cytochromes c; Heme; Humans | 2011 |
Molecular structure and function of bacterial nitric oxide reductase.
Topics: Bacterial Proteins; Cytochromes c; Glutamic Acid; Heme; Models, Molecular; Oxidoreductases; Protein Binding; Protein Structure, Tertiary; Protein Subunits; Pseudomonas aeruginosa | 2012 |
Physiological function and catalytic versatility of bacterial multihaem cytochromes c involved in nitrogen and sulfur cycling.
Topics: Bacteria; Biocatalysis; Cytochromes c; Heme; Nitrogen; Nitrogen Cycle; Sulfur | 2011 |
Cytochrome c assembly.
Topics: Amino Acid Motifs; Animals; Apoproteins; Biological Transport; Cysteine; Cytochromes c; Heme; Humans; Mitochondria; Models, Molecular; Plants; Protein Biosynthesis; Protein Multimerization; Protein Processing, Post-Translational; Protein Structure, Secondary; Protein Structure, Tertiary | 2013 |
The role of key residues in structure, function, and stability of cytochrome-c.
Topics: Cytochromes c; Electron Transport Chain Complex Proteins; Heme; Protein Isoforms; Protein Structure, Secondary; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 2014 |
Structural transformations of cytochrome c upon interaction with cardiolipin.
Topics: Animals; Cardiolipins; Cell Membrane Permeability; Cytochromes c; Free Radicals; Heme; Humans; Protein Binding | 2014 |
Molecular mechanisms of heme based sensors from sediment organisms capable of extracellular electron transfer.
Topics: Amino Acid Sequence; Bacterial Proteins; Cytochromes c; Electron Transport; Geobacter; Geologic Sediments; Heme; Ligands; Membrane Proteins; Oxidation-Reduction; Protein Conformation; Protein Structure, Tertiary | 2014 |
The production of ammonia by multiheme cytochromes C.
Topics: Ammonia; Cytochromes c; Electron Transport; Environment; Heme; Humans; Oxidoreductases; Protein Structure, Tertiary | 2014 |
Cardiolipin-cytochrome c complex: Switching cytochrome c from an electron-transfer shuttle to a myoglobin- and a peroxidase-like heme-protein.
Topics: Animals; Apoptosis; Cardiolipins; Cytochromes c; Electron Transport; Heme; Humans; Inactivation, Metabolic; Multiprotein Complexes; Myoglobin; Nitrite Reductases; Oxidation-Reduction; Peroxynitrous Acid; Protein Carbonylation | 2015 |
About the use of
Topics: Chemistry, Bioinorganic; Cytochromes c; Ferritins; Heme; Humans; Male; Nuclear Magnetic Resonance, Biomolecular | 2019 |
A brief survey of the "cytochromome".
Topics: Cytochromes c; Heme; Oxidation-Reduction | 2019 |
Heme-Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case.
Topics: Cytochromes c; Electron Transport; Heme; Models, Molecular; Oxidation-Reduction | 2022 |
467 other study(ies) available for heme and cytochrome c-t
| Article | Year |
|---|---|
Oxidation state-dependent conformational changes in cytochrome c.
Topics: Amino Acid Sequence; Crystallography; Cytochrome c Group; Cytochromes c; Heme; Ligands; Models, Molecular; Molecular Sequence Data; Molecular Structure; Oxidation-Reduction; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Water; X-Ray Diffraction | 1992 |
Total synthesis of horse heart cytochrome C.
Topics: Amino Acid Sequence; Animals; Apoproteins; Cytochrome c Group; Cytochromes c; Heme; Horses; Isomerism; Mitochondria, Heart; Molecular Sequence Data; Myocardium; Peptide Fragments; Protein Conformation | 1992 |
Structure determination and analysis of yeast iso-2-cytochrome c and a composite mutant protein.
Topics: Amino Acid Sequence; Cytochrome c Group; Cytochromes c; Electrochemistry; Fungal Proteins; Heme; Hydrogen Bonding; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Conformation; Protein Denaturation; Saccharomyces cerevisiae; Sequence Alignment; Solvents; Structure-Activity Relationship; Water | 1992 |
Proton nuclear magnetic resonance as a probe of differences in structure between the C102T and F82S,C102T variants of iso-1-cytochrome c from the yeast Saccharomyces cerevisiae.
Topics: Amino Acid Sequence; Cytochrome c Group; Cytochromes c; Fungal Proteins; Genetic Variation; Heme; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Protein Conformation; Protons; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; X-Ray Diffraction | 1991 |
Complexation which facilitates rejoining of horse cytochrome c apofragment [Homoser-lactone65](1-65) or [Homoser-lactone65] (23-65) to apofragment (66-104).
Topics: Amino Acids; Animals; Apoproteins; Cyanogen Bromide; Cytochrome c Group; Cytochromes c; Heme; Horses; Peptide Fragments; Spectrophotometry | 1991 |
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 |
[The mechanism of the antioxidant effect of cytochrome C heme nonapeptide].
Topics: Animals; Antioxidants; Catalysis; Cytochrome c Group; Cytochrome P-450 Enzyme System; Cytochromes c; Drug Interactions; Heme; Lipid Peroxides; Microsomes, Liver; NADP; Peptide Fragments; Rats | 1990 |
High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c.
Topics: Crystallization; Cytochrome c Group; Cytochromes c; Heme; Hydrogen Bonding; Molecular Structure; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Solvents; Temperature; X-Ray Diffraction | 1990 |
Monoclonal antibody recognizes a conformational epitope in a random coil protein.
Topics: Animals; Antibodies, Monoclonal; Antigen-Antibody Reactions; Apoproteins; Binding Sites, Antibody; Binding, Competitive; Chromatography, Gel; Cytochrome c Group; Cytochromes c; Epitopes; Heme; Horses; Immunoenzyme Techniques; Peptide Mapping; Peptides; Radioimmunoassay | 1988 |
Proton NMR comparison of the Saccharomyces cerevisiae ferricytochrome c isozyme-1 monomer and covalent disulfide dimer.
Topics: Cytochrome c Group; Cytochromes c; Disulfides; Heme; Macromolecular Substances; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Weight; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1989 |
Import of cytochrome c into mitochondria: reduction of heme, mediated by NADH and flavin nucleotides, is obligatory for its covalent linkage to apocytochrome c.
Topics: Apoproteins; Cytochrome c Group; Cytochromes c; Dithionite; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Lyases; Mitochondria; NAD; Oxidation-Reduction; Saccharomyces cerevisiae | 1989 |
A polypeptide chain-refolding event occurs in the Gly82 variant of yeast iso-1-cytochrome c.
Topics: Amino Acid Sequence; Computer Simulation; Cytochrome c Group; Cytochromes c; Electron Transport; Fungal Proteins; Glycine; Heme; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Structure-Activity Relationship; Water | 1989 |
Intramolecular flip between two alternative forms of complex formed from a heme fragment and apoprotein of horse cytochrome c.
Topics: Animals; Apoproteins; Cytochrome c Group; Cytochromes c; Heme; Horses; Kinetics; Models, Molecular; Myocardium; Peptide Fragments; Protein Binding; Protein Conformation; Thermodynamics | 1987 |
Organization of the regulatory region of the yeast CYC7 gene: multiple factors are involved in regulation.
Topics: Chromosome Mapping; Cytochrome c Group; Cytochromes c; Gene Expression Regulation; Genes, Fungal; Genes, Regulator; Glucose; Heme; Mutation; Regulatory Sequences, Nucleic Acid; Saccharomyces cerevisiae; Transcription Factors | 1987 |
Yeast iso-1-cytochrome c. A 2.8 A resolution three-dimensional structure determination.
Topics: Amino Acid Sequence; Animals; Crystallography; Cytochrome c Group; Cytochromes c; Heme; Molecular Conformation; Molecular Sequence Data; Oryza; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Tuna | 1988 |
Influence of heme and importance of the N-terminal part of the protein and physical state of model membranes for the apocytochrome c-lipid interaction.
Topics: Animals; Apoproteins; Biological Transport; Calorimetry, Differential Scanning; Chemical Phenomena; Chemistry, Physical; Cytochrome c Group; Cytochromes c; Fluoresceins; Gels; Heme; Horses; Membrane Lipids; Models, Biological; Phospholipids; Protein Binding; Structure-Activity Relationship; Thermodynamics | 1988 |
Effects of amino acid replacements in yeast iso-1 cytochrome c on heme accessibility and intracomplex electron transfer in complexes with cytochrome c peroxidase.
Topics: Amino Acids; Computer Graphics; Cytochrome c Group; Cytochrome-c Peroxidase; Cytochromes c; Electron Transport; Heme; Mutation; Peroxidases; Saccharomyces cerevisiae Proteins; Yeasts | 1988 |
Co-ordinate control of synthesis of mitochondrial and non-mitochondrial hemoproteins: a binding site for the HAP1 (CYP1) protein in the UAS region of the yeast catalase T gene (CTT1).
Topics: Base Sequence; Binding Sites; Catalase; Cytochrome c Group; Cytochromes c; DNA-Binding Proteins; Enzyme Induction; Fungal Proteins; Genes, Fungal; Heme; Hemin; Mitochondria; Molecular Sequence Data; Nucleic Acid Conformation; Promoter Regions, Genetic; Recombinant Fusion Proteins; Regulatory Sequences, Nucleic Acid; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1988 |
Coupling of heme attachment to import of cytochrome c into yeast mitochondria. Studies with heme lyase-deficient mitochondria and altered apocytochromes c.
Topics: Apoproteins; Cloning, Molecular; Cytochrome c Group; Cytochromes c; Heme; Lyases; Mitochondria; Plasmids; Protein Biosynthesis; RNA, Messenger; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1988 |
Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this position.
Topics: Cytochrome c Group; Cytochromes c; Electron Transport; Heme; Mutation; Oxidation-Reduction; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Serine | 1988 |
Inhibition of lipid peroxidation by heme-nonapeptide derived from cytochrome c.
Topics: Animals; Brain; Cytochrome c Group; Cytochromes c; Heme; Kinetics; Lipid Peroxides; Microsomes; Microsomes, Liver; NAD; NADP; Oxygen Consumption; Peptide Fragments; Rats; Rats, Inbred Strains | 1985 |
Kinetics of dithionite reduction of the heme nonapeptide of cytochrome c.
Topics: Animals; Cytochrome c Group; Cytochromes c; Dithionite; Heme; Horses; Hydrogen-Ion Concentration; In Vitro Techniques; Kinetics; Myocardium; Osmolar Concentration; Oxidation-Reduction; Peptide Fragments | 1985 |
Identification of proteins involved in the regulation of yeast iso- 1-cytochrome C expression by oxygen.
Topics: Anaerobiosis; Cytochrome c Group; Cytochromes c; DNA-Binding Proteins; DNA, Fungal; Gene Expression Regulation; Heme; Oxygen; Promoter Regions, Genetic; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1985 |
Dissociation of bovine cytochrome c1 subcomplex and the status of cysteine residues in the subunits.
Topics: Amino Acid Sequence; Amino Acids; Animals; Cattle; Chloromercuribenzoates; Cysteine; Cytochrome c Group; Cytochromes c; Cytochromes c1; Electrophoresis, Polyacrylamide Gel; Formates; Heme; Mercury; Oxidation-Reduction; Proteins; Sulfhydryl Compounds | 1985 |
Kinetics of the intracellular availability of heme after supplementing a heme-deficient yeast mutant with 5-aminolevulinate.
Topics: Aminolevulinic Acid; Cytochrome c Group; Cytochromes; Cytochromes c; Cytoplasm; Gene Expression Regulation; Heme; Levulinic Acids; Oxygen Consumption; Protein Processing, Post-Translational; RNA, Messenger; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Time Factors; Transcription, Genetic | 1986 |
Localization of enzyme for heme attachment to apocytochrome c in yeast mitochondria.
Topics: Apoproteins; Cell Fractionation; Cytochrome c Group; Cytochromes c; Heme; Intracellular Membranes; Lyases; Mitochondria; Octoxynol; Polyethylene Glycols; Saccharomyces cerevisiae; Solubility; Transferases; Trypsin | 1986 |
A simple and rapid assay for heme attachment to apocytochrome c.
Topics: Apoproteins; Binding Sites; Cytochrome c Group; Cytochromes c; Heme; Iodine Radioisotopes; Protein Binding; Radioisotope Dilution Technique; Saccharomyces cerevisiae | 1987 |
Differential regulation of the duplicated isocytochrome c genes in yeast.
Topics: Cytochrome c Group; Cytochromes c; Gene Expression Regulation; Glucose; Heme; Mutation; RNA, Messenger; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1984 |
Formation of an iso-1-cytochrome c-like species containing a covalently bonded heme group from the apoprotein by a yeast cell-free system in the presence of hemin.
Topics: Apoproteins; Cell-Free System; Cytochrome c Group; Cytochromes c; Heme; Iodine Radioisotopes; NAD; NADP; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1980 |
Differential accumulation of two apo-iso-cytochromes c in processing mutants of yeast.
Topics: Apoproteins; Cytochrome c Group; Cytochromes c; Electrophoresis, Polyacrylamide Gel; Fluorescent Antibody Technique; Heme; Mutation; Radioimmunoassay; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1982 |
Regulation of synthesis of catalases and iso-1-cytochrome c in Saccharomyces cerevisiae by glucose, oxygen and heme.
Topics: Catalase; Cytochrome c Group; Cytochromes c; Genetic Code; Glucose; Heme; Oxygen; Protein Biosynthesis; RNA, Messenger; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1982 |
Structural intermediates in folding of yeast iso-2 cytochrome c.
Topics: Cytochrome c Group; Cytochromes c; Guanidines; Heme; Kinetics; Protein Conformation; Saccharomyces cerevisiae; Spectrophotometry; Temperature | 1983 |
Evidence for formation of two thioether bonds to link heme to apocytochrome c by partially purified cytochrome c synthetase.
Topics: Cytochrome c Group; Cytochromes c; Heme; Lyases; Octoxynol; Polyethylene Glycols; Saccharomyces cerevisiae; Solubility; Sulfides; Transferases | 1983 |
Distinctly regulated tandem upstream activation sites mediate catabolite repression of the CYC1 gene of S. cerevisiae.
Topics: Cytochrome c Group; Cytochromes c; Genes; Genes, Fungal; Genes, Regulator; Heme; Mutation; Plasmids; Repressor Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Templates, Genetic; Transcription Factors; Transcription, Genetic | 1984 |
Synthesis of a heme fragment of horse cytochrome c which forms a productive complex with a native apofragment.
Topics: Amino Acid Sequence; Animals; Apoproteins; Cytochrome c Group; Cytochromes c; Heme; Horses; Lyases; Mitochondria; Models, Molecular; Peptide Fragments; Protein Binding; Protein Conformation; Saccharomyces cerevisiae; Transferases | 1984 |
Three-dimensional solution structure of the cyanide adduct of a Met80Ala variant of Saccharomyces cerevisiae iso-1-cytochrome c. Identification of ligand-residue interactions in the distal heme cavity.
Topics: Alanine; Amino Acid Sequence; Animals; Crystallography, X-Ray; Cyanides; Cytochrome c Group; Cytochromes c; Heme; Horses; Ligands; Magnetic Resonance Spectroscopy; Methionine; Molecular Sequence Data; Myocardium; Protein Conformation; Protein Structure, Secondary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Solutions | 1995 |
A method of directed random mutagenesis of the yeast chromosome shows that the iso-1-cytochrome c heme ligand His18 is essential.
Topics: Base Sequence; Binding Sites; Chromosomes, Fungal; Cytochrome c Group; Cytochromes c; Heme; Histidine; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Saccharomyces cerevisiae Proteins; Selection, Genetic; Spectrophotometry; Structure-Activity Relationship; Transformation, Genetic; Yeasts | 1995 |
Analysis of the bimolecular reduction of ferricytochrome c by ferrocytochrome b5 through mutagenesis and molecular modelling.
Topics: Amino Acid Sequence; Animals; Cattle; Cytochrome c Group; Cytochromes b5; Cytochromes c; Heme; Kinetics; Liver; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics | 1994 |
Noncovalent binding of heme induces a compact apocytochrome c structure.
Topics: Animals; Apoproteins; Chromatography, Gel; Circular Dichroism; Cytochrome c Group; Cytochromes c; Heme; Horses; Iron; Protein Binding; Protein Conformation; Ribonucleases; Spectrometry, Fluorescence | 1994 |
Thermodynamics of the equilibrium unfolding of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochromes c.
Topics: Base Sequence; Cytochrome c Group; Cytochromes c; DNA, Fungal; Genes, Fungal; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics | 1994 |
Structural changes in cytochrome c upon hydrogen-deuterium exchange.
Topics: Cytochrome c Group; Cytochromes c; Deuterium; Heme; Hydrogen; Hydrogen Bonding; Oxidation-Reduction; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrum Analysis, Raman | 1993 |
Structurally engineered cytochromes with unusual ligand-binding properties: expression of Saccharomyces cerevisiae Met-80-->Ala iso-1-cytochrome c.
Topics: Alanine; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cloning, Molecular; Cytochrome c Group; Cytochromes; Cytochromes c; Escherichia coli; Heme; Horses; Methionine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Conformation; Protein Engineering; Recombinant Proteins; Restriction Mapping; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Transcription, Genetic | 1993 |
Effects of charged amino acid mutations on the bimolecular kinetics of reduction of yeast iso-1-ferricytochrome c by bovine ferrocytochrome b5.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cattle; Cytochrome c Group; Cytochromes b5; Cytochromes c; Heme; Histidine; Kinetics; Liver; Lysine; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1993 |
Resonance Raman study of the interactions between cytochrome c variants and cytochrome c oxidase.
Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; Cattle; Cytochrome c Group; Cytochromes c; Electron Transport Complex IV; Heme; Horses; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrum Analysis, Raman | 1993 |
The Paracoccus denitrificans ccmA, B and C genes: cloning and sequencing, and analysis of the potential of their products to form a haem or apo- c-type cytochrome transporter.
Topics: Amino Acid Sequence; Apoproteins; ATP-Binding Cassette Transporters; Biological Transport; Cloning, Molecular; Cytochrome c Group; Cytochromes; Cytochromes c; Genes, Bacterial; Heme; Molecular Sequence Data; Mutagenesis, Insertional; Nitrite Reductases; Paracoccus denitrificans; Recombinant Fusion Proteins; Sequence Analysis, DNA; Sequence Homology, Amino Acid | 1997 |
Proton NMR assignments and magnetic axes orientations for wild-type yeast iso-1-ferricytochrome c free in solution and bound to cytochrome c peroxidase.
Topics: Binding Sites; Cytochrome c Group; Cytochrome-c Peroxidase; Cytochromes c; Heme; Magnetic Resonance Spectroscopy; Models, Chemical; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Solutions | 1997 |
Translocation to the periplasm and signal sequence cleavage of preapocytochrome c depend on sec and lep, but not on the ccm gene products.
Topics: Apoproteins; ATP-Binding Cassette Transporters; Cytochrome c Group; Cytochromes c; Cytoplasm; DNA-Binding Proteins; Drosophila Proteins; Escherichia coli; Heme; Intracellular Membranes; Membrane Proteins; Protein Processing, Post-Translational; Protein Sorting Signals; Serine Endopeptidases; Transcription Factors; Translocation, Genetic | 1997 |
Paramagnetic NMR shifts in cyanoferricytochrome c. Investigation of thermal stability and deviations from Curie law behaviour.
Topics: Cytochrome c Group; Cytochromes c; Drug Stability; Electron Spin Resonance Spectroscopy; Heme; Kinetics; Models, Chemical; Nuclear Magnetic Resonance, Biomolecular; Thermodynamics | 1997 |
A molecular dynamics study in explicit water of the reduced and oxidized forms of yeast iso-1-cytochrome c--solvation and dynamic properties of the two oxidation states.
Topics: Computer Simulation; Crystallography, X-Ray; Cytochrome c Group; Cytochromes c; Fungal Proteins; Heme; Hydrogen Bonding; Iron; Magnetic Resonance Spectroscopy; Models, Molecular; Oxidation-Reduction; Protein Conformation; Protein Structure, Tertiary; Saccharomyces cerevisiae Proteins; Software; Solubility; Water | 1997 |
Prototype of a heme chaperone essential for cytochrome c maturation.
Topics: Amino Acid Sequence; Apoproteins; Bacterial Proteins; Binding Sites; Cytochrome c Group; Cytochromes c; Escherichia coli; Heme; Histidine; Mass Spectrometry; Membrane Proteins; Molecular Chaperones; Recombinant Fusion Proteins | 1998 |
Interaction site for soluble cytochromes on the tetraheme cytochrome subunit bound to the bacterial photosynthetic reaction center mapped by site-directed mutagenesis.
Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Cytochromes; Cytochromes c; Electron Transport; Glutamic Acid; Heme; Light-Harvesting Protein Complexes; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Photosynthetic Reaction Center Complex Proteins; Protein Binding; Rhodospirillaceae; Solubility; Spectrophotometry; Static Electricity | 1998 |
Characterization and expression of the co-transcribed cyc1 and cyc2 genes encoding the cytochrome c4 (c552) and a high-molecular-mass cytochrome c from Thiobacillus ferrooxidans ATCC 33020.
Topics: Amino Acid Sequence; Base Sequence; Cloning, Molecular; Cytochrome c Group; Cytochromes c; DNA, Bacterial; Electron Transport; Genes, Bacterial; Heme; Kinetics; Molecular Sequence Data; Open Reading Frames; Oxidation-Reduction; Periplasm; Reverse Transcriptase Polymerase Chain Reaction; RNA, Bacterial; Saccharomyces cerevisiae Proteins; Thiobacillus; Transcription, Genetic | 1998 |
Resonance Raman spectroscopic study of the caa3 oxidase from Thermus thermophilus.
Topics: Cytochrome c Group; Cytochromes c; Electron Transport Complex IV; Heme; Oxidation-Reduction; Protein Conformation; Saccharomyces cerevisiae Proteins; Spectrum Analysis, Raman; Thermus thermophilus | 1998 |
Yeast iso-1-cytochrome c met80X mutants: the pKa of the spin state transition as a probe for haem pocket flexibility.
Topics: Cytochrome c Group; Cytochromes c; Heme; Hydrogen-Ion Concentration; Methionine; Molecular Probes; Mutation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1998 |
Pseudo-native motifs in the noncovalent heme-apocytochrome c complex. Evidence from antibody binding studies by enzyme-linked immunosorbent assay and microcalorimetry.
Topics: Animals; Antibodies, Monoclonal; Apoproteins; Calorimetry; Cattle; Circular Dichroism; Cytochrome c Group; Cytochromes c; Enzyme-Linked Immunosorbent Assay; Heme; Horses; Ligands; Macromolecular Substances; Mice; Mice, Inbred BALB C; Protein Conformation; Protein Folding; Spectrophotometry, Ultraviolet | 1999 |
Engineering cytochrome c peroxidase into cytochrome P450: a proximal effect on heme-thiolate ligation.
Topics: Aspartic Acid; Circular Dichroism; Cysteine; Cytochrome c Group; Cytochrome P-450 Enzyme System; Cytochrome-c Peroxidase; Cytochromes c; Electron Spin Resonance Spectroscopy; Escherichia coli; Ferric Compounds; Heme; Histidine; Imidazoles; Leucine; Ligands; Mutagenesis, Site-Directed; Protein Engineering; Spectrophotometry, Ultraviolet | 1999 |
Measuring denatured state energetics: deviations from random coil behavior and implications for the folding of iso-1-cytochrome c.
Topics: Binding, Competitive; Biopolymers; Circular Dichroism; Cytochrome c Group; Cytochromes c; Enzyme Stability; Genetic Variation; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Models, Chemical; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics; Titrimetry | 2000 |
A cytochrome c variant resistant to heme degradation by hydrogen peroxide.
Topics: Cytochrome c Group; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Enzyme Stability; Heme; Hydrogen Peroxide; Kinetics; Mutagenesis, Site-Directed; Saccharomyces cerevisiae Proteins; Spectrophotometry; Yeasts | 2000 |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization.
Topics: Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cytochrome c Group; Cytochromes c; Enzyme Stability; Fluorescence; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Proline; Protein Conformation; Protein Denaturation; Protein Folding; Protein Renaturation; Saccharomyces cerevisiae; Sequence Alignment; Thermodynamics | 2000 |
Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c.
Topics: Amino Acid Substitution; Cytochrome c Group; Cytochromes c; Electrochemistry; Electron Spin Resonance Spectroscopy; Enzyme Stability; Fungal Proteins; Heme; Hydrogen-Ion Concentration; Iron; Kinetics; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Phenylalanine; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrum Analysis, Raman; Structure-Activity Relationship; Tryptophan | 2000 |
Dissociation reactions of gaseous ferro-, ferri-, and apo-cytochrome c ions.
Topics: Apoproteins; Cytochrome c Group; Cytochromes c; Electrochemistry; Heme; Oxidation-Reduction | 2001 |
Denatured state thermodynamics: residual structure, chain stiffness and scaling factors.
Topics: Acetylation; Circular Dichroism; Cytochrome c Group; Cytochromes c; Enzyme Stability; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Mutation; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae Proteins; Serine Endopeptidases; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Thermodynamics; Titrimetry; Yeasts | 2001 |
A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c.
Topics: Amino Acid Motifs; Amino Acid Sequence; Apoproteins; Bacterial Outer Membrane Proteins; Cytochrome c Group; Cytochromes c; DNA Primers; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Lyases; Models, Biological; Molecular Sequence Data; Mutation; Periplasm; Plasmids; Point Mutation; Precipitin Tests; Protein Binding; Protein Structure, Tertiary; Protein Transport; Tryptophan | 2002 |
Increasing the redox potential of isoform 1 of yeast cytochrome c through the modification of select haem interactions.
Topics: Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Circular Dichroism; Cytochrome c Group; Cytochromes c; Electrochemistry; Heme; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Protein Isoforms; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrophotometry | 2002 |
Solution structure of cyanoferricytochrome c: ligand-controlled conformational flexibility and electronic structure of the heme moiety.
Topics: Amino Acid Sequence; Cytochrome c Group; Cytochromes c; Electrons; Heme; Ligands; Magnetic Resonance Spectroscopy; Magnetics; Molecular Sequence Data; Protein Conformation; Solutions | 2002 |
The Escherichia coli cytochrome c maturation (Ccm) system does not detectably attach heme to single cysteine variants of an apocytochrome c.
Topics: Amino Acid Motifs; Apoproteins; Binding Sites; Cysteine; Cytochrome c Group; Cytochromes c; Escherichia coli; Heme | 2002 |
Spectroscopic properties of a mitochondrial cytochrome C with a single thioether bond to the heme prosthetic group.
Topics: Amino Acid Substitution; Binding Sites; Circular Dichroism; Cysteine; Cytochrome c Group; Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Isoenzymes; Mitochondria; Nuclear Magnetic Resonance, Biomolecular; Saccharomyces cerevisiae Proteins; Serine; Sulfides | 2002 |
Cytochrome c maturation. The in vitro reactions of horse heart apocytochrome c and Paracoccus dentrificans apocytochrome c550 with heme.
Topics: Animals; Apoproteins; Circular Dichroism; Cysteine; Cytochrome c Group; Cytochromes c; Heme; Horses; Myocardium; Paracoccus denitrificans; Substrate Specificity | 2003 |
Effect of pH on the iso-1-cytochrome c denatured state: changing constraints due to heme ligation.
Topics: Acetylation; Amino Acid Substitution; Binding, Competitive; Cytochrome c Group; Cytochromes c; Genetic Variation; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Lysine; Mutagenesis, Site-Directed; Protein Conformation; Protein Denaturation; Protein Structure, Tertiary; Saccharomyces cerevisiae Proteins; Spectrometry, Fluorescence; Tryptophan | 2003 |
Interaction of heme with variants of the heme chaperone CcmE carrying active site mutations and a cleavable N-terminal His tag.
Topics: Apoproteins; Bacterial Outer Membrane Proteins; Binding Sites; Cytochrome c Group; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Binding | 2003 |
Chemiluminescent-based methods to detect subpicomole levels of c-type cytochromes.
Topics: Bacterial Proteins; Benzidines; Chemistry Techniques, Analytical; Chromogenic Compounds; Cytochromes c; Electrophoresis, Polyacrylamide Gel; Heme; Heterocyclic Compounds; Luminescent Measurements; Peroxidases; Rhodobacter capsulatus; Sensitivity and Specificity; Staining and Labeling | 2003 |
Redox-Bohr and other cooperativity effects in the nine-heme cytochrome C from Desulfovibrio desulfuricans ATCC 27774: crystallographic and modeling studies.
Topics: Binding Sites; Crystallography, X-Ray; Cytochromes c; Desulfovibrio; Electron Transport; Electrons; Heme; Hydrogen-Ion Concentration; Models, Molecular; Monte Carlo Method; Oxidation-Reduction; Oxygen; Protein Conformation; Protein Structure, Tertiary; Protons | 2003 |
NMR investigation of the alkaline-like conformational transition of horse heart cytochrome c in the presence of exogenous thiazole.
Topics: Alkalies; Animals; Cytochromes c; Heart; Heme; Horses; Hydrogen-Ion Concentration; Isomerism; Ligands; Magnetic Resonance Spectroscopy; Methylation; Molecular Structure; Protein Conformation; Protons; Thiazoles; Titrimetry | 2003 |
Electrostatic complexation and photoinduced electron transfer between Zn-cytochrome c and [olyanionic fullerene dendrimers.
Topics: Anions; Cytochromes c; Electrochemistry; Electron Transport; Fullerenes; Heme; Hydrogen Bonding; Models, Chemical; Models, Molecular; Molecular Structure; Photochemistry; Polymers; Spectrometry, Fluorescence; Spectrophotometry, Infrared; Static Electricity; Stereoisomerism; Zinc | 2003 |
Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Topics: Animals; Cytochromes c; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Horses; Magnetic Resonance Spectroscopy; Oxidation-Reduction | 2003 |
Vibrational frequency shifts and relaxation rates for a selected vibrational mode in cytochrome C.
Topics: Animals; Binding Sites; Biophysical Phenomena; Biophysics; Cytochromes c; Heme; Horses; Models, Molecular; Models, Statistical; Molecular Conformation; Oxygen; Protein Conformation; Software; Static Electricity; Temperature; Time Factors | 2003 |
Tuning heme redox potentials in the cytochrome C subunit of photosynthetic reaction centers.
Topics: Binding Sites; Cytochromes c; Heme; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Models, Statistical; Mutagenesis, Site-Directed; Oxidation-Reduction; Photosynthetic Reaction Center Complex Proteins; Protein Binding; Protons; Rhodopseudomonas | 2003 |
A study of the cytochrome c haemochromogen.
Topics: Amino Acids; Cytochromes; Cytochromes c; Heme | 1959 |
Interaction of nitrogenous ligands with heme peptides from mammalian cytochrome c.
Topics: Animals; Cytochromes; Cytochromes c; Heme; Ligands; Mammals; Nitrogen; Peptides | 1960 |
Oxidation-linked proton functions in heme octa- and undecapeptides from mammalian cytochrome c.
Topics: Animals; Cytochromes; Cytochromes c; Heme; Imidazoles; Mammals; Oxidation-Reduction; Peptides; Protons | 1960 |
THE 695-MMM. BAND OF FERRICYTOCHROME C AND ITS RELATIONSHIP TO PROTEIN CONFORMATION.
Topics: Chemical Phenomena; Chemistry, Physical; Cold Temperature; Cytochromes; Cytochromes c; Heme; Hot Temperature; Imidazoles; Iron; Pharmacology; Protein Conformation; Proteins; Research | 1964 |
RECONSTITUTION OF RESPIRATORY CHAIN ENZYME SYSTEMS. 13. SEQUENTIAL FRAGMENTATION OF SUCCINATE OXIDASE: PREPARATION AND PROPERTIES OF SUCCINATE-CYTOCHROME C REDUCTASE AND THE CYTOCHROME B-C1 PARTICLE.
Topics: Animals; Bile Acids and Salts; Cattle; Cytochromes; Cytochromes b; Cytochromes c; Electron Transport; Electron Transport Complex II; Electron Transport Complex IV; Enzyme Inhibitors; Flavins; Heme; Indophenol; Myocardium; NAD; Oxidoreductases; Research; Salts; Spectrophotometry; Succinate Cytochrome c Oxidoreductase; Succinate Dehydrogenase; Succinates; Succinic Acid; Ubiquinone | 1964 |
Thermodynamic data for myoglobin, haemoglobin and cytochrome-c reactions, and the position of the haem groups.
Topics: Cytochromes; Cytochromes c; Heme; Hemoglobins; Myoglobin; Thermodynamics | 1955 |
Mimicking photosynthesis in a computationally designed synthetic metalloprotein.
Topics: 2,2'-Dipyridyl; Amino Acid Sequence; Biomimetic Materials; Circular Dichroism; Cytochromes c; Helix-Loop-Helix Motifs; Heme; Metalloproteins; Molecular Sequence Data; Naphthoquinones; Organometallic Compounds; Oxidation-Reduction; Photosynthesis; Photosynthetic Reaction Center Complex Proteins; Protein Conformation; Ruthenium; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | 2003 |
Overlapping specificities of the mitochondrial cytochrome c and c1 heme lyases.
Topics: Alleles; Animals; Binding Sites; Cytochromes c; Cytochromes c1; Flavin-Adenine Dinucleotide; Fungal Proteins; Genes, Dominant; Glucose; Glycerol; Heme; Humans; Lyases; Mice; Mitochondria; Models, Biological; Mutation; Oxidation-Reduction; Plasmids; RNA; RNA, Messenger; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Species Specificity; Substrate Specificity; Ultraviolet Rays | 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 |
Dynamic features of a heme delivery system for cytochrome C maturation.
Topics: Alanine; Amino Acid Motifs; Bacterial Outer Membrane Proteins; Bacterial Proteins; Cell Division; Cytochromes c; Cytoplasm; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Genotype; Heme; Hemeproteins; Histidine; Membrane Proteins; Models, Biological; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Periplasm; Phenotype; Plasmids; Precipitin Tests; Protein Binding; Subcellular Fractions; Tryptophan | 2003 |
Reversal of cyanide inhibition of cytochrome c oxidase by the auxiliary substrate nitric oxide: an endogenous antidote to cyanide poisoning?
Topics: Animals; Brain; Catalysis; Cattle; Copper; Cyanides; Cytochromes c; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Electrons; Heme; Histidine; Iron; Kinetics; Magnetics; Mitochondria; Models, Chemical; Myocardium; Nitric Oxide; Oxygen; Potassium Cyanide; Spectrophotometry | 2003 |
A cytochrome b562 variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation system.
Topics: Amino Acid Motifs; Cysteine; Cytochrome b Group; Cytochromes c; Disulfides; Dithionite; Dithiothreitol; Escherichia coli; Escherichia coli Proteins; Heme; Hemin; Mutation; Plasmids; Protein Binding; Protein Disulfide-Isomerases; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry; Subcellular Fractions | 2003 |
Radiation-induced enhancement of nitrite reducing activity of cytochrome c.
Topics: Circular Dichroism; Cytochromes c; Drug Stability; Gamma Rays; Heme; Methionine; Nitrite Reductases; Nitrites; Oxidation-Reduction; Protein Folding | 2003 |
Co-ordination of iron acquisition, iron porphyrin chelation and iron-protoporphyrin export via the cytochrome c biogenesis protein CcmC in Pseudomonas fluorescens.
Topics: Bacterial Proteins; Base Sequence; Biological Transport, Active; Cytochromes c; DNA, Bacterial; Ferrochelatase; Genes, Bacterial; Heme; Iron; Iron Chelating Agents; Membrane Proteins; Models, Biological; Mutation; Oligopeptides; Oxidative Stress; Phenotype; Pigments, Biological; Porphyrins; Protoporphyrins; Pseudomonas fluorescens; Quinolines; Siderophores | 2003 |
1H NMR structural characterization of the cytochrome c modifications in a micellar environment.
Topics: Animals; Cytochromes c; Electron Transport; Ferric Compounds; Ferrous Compounds; Heme; Horses; Ligands; Micelles; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protons; Sodium Dodecyl Sulfate; Spectrophotometry, Ultraviolet; Thermodynamics | 2003 |
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 |
The roles of different regions of the CycH protein in c-type cytochrome biogenesis in Sinorhizobium meliloti.
Topics: Amino Acid Sequence; Bacterial Proteins; beta-Galactosidase; Cytochromes c; DNA Primers; Escherichia coli; Heme; Membrane Proteins; Molecular Sequence Data; Plasmids; Protein Structure, Tertiary; Sequence Alignment; Sequence Analysis, DNA; Sinorhizobium meliloti | 2004 |
Anti-cooperative oxidation of ubiquinol by the yeast cytochrome bc1 complex.
Topics: Antimycin A; Cytochromes b; Cytochromes c; Dimerization; Electron Transport Complex III; Fungal Proteins; Heme; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Kinetics; Mutation; Oxidation-Reduction; Oxygen; Spectrophotometry; Time Factors; Ubiquinone; Ultraviolet Rays | 2004 |
A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide.
Topics: Animals; Binding Sites; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Stability; Ferric Compounds; Glycine; Heme; Hemeproteins; Histidine; Horses; Imidazoles; Iron; Ligands; Mercaptoethanol; Methionine; Peptide Fragments; Peptides; Protein Structure, Secondary; Spectrum Analysis, Raman; Structure-Activity Relationship | 2004 |
Reversible redox energy coupling in electron transfer chains.
Topics: Adenosine Triphosphate; Catalysis; Coenzymes; Cytochrome b Group; Cytochromes c; Electron Transport; Electron Transport Complex III; Heme; Hydrogen-Ion Concentration; Hydroquinones; Kinetics; Photosynthesis; Protons; Rhodobacter capsulatus; Thermodynamics | 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 |
New activities of a catalytic antibody with a peroxidase activity: formation of Fe(II)-RNO complexes and stereoselective oxidation of sulfides.
Topics: Animals; Binding Sites; Cytochromes c; Heme; Horses; Hydrogen Peroxide; Hydroxylamines; Iron; Kinetics; Models, Biological; Models, Chemical; Oxygen; Peroxidases; Porphyrins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Stereoisomerism; Sulfides; tert-Butylhydroperoxide; Time Factors; Ultraviolet Rays | 2004 |
Crystallization and preliminary X-ray diffraction analysis of the 16-haem cytochrome of Desulfovibrio gigas.
Topics: Crystallization; Crystallography, X-Ray; Cytochromes c; Desulfovibrio gigas; Desulfovibrio vulgaris; Heme; Models, Molecular; Structural Homology, Protein | 2004 |
Identification of 42 possible cytochrome C genes in the Shewanella oneidensis genome and characterization of six soluble cytochromes.
Topics: Amino Acid Sequence; Cell Division; Cytochrome c Group; Cytochromes; Cytochromes c; Electrophoresis, Gel, Two-Dimensional; Fumarates; Genome, Bacterial; Heme; Molecular Sequence Data; Oligonucleotide Array Sequence Analysis; Proteome; Sequence Homology, Amino Acid; Shewanella; Spectrophotometry; Ultraviolet Rays | 2004 |
Conformational properties of the iso-1-cytochrome C denatured state: dependence on guanidine hydrochloride concentration.
Topics: Cytochromes c; Guanidine; Heme; Histidine; Isoenzymes; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 2004 |
Induction of heme oxygenase-1 inhibits NAD(P)H oxidase activity by down-regulating cytochrome b558 expression via the reduction of heme availability.
Topics: Actins; Animals; Anions; Antioxidants; Blotting, Western; Cell Line; Cell Survival; Cytochrome b Group; Cytochromes c; Dose-Response Relationship, Drug; Down-Regulation; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Luminescent Measurements; Macrophages; Male; Membrane Glycoproteins; Membrane Proteins; Membrane Transport Proteins; Mice; Microscopy, Confocal; Microscopy, Fluorescence; NADPH Dehydrogenase; NADPH Oxidase 2; NADPH Oxidases; Oxygen; Phagocytosis; Phosphoproteins; Plasmids; Polymerase Chain Reaction; Rats; Rats, Sprague-Dawley; Reactive Oxygen Species; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Superoxides; Time Factors; Transfection | 2004 |
NCB5OR is a novel soluble NAD(P)H reductase localized in the endoplasmic reticulum.
Topics: Animals; Base Sequence; Blotting, Western; Calreticulin; Cell Line; Chromatography, High Pressure Liquid; Computational Biology; COS Cells; Cytochrome-B(5) Reductase; Cytochromes b5; Cytochromes c; Dose-Response Relationship, Drug; Endoplasmic Reticulum; Female; Ferricyanides; Heme; Humans; Kinetics; Liver; Methemoglobin; Mice; Microscopy, Confocal; Molecular Sequence Data; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Oxygen; Phenotype; Photons; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Nucleic Acid; Spectrum Analysis, Raman; Subcellular Fractions; Superoxides; Time Factors; Transfection; Ultraviolet Rays | 2004 |
Paracoccus pantotrophus NapC can reductively activate cytochrome cd1 nitrite reductase.
Topics: Catalysis; Cytochromes; Cytochromes c; Electron Transport Complex IV; Enzyme Activation; Heme; Histidine; Kinetics; Ligands; Nitrite Reductases; Oxygen; Paracoccus pantotrophus; Spectrophotometry; Time Factors; Tyrosine | 2004 |
A model for the misfolded bis-His intermediate of cytochrome c: the 1-56 N-fragment.
Topics: Animals; Cytochromes c; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Models, Molecular; Myocardium; Peptides; Protein Denaturation; Protein Folding; Protein Structure, Tertiary | 2004 |
Three different oxygen-induced radical species in endothelial nitric-oxide synthase oxygenase domain under regulation by L-arginine and tetrahydrobiopterin.
Topics: Amino Acids; Arginine; Biopterins; Catalysis; Cytochromes c; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Humans; Kinetics; Models, Chemical; Nitric Oxide Synthase; Nitric Oxide Synthase Type III; Normal Distribution; Oxygen; Oxygenases; Protein Structure, Tertiary; Proteins; Reactive Oxygen Species; Recombinant Proteins; Spectrophotometry; Superoxides; Time Factors | 2004 |
Heme deficiency causes apoptosis but does not increase ROS generation in HeLa cells.
Topics: Apoptosis; Caspase 3; Caspases; Cell Division; Cell Survival; Cytochromes c; Enzyme Activation; Enzyme Inhibitors; HeLa Cells; Heme; Heptanoates; Humans; In Situ Nick-End Labeling; Membrane Potentials; Mitochondria; Reactive Oxygen Species | 2004 |
The function of the small insertion in the hinge subdomain in the control of constitutive mammalian nitric-oxide synthases.
Topics: Adenosine Diphosphate; Animals; Base Sequence; Binding Sites; Calmodulin; Cattle; Chromatography; Cytochrome Reductases; Cytochromes c; Electrons; Electrophoresis, Polyacrylamide Gel; Endopeptidases; Escherichia coli; Gene Deletion; Heme; Models, Molecular; Molecular Sequence Data; Mutagenesis; Mutation; NADPH-Ferrihemoprotein Reductase; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Nitric Oxide Synthase Type III; Protein Structure, Tertiary; Rats; Sequence Homology, Nucleic Acid; Ultraviolet Rays | 2004 |
Classical force field parameters for the heme prosthetic group of cytochrome c.
Topics: Algorithms; Computer Simulation; Crystallography, X-Ray; Cytochromes c; Heme; Models, Molecular; Molecular Conformation; Molecular Structure; Oxidation-Reduction; Static Electricity; Thermodynamics | 2004 |
Design and synthesis of de novo cytochromes c.
Topics: Amino Acid Sequence; Animals; Cattle; Cytochromes b; Cytochromes c; Genes, Synthetic; Helix-Loop-Helix Motifs; Heme; Histidine; Methionine; Molecular Sequence Data; Oxidation-Reduction; Peptides; Protein Binding; Protein Engineering; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Sulfides | 2004 |
Purification and spectropotentiometric characterization of Escherichia coli NrfB, a decaheme homodimer that transfers electrons to the decaheme periplasmic nitrite reductase complex.
Topics: Cytochrome c Group; Cytochromes c; Dimerization; Electron Transport; Escherichia coli Proteins; Heme; Iron; Nitrite Reductases; Oxidation-Reduction; Periplasmic Proteins; Spectrum Analysis | 2004 |
Biosynthesis of artificial microperoxidases by exploiting the secretion and cytochrome c maturation apparatuses of Escherichia coli.
Topics: Bradyrhizobium; Cytochromes c; Escherichia coli; Heme; Oligopeptides; Peroxidases; Protein Engineering | 2004 |
Effect of axial coordination on the kinetics of assembly and folding of the two halves of horse heart cytochrome C.
Topics: Animals; Circular Dichroism; Cytochromes; Cytochromes c; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Models, Molecular; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Protons; Spectrophotometry; Time Factors; Ultraviolet Rays | 2004 |
Internal friction controls the speed of protein folding from a compact configuration.
Topics: Animals; Carbon Monoxide; Cytochromes c; Enzyme Stability; Ferrous Compounds; Heme; Horses; Protein Conformation; Protein Denaturation; Protein Folding; Solvents; Spectrophotometry; Thermodynamics; Viscosity | 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 |
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 |
Photodissociation of heme distal methionine in ferrous cytochrome C revealed by subpicosecond time-resolved resonance Raman spectroscopy.
Topics: Cytochromes c; Heme; Kinetics; Methionine; Photochemistry; Spectrum Analysis, Raman | 2004 |
Modulation of the folding energy landscape of cytochrome C with salt.
Topics: Cytochromes c; Fluorescence; Heme; Kinetics; Potassium Chloride; Protein Folding; Thermodynamics; Tryptophan | 2004 |
CcmD is involved in complex formation between CcmC and the heme chaperone CcmE during cytochrome c maturation.
Topics: Amino Acid Sequence; Bacterial Outer Membrane Proteins; Bacterial Proteins; Biological Transport; Cytochromes c; Escherichia coli Proteins; Heme; Hemeproteins; Membrane Proteins; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Structure, Tertiary | 2005 |
Computationally analyzing the possible biological function of YJL103C--an ORF potentially involved in the regulation of energy process in yeast.
Topics: Binding Sites; Computer Simulation; Cytochromes c; Heme; Oligonucleotide Array Sequence Analysis; Open Reading Frames; Promoter Regions, Genetic; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Transcription Factors | 2005 |
Overexpression of multi-heme C-type cytochromes.
Topics: Cloning, Molecular; Cytochromes c; Gene Expression Regulation, Enzymologic; Genetic Enhancement; Heme; Protein Engineering; Recombinant Proteins; Shewanella | 2005 |
Small interference RNA-mediated gene silencing of human biliverdin reductase, but not that of heme oxygenase-1, attenuates arsenite-mediated induction of the oxygenase and increases apoptosis in 293A kidney cells.
Topics: Acetylcysteine; Apoptosis; Apoptosis Regulatory Proteins; Arsenites; Biliverdine; Blotting, Northern; Blotting, Western; Cell Line; Cell Nucleus; Cell Survival; Cytochromes c; Enzyme-Linked Immunosorbent Assay; Flow Cytometry; Gene Silencing; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Humans; Luciferases; Membrane Glycoproteins; Membrane Proteins; Oligonucleotides; Oxidative Stress; Oxidoreductases Acting on CH-CH Group Donors; Oxygen; Phosphorylation; Poly(ADP-ribose) Polymerases; Promoter Regions, Genetic; Protein Binding; Protein Biosynthesis; Receptors, TNF-Related Apoptosis-Inducing Ligand; Receptors, Tumor Necrosis Factor; Retroviridae; RNA, Messenger; RNA, Small Interfering; Serine; Sodium Compounds; Threonine; Time Factors; TNF-Related Apoptosis-Inducing Ligand; Transcription Factor AP-1; Transfection; Tumor Necrosis Factor-alpha | 2005 |
Functional characterization and purification of a Saccharomyces cerevisiae ADP/ATP carrier-iso 1 cytochrome c fusion protein.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Atractyloside; Chromatography; Cloning, Molecular; Crystallization; Cytochromes c; Escherichia coli; Genetic Engineering; Heme; Histidine; Kinetics; Mitochondrial ADP, ATP Translocases; Molecular Probes; Recombinant Fusion Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 2005 |
Photoinduced electron transfer between cytochrome c and a novel 1,4,5,8-naphthalenetetracarboxylic diimide with amphiphilic character.
Topics: Cytochromes c; Electron Transport; Heme; Imides; Micelles; Naphthalenes; Photochemistry; Surface-Active Agents; Ultraviolet Rays | 2005 |
The histidine of the c-type cytochrome CXXCH haem-binding motif is essential for haem attachment by the Escherichia coli cytochrome c maturation (Ccm) apparatus.
Topics: Amino Acid Substitution; Arginine; Binding Sites; Cytochrome b Group; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Lysine; Mutation; Protein Binding | 2005 |
Direct electrochemistry of heme multicofactor-containing enzymes on alkanethiol-modified gold electrodes.
Topics: Adsorption; Carbohydrate Dehydrogenases; Cysteamine; Cytochromes c; Electrochemistry; Electrodes; Electron Transport; Gold; Heme; Hydrogen-Ion Concentration; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Spectrophotometry; Sulfhydryl Compounds | 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 |
A heme tag for in vivo synthesis of artificial cytochromes.
Topics: Amino Acid Sequence; Carrier Proteins; Chromatography, Ion Exchange; Cytochromes c; Escherichia coli; Heme; Maltose-Binding Proteins; Molecular Sequence Data; Recombinant Fusion Proteins | 2005 |
Hopping in the electron-transfer photocycle of the 1:1 complex of Zn-cytochrome c peroxidase with cytochrome c.
Topics: Cytochrome-c Peroxidase; Cytochromes c; Heme; Kinetics; Oxidation-Reduction; Photochemistry; Zinc | 2005 |
Early events in the folding of four-helix-bundle heme proteins.
Topics: Carbon Monoxide; Circular Dichroism; Cytochromes b; Cytochromes c; Escherichia coli; Heme; Kinetics; Protein Conformation; Protein Folding; Spectrometry, Fluorescence | 2005 |
Electron transfer chain reaction of the extracellular flavocytochrome cellobiose dehydrogenase from the basidiomycete Phanerochaete chrysosporium.
Topics: Carbohydrate Dehydrogenases; Cellobiose; Cytochromes c; Electron Transport; Flavin-Adenine Dinucleotide; Flavins; Fungal Proteins; Heme; Kinetics; Mutation; Oxidation-Reduction; Phanerochaete; Thermodynamics | 2005 |
Suppression of the pro-apoptotic function of cytochrome c by singlet oxygen via a haem redox state-independent mechanism.
Topics: Animals; Apoptosis; Caspases; Cell Line, Tumor; Cysteine; Cytochromes c; Enzyme Activation; Glutathione; Heme; Horses; Humans; Oxidation-Reduction; Singlet Oxygen | 2005 |
A funneled energy landscape for cytochrome c directly predicts the sequential folding route inferred from hydrogen exchange experiments.
Topics: Biophysical Phenomena; Biophysics; Cytochromes c; Heme; Hydrogen; Models, Molecular; Protein Conformation; Protein Folding; Thermodynamics | 2005 |
Functional characterization of the C-terminal domain of the cytochrome c maturation protein CcmE.
Topics: Anilino Naphthalenesulfonates; Bacterial Outer Membrane Proteins; Binding Sites; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Mutagenesis, Site-Directed; Periplasm; Protein Binding; Protein Structure, Tertiary; Protoporphyrins | 2005 |
Axial ligation and polypeptide matrix effects on the reduction potential of heme proteins probed on their cyanide adducts.
Topics: Cyanides; Cytochromes c; Electrochemistry; Heme; Hemeproteins; Histidine; Oxidation-Reduction; Peptides; Peroxidases; Plant Proteins; Plants; Thermodynamics; Ultraviolet Rays | 2005 |
Upregulation of alpha globin promotes apoptotic cell death in the hematopoietic cell line FL5.12.
Topics: Amino Acid Chloromethyl Ketones; Animals; Apoptosis; B-Lymphocytes; bcl-2-Associated X Protein; BH3 Interacting Domain Death Agonist Protein; Caspases; Cell Line; Cisplatin; Cycloheximide; Cytochromes c; Doxorubicin; Globins; Green Fluorescent Proteins; HeLa Cells; Hematopoietic Stem Cells; Heme; Humans; Interleukin-3; K562 Cells; Mice; NIH 3T3 Cells; Oligonucleotide Array Sequence Analysis; Staurosporine; Tumor Necrosis Factor-alpha; Up-Regulation | 2005 |
A size dependent folding contour for cytochrome C.
Topics: Binding Sites; Cytochromes c; Heme; Molecular Weight; Peroxidase; Protein Conformation; Protein Folding; Protein Renaturation; Scattering, Radiation | 2006 |
Coverage-dependent changes of cytochrome c transverse location in phospholipid membranes revealed by FRET.
Topics: Adsorption; Animals; Cardiolipins; Cattle; Cell Membrane; Cytochromes c; Dose-Response Relationship, Drug; Fluorescence Resonance Energy Transfer; Heme; Horses; Kinetics; Lipid Bilayers; Lipids; Liposomes; Membranes, Artificial; Models, Chemical; Models, Statistical; Phosphatidylcholines; Phosphatidylglycerols; Phospholipids; Protein Binding; Proteins; Spectrometry, Fluorescence; Surface Properties | 2005 |
Cyc2p, a membrane-bound flavoprotein involved in the maturation of mitochondrial c-type cytochromes.
Topics: Amino Acid Motifs; Binding Sites; Carrier Proteins; Cell Membrane; Cytochromes c; Cytochromes c1; Electrophoresis, Polyacrylamide Gel; Flavins; Flavoproteins; Fungal Proteins; Gene Expression Regulation, Fungal; Heme; Kinetics; Lyases; Mitochondria; Mitochondrial Proteins; Models, Biological; Mutation; Oxidation-Reduction; Oxygen Consumption; Plasmids; Protein Binding; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Submitochondrial Particles; Temperature | 2005 |
Endonuclease-like activity of heme proteins.
Topics: Animals; Binding Sites; Blood Proteins; Calorimetry; Calorimetry, Differential Scanning; Cattle; Circular Dichroism; Cytochromes c; DNA; Electrophoresis, Agar Gel; Endonucleases; Heme; Hemoglobins; Horses; Kinetics; Metmyoglobin; Nucleic Acid Conformation; Oxidation-Reduction; Protein Binding; Protein Denaturation; Spectrophotometry, Ultraviolet | 2005 |
A new soluble 10kDa monoheme cytochrome c-552 from the anammox bacterium Candidatus "Kuenenia stuttgartiensis".
Topics: Amino Acid Sequence; Bacteria, Anaerobic; Chromatography, Ion Exchange; Cytochromes c; DNA, Bacterial; Electrophoresis, Polyacrylamide Gel; Geobacter; Heme; Molecular Sequence Data; Molecular Weight; Nitrosomonas europaea; Sequence Analysis, DNA; Sequence Analysis, Protein; Sequence Homology, Amino Acid; Solubility; Spectrum Analysis; Ultracentrifugation | 2005 |
Frataxin deficiency alters heme pathway transcripts and decreases mitochondrial heme metabolites in mammalian cells.
Topics: Amino Acid Sequence; Animals; Cells, Cultured; Coproporphyrinogen Oxidase; Cytochromes c; Ferrochelatase; Frataxin; Heart; Heme; Humans; Iron-Binding Proteins; Mammals; Mice; Mice, Knockout; Mitochondria; Molecular Sequence Data; Mutation; Myocardium; Oligonucleotide Array Sequence Analysis; Proto-Oncogene Proteins; Protoporphyrins; Sequence Homology, Amino Acid; Transcription, Genetic; Zinc | 2005 |
Redox properties of wild-type and heme-binding loop mutants of bacterial cytochromes C measured by direct electrochemistry.
Topics: Bacterial Proteins; Binding Sites; Buffers; Cytochromes c; Electrochemistry; Heme; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Mutation; Nitrosomonas europaea; Osmolar Concentration; Oxidation-Reduction; Protein Conformation; Pseudomonas aeruginosa | 2005 |
Cytochrome c conformations resolved by the photon counting histogram: watching the alkaline transition with single-molecule sensitivity.
Topics: Alkalies; Cysteine; Cytochromes c; Fluorescence; Heme; Microscopy, Confocal; Models, Molecular; Photons; Protein Structure, Tertiary; Rhodamines; Saccharomyces cerevisiae; Sensitivity and Specificity | 2005 |
Interaction of azide ion with hemin and cytochrome c immobilized on Au and Ag nanoparticles.
Topics: Azides; Cytochrome c Group; Cytochromes c; Heme; Hemin; Nanoparticles | 2005 |
Snapshots of cytochrome c folding.
Topics: Cytochromes c; Fluorescence Resonance Energy Transfer; Heme; Kinetics; Models, Molecular; Peptides; Protein Folding; Protein Structure, Tertiary; Saccharomyces cerevisiae | 2005 |
The membrane anchors of the heme chaperone CcmE and the periplasmic thioredoxin CcmG are functionally important.
Topics: Bacterial Outer Membrane Proteins; Biological Transport; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Periplasm; Protein Disulfide Reductase (Glutathione); Protein Processing, Post-Translational; Protein Structure, Tertiary; Recombinant Fusion Proteins; Thioredoxins | 2006 |
Dehydration in the folding of reduced cytochrome c revealed by the electron-transfer-triggered folding under high pressure.
Topics: Cytochromes c; Guanidine; Heme; Hydrophobic and Hydrophilic Interactions; Kinetics; Oxidation-Reduction; Pressure; Protein Folding; Water | 2006 |
The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c.
Topics: Animals; Cyanides; Cytochromes c; Entropy; Heme; Horses; Iron; Oxidation-Reduction; Protein Conformation; Static Electricity; Thermodynamics | 2006 |
Nitric oxide inhibits peroxidase activity of cytochrome c.cardiolipin complex and blocks cardiolipin oxidation.
Topics: Animals; Apoptosis; Cardiolipins; Cytochromes c; Electron Spin Resonance Spectroscopy; Etoposide; Heme; Horses; Hydrogen Peroxide; Nitric Oxide; Oxygen; Phospholipids | 2006 |
Order parameters and orientation distributions of solution adsorbed and microcontact printed cytochrome c protein films on glass and ITO.
Topics: Adsorption; Animals; Cytochromes c; Electrons; Glass; Heme; Horses; Solutions; Spectrophotometry | 2006 |
Photon echo spectroscopy of porphyrins and heme proteins: effects of quasidegenerate electronic structure on the peak shift decay.
Topics: Animals; Chemical Phenomena; Chemistry, Physical; Cytochromes c; Heme; Horses; Models, Statistical; Models, Theoretical; Oscillometry; Porphyrins; Protoporphyrins; Solvents; Spectrophotometry; Zinc | 2006 |
Extracytoplasmic prosthetic group ligation to apoproteins: maturation of c-type cytochromes.
Topics: Bordetella pertussis; Cytochromes c; Cytochromes c1; Cytochromes c2; Escherichia coli; Heme; Mutation; Recombinant Proteins | 2006 |
Studies on the respiratory enzymes of the adrenal gland. I. The medulla.
Topics: Adrenal Cortex; Adrenal Medulla; Cytochromes; Cytochromes c; Heme; Humans; Liver; Mitochondria; NADP Transhydrogenases; Oxidation-Reduction; Succinate Dehydrogenase; Viscera | 1961 |
Redox-coupled dynamics and folding in cytochrome c.
Topics: Carbon; Cytochromes c; Deuterium; Electron Transport; Heme; Oxidation-Reduction; Protein Conformation; Protein Folding; Spectroscopy, Fourier Transform Infrared | 2006 |
Ultrafast heme dynamics in ferrous versus ferric cytochrome c studied by time-resolved resonance Raman and transient absorption spectroscopy.
Topics: Cytochromes c; Ferric Compounds; Ferrous Compounds; Heme; Kinetics; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman | 2006 |
Extensive misfolding in the refolding reaction of alkaline ferrocytochrome C.
Topics: Animals; Carbon Monoxide; Cytochromes c; Heme; Horses; Hydrogen; Magnetic Resonance Spectroscopy; Protein Denaturation; Protein Folding; Sulfates | 2006 |
Heme coordination states of unfolded ferrous cytochrome C.
Topics: Animals; Cytochromes c; Detergents; Guanfacine; Heme; Horses; Hydrogen Bonding; Hydrogen-Ion Concentration; Liposomes; Peroxidases; Phosphatidylglycerols; Protein Denaturation; Protein Folding; Quaternary Ammonium Compounds; Sodium Dodecyl Sulfate; Spectrum Analysis; Temperature | 2006 |
Estimation of the orientation of heme in cytochrome C immobilized on a carboxylate-terminated alkanethiol monolayer on a au electrode by the use of electroreflectance spectroscopy with polarized light incidence.
Topics: Alkanes; Animals; Anisotropy; Carboxylic Acids; Cytochromes c; Electrochemistry; Electrodes; Enzymes, Immobilized; Gold; Heme; Horses; Light; Models, Biological; Myocardium; Optical Rotation; Spectrum Analysis; Sulfhydryl Compounds; Surface Properties | 2006 |
c-Type cytochromes in Pelobacter carbinolicus.
Topics: Bacterial Proteins; Cytochromes c; Deltaproteobacteria; Heme; Polymerase Chain Reaction; Proteomics; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger | 2006 |
Frataxin knockdown causes loss of cytoplasmic iron-sulfur cluster functions, redox alterations and induction of heme transcripts.
Topics: Cell Line; Cytochromes c; Cytoplasm; Frataxin; Gene Expression; Heme; Humans; Iron-Binding Proteins; Iron-Sulfur Proteins; Mitochondrial Proteins; Oxidative Stress; Protein Folding; RNA, Small Interfering; Signal Transduction; Superoxide Dismutase | 2007 |
Optical band splitting and electronic perturbations of the heme chromophore in cytochrome C at room temperature probed by visible electronic circular dichroism spectroscopy.
Topics: Circular Dichroism; Computer Simulation; Cytochromes c; Electron Transport; Heme; Light; Models, Chemical; Temperature | 2007 |
Extractive solubilization, structural change, and functional conversion of cytochrome c in ionic liquids via crown ether complexation.
Topics: Catalysis; Crown Ethers; Cytochromes c; Electron Transport; Heme; Hydrogen Peroxide; Ions; Oxidation-Reduction; Peptides; Peroxidase; Proteins; Solubility; Solutions; Spectrum Analysis; Time Factors | 2006 |
Ligand dynamics in an electron transfer protein. Picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome c.
Topics: Carbon Monoxide; Cytochromes c; Electrons; Heme; Kinetics; Ligands; Models, Chemical; Mutagenesis, Site-Directed; Mutation; Myoglobin; Nitric Oxide; Oxidation-Reduction; Oxygen; Protein Binding; Saccharomyces cerevisiae | 2007 |
X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Cell Membrane; Crystallography, X-Ray; Cytochromes c; Desulfovibrio vulgaris; Heme; Models, Molecular; Molecular Sequence Data; Oxidoreductases; Protein Folding; Protein Structure, Secondary; Sequence Alignment; Static Electricity | 2006 |
Cytochrome C in a dry trehalose matrix: structural and dynamical effects probed by x-ray absorption spectroscopy.
Topics: Animals; Cytochromes c; Heme; Histidine; Horses; Iron; Models, Molecular; Myocardium; Polyvinyl Alcohol; Protein Conformation; Solutions; Spectrum Analysis; Trehalose; X-Rays | 2007 |
Weak-field anions displace the histidine ligand in a synthetic heme peptide but not in N-acetylmicroperoxidase-8: possible role of heme geometry differences.
Topics: Animals; Anions; Azides; Binding Sites; Cyanides; Cytochromes c; Fluorides; Heme; Hemeproteins; Histidine; Horses; Ligands; Molecular Structure; Myocardium; Peptide Fragments; Peptides; Protein Conformation | 2007 |
Electron transfer and ligand binding to cytochrome c' immobilized on self-assembled monolayers.
Topics: Adsorption; Animals; Carbon Monoxide; Carboxylic Acids; Cytochromes c; Electrochemistry; Electrons; Gold; Heme; Horses; Hydrogen-Ion Concentration; Myocardium; Proteobacteria; Static Electricity; Sulfhydryl Compounds | 2007 |
A conformational switch to beta-sheet structure in cytochrome c leads to heme exposure. Implications for cardiolipin peroxidation and apoptosis.
Topics: Apoptosis; Cardiolipins; Cytochromes c; Heme; Hydrogen-Ion Concentration; Iron; Models, Molecular; Peroxidases; Peroxides; Protein Structure, Secondary; Spectrum Analysis, Raman; Temperature | 2007 |
Ab initio molecular dynamics of heme in cytochrome c.
Topics: Computer Simulation; Cytochromes c; Heme; Magnetic Resonance Spectroscopy; Models, Chemical; Reference Standards; Sensitivity and Specificity; Thermodynamics; Time Factors | 2007 |
Effects of heme pocket structure and mobility on cytochrome c stability.
Topics: Bacteria; Crystallography, X-Ray; Cytochromes c; Enzyme Stability; Heme; Models, Molecular; Protein Conformation; Protein Denaturation | 2007 |
Direct electrochemical and spectroscopic assessment of heme integrity in multiphoton photo-cross-linked cytochrome C structures.
Topics: Animals; Cattle; Cross-Linking Reagents; Cytochromes c; Electrochemistry; Heme; Peroxidase; Photochemistry; Photons; Protein Conformation; Spectrum Analysis, Raman | 2007 |
Functional roles of the heme architecture and its environment in tetraheme cytochrome c.
Topics: Cytochrome c Group; Cytochromes c; Electron Transport; Escherichia coli; Heme; Molecular Conformation; Oxidation-Reduction; Plasmids; Protein Conformation; Shewanella | 2007 |
Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE.
Topics: Adenosine Triphosphate; Amino Acid Motifs; Aspartic Acid; ATP-Binding Cassette Transporters; Bacterial Outer Membrane Proteins; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Histidine; Hydrolysis; Lysine; Mutagenesis, Site-Directed; Protein Processing, Post-Translational; Protein Subunits; Sequence Deletion | 2007 |
Solution conformation of the His-47 to Ala-47 mutant of Pseudomonas stutzeri ZoBell ferrocytochrome c-551.
Topics: Alanine; Bacterial Proteins; Cytochrome c Group; Cytochromes c; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Models, Chemical; Molecular Conformation; Mutation; Oxidation-Reduction; Protein Conformation; Pseudomonas stutzeri; Thermodynamics | 2007 |
Oleamide synthesizing activity from rat kidney: identification as cytochrome c.
Topics: Acyl Coenzyme A; Ammonium Sulfate; Animals; Catalysis; Chromatography, High Pressure Liquid; Cytochromes c; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kidney; Kinetics; Models, Biological; Oleic Acids; Rats; Temperature | 2007 |
A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding.
Topics: Amino Acid Motifs; Amino Acid Sequence; Binding Sites; Cytochromes c; Heme; Lyases; Mass Spectrometry; Molecular Sequence Data; Protein Binding; Protein Processing, Post-Translational; Wolinella | 2007 |
Static normal coordinate deformations of the heme group in mutants of ferrocytochrome c from Saccharomyces cerevisiae probed by resonance Raman spectroscopy.
Topics: Algorithms; Chemical Phenomena; Chemistry, Physical; Computer Simulation; Cytochromes c; Heme; Models, Chemical; Models, Molecular; Molecular Conformation; Mutation; Protein Conformation; Saccharomyces cerevisiae; Spectrum Analysis, Raman | 2007 |
The crystal structure of the pentahaem c-type cytochrome NrfB and characterization of its solution-state interaction with the pentahaem nitrite reductase NrfA.
Topics: Amino Acid Motifs; Amino Acid Sequence; Conserved Sequence; Crystallography, X-Ray; Cytochrome c Group; Cytochromes c; Dimerization; Escherichia coli; Escherichia coli Proteins; Heme; Light; Models, Molecular; Molecular Sequence Data; Nitrate Reductases; Oxidation-Reduction; Protein Binding; Protein Structure, Tertiary; Scattering, Radiation; Solutions; Spectrometry, Fluorescence; Ultracentrifugation | 2007 |
In vitro synthesis of oleoylglycine by cytochrome c points to a novel pathway for the production of lipid signaling molecules.
Topics: Acyl Coenzyme A; Animals; Chromatography, Thin Layer; Cytochromes c; Fatty Acids; Glycine; Heme; Hemoglobins; Hydrogen Peroxide; In Vitro Techniques; Lipids; Mass Spectrometry; Models, Biological; Myoglobin; Oleic Acids; Rats; Signal Transduction | 2007 |
Redox-linked conformational changes of a multiheme cytochrome from Geobacter sulfurreducens.
Topics: Cytochromes c; Geobacter; Heme; Oxidation-Reduction; Oxygen; Protein Conformation | 2007 |
Sequence composition effects on denatured state loop formation in iso-1-cytochrome c variants: polyalanine versus polyglycine inserts.
Topics: Amino Acid Sequence; Cytochromes c; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutagenesis, Insertional; Mutant Proteins; Peptides; Protein Denaturation; Protein Structure, Secondary; Saccharomyces cerevisiae Proteins; Thermodynamics; Titrimetry | 2007 |
A kinetic approach to the dependence of dissimilatory metal reduction by Shewanella oneidensis MR-1 on the outer membrane cytochromes c OmcA and OmcB.
Topics: Bacterial Outer Membrane Proteins; Chelating Agents; Cytochromes c; Enzyme Inhibitors; Heme; Kinetics; Metals; Mutation; Oxidation-Reduction; Sensitivity and Specificity; Shewanella | 2007 |
Probing the role of the conserved beta-II turn Pro-76/Gly-77 of mitochondrial cytochrome c.
Topics: Amino Acid Substitution; Animals; Base Sequence; Binding Sites; Circular Dichroism; Conserved Sequence; Cytochromes c; DNA Primers; Heme; In Vitro Techniques; Mitochondria; Models, Molecular; Mutagenesis, Site-Directed; Protein Denaturation; Protein Structure, Secondary; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics | 2007 |
Alkaline conformational transition and gated electron transfer with a Lys 79 --> his variant of iso-1-cytochrome c.
Topics: Alkalies; Anaerobiosis; Cytochromes c; Electron Transport; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Lysine; Magnetic Resonance Spectroscopy; Mutant Proteins; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protons; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics | 2007 |
Heme levels switch the function of Hap1 of Saccharomyces cerevisiae between transcriptional activator and transcriptional repressor.
Topics: Aerobiosis; Anaerobiosis; Base Sequence; Binding Sites; Cytochrome P-450 Enzyme System; Cytochromes c; DNA-Binding Proteins; Gene Expression Regulation, Fungal; Genes, Fungal; Heme; HSP70 Heat-Shock Proteins; HSP90 Heat-Shock Proteins; Molecular Sequence Data; Nuclear Proteins; Oligonucleotide Array Sequence Analysis; Oxidoreductases; Promoter Regions, Genetic; Protein Binding; Repressor Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Trans-Activators; Transcription Factors; Transcription, Genetic | 2007 |
Mitochondrial resuscitation with exogenous cytochrome c in the septic heart.
Topics: Animals; Cytochromes c; Electron Transport Complex IV; Heme; Male; Mice; Mice, Inbred C57BL; Mitochondria, Heart; Oxidative Phosphorylation; Prospective Studies; Sepsis | 2007 |
Characterization of N-terminal amino group-heme ligation emerging upon guanidine hydrochloric acid induced unfolding of Hydrogenobacter thermophilus ferricytochrome c552.
Topics: Acids; Bacteria; Circular Dichroism; Cytochromes c; Guanidine; Heme; Hydrogen-Ion Concentration; Nuclear Magnetic Resonance, Biomolecular; Protein Denaturation; Spectrophotometry, Ultraviolet | 2008 |
Non-native heme-histidine ligation promotes microsecond time scale secondary structure formation in reduced horse heart cytochrome c.
Topics: Animals; Circular Dichroism; Cytochromes c; Guanidine; Heme; Histidine; Horses; Myocardium; Protein Folding; Protein Structure, Secondary; Spectrophotometry, Ultraviolet | 2007 |
Site-directed mutagenesis of five conserved residues of subunit i of the cytochrome cbb3 oxidase in Rhodobacter capsulatus.
Topics: Amino Acid Sequence; Amino Acids; Asparagine; Bacterial Proteins; Catalysis; Cytochromes c; Electron Transport Complex IV; Electrophoresis, Polyacrylamide Gel; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Subunits; Rhodobacter capsulatus; Sequence Homology, Amino Acid; Serine; Structure-Activity Relationship; Threonine | 2007 |
The hierarchy of structural transitions induced in cytochrome c by anionic phospholipids determines its peroxidase activation and selective peroxidation during apoptosis in cells.
Topics: Animals; Apoptosis; Cardiolipins; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Activation; Etoposide; Fluorescence; Heme; Humans; Mice; Peroxidase; Phosphatidic Acids; Phosphatidylcholines; Phosphatidylinositol 4,5-Diphosphate; Phosphatidylinositol Phosphates; Phosphatidylserines; Phospholipids; Protein Structure, Tertiary; Tryptophan | 2007 |
Fast folding kinetics and stabilization of apo-cytochrome c.
Topics: Bacterial Proteins; Cytochromes c; Enzyme Stability; Heme; Kinetics; Mutagenesis, Site-Directed; Protein Conformation; Protein Folding; Pseudomonas aeruginosa | 2008 |
Correlation of acid-induced conformational transition of ferricytochrome c with cyanide binding kinetics.
Topics: Acids; Animals; Circular Dichroism; Cyanides; Cytochromes c; Heme; Horses; Hydrogen-Ion Concentration; Iron; Kinetics; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry, Ultraviolet; Viscosity | 2008 |
How does reorganization energy change upon protein unfolding? Monitoring the structural perturbations in the heme cavity of cytochrome c.
Topics: Animals; Cytochromes c; Electrochemistry; Heme; Horses; Protein Denaturation; Protein Folding; Thermodynamics | 2008 |
Mutations in cytochrome b that affect kinetics of the electron transfer reactions at center N in the yeast cytochrome bc1 complex.
Topics: Amino Acid Sequence; Binding Sites; Cytochromes b; Cytochromes c; Electron Transport; Electron Transport Complex III; Heme; Kinetics; Ligands; Mitochondria; Models, Molecular; Molecular Sequence Data; Mutation; Oxidation-Reduction; Protein Binding; Protein Conformation; Proton-Motive Force; Quinone Reductases; Thermodynamics; Ubiquinone; Yeasts | 2008 |
Exogenous cytochrome C restores myocardial cytochrome oxidase activity into the late phase of sepsis.
Topics: Animals; Cytochromes c; Electron Transport Complex IV; Heart; Heme; Kinetics; Male; Mice; Mice, Inbred C57BL; Mitochondria; Myocardium; Oxidative Stress; Phosphorylation; Sepsis | 2008 |
Variants of the tetrahaem cytochrome c quinol dehydrogenase NrfH characterize the menaquinol-binding site, the haem c-binding motifs and the transmembrane segment.
Topics: Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Cells, Cultured; Cytochromes c; Desulfovibrio vulgaris; Genetic Variation; Heme; Membrane Proteins; Molecular Sequence Data; Naphthols; Nitrate Reductases; Oxidoreductases; Sequence Homology, Amino Acid; Terpenes; Wolinella | 2008 |
Ultrafast heme-residue bond formation in six-coordinate heme proteins: implications for functional ligand exchange.
Topics: Animals; Biochemistry; Cytochromes c; Drosophila; Escherichia coli; Globins; Haemophilus ducreyi; Heme; Hemeproteins; Horses; Humans; Ligands; Nerve Tissue Proteins; Neuroglobin; Oxygen; Spinacia oleracea; Superoxide Dismutase | 2008 |
Probing the bottom of a folding funnel using conformationally gated electron transfer reactions.
Topics: Cytochromes c; Electron Transport; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Mutation; Protein Conformation; Protein Folding | 2008 |
A novel pathway of cytochrome c biogenesis is involved in the assembly of the cytochrome b6f complex in arabidopsis chloroplasts.
Topics: Algal Proteins; Animals; Arabidopsis; Arabidopsis Proteins; Chlamydomonas; Chloroplasts; Cytochrome b6f Complex; Cytochromes c; Heme; Mutagenesis, Insertional; Mutation; Plant Proteins; Protein Transport; Protozoan Proteins | 2008 |
Internal electric field in cytochrome C explored by visible electronic circular dichroism spectroscopy.
Topics: Animals; Cattle; Circular Dichroism; Cytochromes c; Electrochemistry; Electronics; Heme; Horses; Hydrogen-Ion Concentration; Models, Statistical; Molecular Conformation; Myocardium; Oxygen; Yeasts | 2008 |
The cytochrome c maturation components CcmF, CcmH, and CcmI form a membrane-integral multisubunit heme ligation complex.
Topics: Cell Membrane; Chromatography; Chromatography, Affinity; Cytochromes c; Detergents; Epitopes; Genetic Techniques; Heme; Models, Biological; Multiprotein Complexes; Mutation; Photosynthesis; Plasmids; Protein Structure, Tertiary; Rhodobacter capsulatus | 2008 |
A cytochrome c containing nitrate reductase plays a role in electron transport for denitrification in Thermus thermophilus without involvement of the bc respiratory complex.
Topics: Anaerobiosis; Artificial Gene Fusion; Bacterial Proteins; beta-Galactosidase; Cytochromes c; Electron Transport; Genes, Reporter; Heme; Microbial Viability; Models, Biological; Mutation; NAD; Nitrate Reductase; Nitrates; Nitric Oxide; Nitrites; Nitrogen; Oxidation-Reduction; Thermus thermophilus | 2008 |
Early structural evolution of native cytochrome c after solvent removal.
Topics: Computer Simulation; Cytochromes c; Heme; Hydrogen Bonding; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Protein Denaturation; Protein Structure, Tertiary; Solvents | 2008 |
A novel type of monoheme cytochrome c: biochemical and structural characterization at 1.23 A resolution of rhodothermus marinus cytochrome c.
Topics: Aerobiosis; Anaerobiosis; Bacterial Proteins; Crystallography, X-Ray; Cytochromes c; Electron Transport; Heme; Protein Structure, Secondary; Protein Structure, Tertiary; Rhodothermus | 2008 |
The haem-copper oxygen reductase of Desulfovibrio vulgaris contains a dihaem cytochrome c in subunit II.
Topics: Amino Acid Sequence; Cell Membrane; Copper; Cytochrome c Group; Cytochromes c; Desulfovibrio vulgaris; Electrons; Heme; Molecular Sequence Data; Multigene Family; Oxidoreductases; Oxygen; Protein Structure, Tertiary; Protein Subunits; Sequence Alignment; Sequence Analysis, Protein | 2008 |
The solution structure of a tetraheme cytochrome from Shewanella frigidimarina reveals a novel family structural motif.
Topics: Amino Acid Motifs; Bacterial Proteins; Cytochromes c; Desulfovibrio; Heme; Iron; Oxidation-Reduction; Oxides; Protein Folding; Shewanella; Species Specificity | 2008 |
Stability enhancement of cytochrome c through heme deprotonation and mutations.
Topics: Bacterial Proteins; Cytochromes c; Guanidine; Heme; Hydrogen Bonding; Hydrogen-Ion Concentration; Mutation; Protein Denaturation; Protein Stability; Protons; Pseudomonas aeruginosa | 2009 |
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 |
Analysis of the electrochemistry of hemes with E(m)s spanning 800 mV.
Topics: Algorithms; Cytochromes c; Electrochemistry; Energy Transfer; Heme; Hemeproteins; Kinetics; Ligands; Models, Molecular; Oxidation-Reduction; Protein Conformation; Static Electricity | 2009 |
Avoidance of the cytochrome c biogenesis system by periplasmic CXXCH motifs.
Topics: Amino Acid Motifs; Amino Acid Sequence; Cytochromes c; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Heme; Molecular Sequence Data; Oxidoreductases; Periplasm; Protein Disulfide-Isomerases; Recombinant Fusion Proteins; Spectrophotometry, Ultraviolet | 2008 |
Stability of the heme Fe-N-terminal amino group coordination bond in denatured cytochrome c.
Topics: Amino Acid Sequence; Aquifoliaceae; Cytochromes c; Electrons; Guanidine; Heme; Histidine; Iron; Magnetic Resonance Spectroscopy; Mutation; Nitrogen; Oxidation-Reduction; Protein Denaturation; Pseudomonas aeruginosa | 2009 |
Variant c-type cytochromes as probes of the substrate specificity of the E. coli cytochrome c maturation (Ccm) apparatus.
Topics: Amino Acid Motifs; Cysteine; Cytochrome b Group; Cytochromes c; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Heme; Magnetic Resonance Spectroscopy; Protein Binding; Protein Processing, Post-Translational; Spectrometry, Mass, Electrospray Ionization; Substrate Specificity | 2009 |
Competition between reversible aggregation and loop formation in denatured iso-1-cytochrome c.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cytochromes c; Enzyme Stability; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Ligands; Models, Chemical; Molecular Sequence Data; Mutation; Protein Binding; Protein Denaturation; Protein Multimerization; Protein Renaturation; Protein Structure, Secondary; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Temperature | 2009 |
Probing 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 |
Ultrafast proteinquake dynamics in cytochrome c.
Topics: Animals; Cytochromes c; Ferric Compounds; Ferrous Compounds; Heme; Horses; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Photolysis; Protein Conformation; Spectrophotometry, Ultraviolet; Thermodynamics; Tryptophan | 2009 |
Cytochrome C mutants for superoxide biosensors.
Topics: Biosensing Techniques; Circular Dichroism; Cytochromes c; Electrochemistry; Electrodes; Heme; Humans; Iron; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Mutant Proteins; Mutation; Protein Conformation; Protein Folding; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Superoxides | 2009 |
Catalytic reduction of O2 by cytochrome C using a synthetic model of cytochrome C oxidase.
Topics: Animals; Biomimetics; Catalysis; Catalytic Domain; Copper; Cytochromes c; Electron Transport; Electron Transport Complex IV; Ferric Compounds; Heme; Horses; Imidazoles; Kinetics; Oxidation-Reduction; Oxygen; Water | 2009 |
His protects heme as it crosses the membrane.
Topics: Biological Transport; Catalysis; Cell Membrane; Chloroplasts; Cytochromes c; Heme; Histidine | 2009 |
Kinetics of cyanide binding as a probe of local stability/flexibility of cytochrome c.
Topics: Animals; Circular Dichroism; Cyanides; Cytochromes c; Heme; Horses; Iron; Kinetics; Protein Binding; Thermodynamics | 2009 |
Superoxide radical protects liposome-contained cytochrome c against oxidative damage promoted by peroxynitrite and free radicals.
Topics: Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Lipid Peroxidation; Nitrosation; Oxidation-Reduction; Oxidative Stress; Peroxidase; Peroxynitrous Acid; Protein Processing, Post-Translational; Protein Structure, Secondary; Spectrophotometry; Superoxides; Tryptophan; Unilamellar Liposomes | 2009 |
A conserved haem redox and trafficking pathway for cofactor attachment.
Topics: Amino Acid Sequence; Bacterial Outer Membrane Proteins; Binding Sites; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Hydroquinones; Iron; Lyases; Oxidation-Reduction; Protein Binding | 2009 |
Microperoxidase 11: a model system for porphyrin networks and heme-protein interactions.
Topics: Animals; Circular Dichroism; Cytochromes c; Heme; Horses; Peroxidases; Porphyrins; Protein Conformation; Spectrum Analysis, Raman; Temperature | 2009 |
Haem-delivery proteins in cytochrome c maturation System II.
Topics: Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Carrier Proteins; Cytochromes c; Escherichia coli; Helicobacter; Heme; Heme-Binding Proteins; Hemeproteins; Molecular Sequence Data; Recombinant Proteins | 2009 |
Graphene oxide-facilitated electron transfer of metalloproteins at electrode surfaces.
Topics: Animals; Cytochromes c; Electrochemistry; Electrodes; Electron Transport; Graphite; Heme; Horseradish Peroxidase; Metalloproteins; Models, Molecular; Myoglobin; Oxides; Protein Conformation; Surface Properties | 2010 |
On the mechanism of SDS-induced protein denaturation.
Topics: Cytochromes c; Detergents; Heme; Hydrogen-Ion Concentration; Micelles; Models, Molecular; Oxidation-Reduction; Protein Denaturation; Protein Structure, Secondary; Protein Structure, Tertiary; Sodium Dodecyl Sulfate; Spectrophotometry | 2010 |
Structural characterization of a family of cytochromes c(7) involved in Fe(III) respiration by Geobacter sulfurreducens.
Topics: Amino Acid Sequence; Cell Respiration; Cloning, Molecular; Crystallization; Crystallography, X-Ray; Cytochromes c; Ferric Compounds; Geobacter; Heme; Hydrogen Bonding; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid | 2010 |
Molecular basis for the electric field modulation of cytochrome C structure and function.
Topics: Apoptosis; Cytochromes c; Heme; Ligands; Molecular Dynamics Simulation; Oxidation-Reduction; Peroxidases; Protein Conformation; Static Electricity; Thermodynamics | 2009 |
Iron regulation through the back door: iron-dependent metabolite levels contribute to transcriptional adaptation to iron deprivation in Saccharomyces cerevisiae.
Topics: 3-Isopropylmalate Dehydrogenase; CCAAT-Binding Factor; Ceruloplasmin; Cytochromes c; DNA-Binding Proteins; Down-Regulation; Ferrochelatase; Gene Expression; Gene Expression Regulation, Fungal; Heme; Homeostasis; Hydro-Lyases; Iron; Iron Chelating Agents; Iron Deficiencies; Isomerases; Malates; Peroxidases; Phenanthrolines; Promoter Regions, Genetic; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Terminator Regions, Genetic; Trans-Activators; Transcription Factors; Tristetraprolin; Up-Regulation | 2010 |
Comparing the substrate specificities of cytochrome c biogenesis Systems I and II: bioenergetics.
Topics: Bacterial Outer Membrane Proteins; Cytochrome c Group; Cytochromes c; Energy Metabolism; Escherichia coli Proteins; Helicobacter pylori; Heme; Multienzyme Complexes; Paracoccus denitrificans; Protein Processing, Post-Translational; Substrate Specificity | 2010 |
Electron transfer properties and hydrogen peroxide electrocatalysis of cytochrome c variants at positions 67 and 80.
Topics: Amino Acid Substitution; Catalysis; Cytochromes c; Electrochemical Techniques; Electron Transport; Heme; Hydrogen Bonding; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Thermodynamics | 2010 |
Crystal structure of the electron carrier domain of the reaction center cytochrome c(z) subunit from green photosynthetic bacterium Chlorobium tepidum.
Topics: Chlorobi; Chlorobium; Crystallography, X-Ray; Cytochromes c; Electron Transport; Heme; Oxidation-Reduction; Protein Structure, Tertiary; Protein Subunits | 2010 |
Maturation of a eukaryotic cytochrome c in the cytoplasm of Escherichia coli without the assistance by a dedicated biogenesis apparatus.
Topics: Animals; Cytochromes c; Electron Transport Complex IV; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Heme; Horses | 2010 |
Aberrant attachment of heme to cytochrome by the Ccm system results in a cysteine persulfide linkage.
Topics: Cysteine; Cytochromes c; Disulfides; Escherichia coli; Escherichia coli Proteins; Heme; Models, Molecular | 2010 |
Time-dependant protective effects of mangenese(III) tetrakis (1-methyl-4-pyridyl) porphyrin on mitochondrial function following renal ischemia-reperfusion injury.
Topics: Aconitate Hydratase; Animals; Antioxidants; Apoptosis; Apoptosis Regulatory Proteins; Carrier Proteins; Caspase 3; Cytochromes c; Drug Evaluation, Preclinical; Electron Spin Resonance Spectroscopy; Heme; In Situ Nick-End Labeling; Kidney; Male; Metalloporphyrins; Mitochondria; Mitochondrial Proteins; Oxidation-Reduction; Oxidative Stress; Rats; Rats, Sprague-Dawley; Reactive Oxygen Species; Reperfusion Injury; Superoxide Dismutase; Time Factors | 2010 |
Nitric oxide binds to the proximal heme coordination site of the ferrocytochrome c/cardiolipin complex: formation mechanism and dynamics.
Topics: Binding Sites; Cardiolipins; Cytochromes c; Heme; Kinetics; Nitric Oxide; Protein Binding; Spectrophotometry; Time Factors | 2010 |
Direct electrochemistry of cytochrome c at modified Si(100) electrodes.
Topics: Animals; Azides; Cytochromes c; Electrodes; Electron Transport; Heme; Horses; Kinetics; Ligands; Molecular Structure; Protein Binding; Proteins; Silicon; Surface Properties | 2010 |
Purification and characterization of OmcZ, an outer-surface, octaheme c-type cytochrome essential for optimal current production by Geobacter sulfurreducens.
Topics: Binding Sites; Bioelectric Energy Sources; Cytochromes c; Electricity; Electron Transport; Geobacter; Heme; Hot Temperature; Molecular Sequence Data; Molecular Weight; Oxidation-Reduction; Protein Binding; Protein Stability; Sequence Alignment; Sequence Analysis, Protein | 2010 |
c-Type cytochrome biogenesis can occur via a natural Ccm system lacking CcmH, CcmG, and the heme-binding histidine of CcmE.
Topics: Amino Acid Sequence; Bacterial Proteins; Cytochromes c; Desulfovibrio desulfuricans; Escherichia coli; Gene Deletion; Genome, Bacterial; Heme; Histidine; Models, Molecular; Molecular Sequence Data; Protein Conformation; Solubility | 2010 |
Denatured states of low-complexity polypeptide sequences differ dramatically from those of foldable sequences.
Topics: Cytochromes c; Heme; Histidine; Histones; Hydrogen-Ion Concentration; Kinetics; Molecular Conformation; Peptides; Protein Conformation; Protein Denaturation; Protein Folding; Proteins; Rhodopseudomonas; Thermodynamics | 2010 |
Characterization of the decaheme c-type cytochrome OmcA in solution and on hematite surfaces by small angle x-ray scattering and neutron reflectometry.
Topics: Anthraquinones; Cytochromes c; Ferric Compounds; Flavins; Heme; Ligands; Models, Molecular; Neutron Diffraction; Nitrilotriacetic Acid; Oxidation-Reduction; Protein Conformation; Scattering, Small Angle; Shewanella; Solutions; Structure-Activity Relationship; Surface Properties; Water; X-Ray Diffraction | 2010 |
NMR and DFT investigation of heme ruffling: functional implications for cytochrome c.
Topics: Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Models, Theoretical; Nuclear Magnetic Resonance, Biomolecular | 2010 |
The CcmC:heme:CcmE complex in heme trafficking and cytochrome c biosynthesis.
Topics: Amino Acid Substitution; Bacterial Outer Membrane Proteins; Bacterial Proteins; Binding Sites; Biological Transport; Cytochromes c; Escherichia coli Proteins; Heme; Hemeproteins; Membrane Proteins; Multiprotein Complexes; Protein Binding; Protein Transport | 2010 |
CCS5, a thioredoxin-like protein involved in the assembly of plastid c-type cytochromes.
Topics: Animals; Arabidopsis; Arabidopsis Proteins; Binding Sites; Chlamydomonas reinhardtii; Cytochromes c; Cytochromes c6; Cytochromes f; Heme; Mutation; Oxidation-Reduction; Protozoan Proteins; Thioredoxins; Thylakoids | 2010 |
Variation and analysis of second-sphere interactions and axial histidinate character in c-type cytochromes.
Topics: Amino Acid Motifs; Bacteria; Binding Sites; Cytochromes c; Heme; Histidine; Hydrogen Bonding; Iron; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Binding | 2010 |
The off-pathway status of the alkali molten globule is unrelated to heme misligation and trans-pH effects: experiments with ferrocytochrome c.
Topics: Alkalies; Cytochromes c; Heme; Hydrogen-Ion Concentration; Kinetics; Ligands; Protein Folding | 2010 |
c-type cytochrome assembly in Saccharomyces cerevisiae: a key residue for apocytochrome c1/lyase interaction.
Topics: Binding Sites; Carrier Proteins; Cytochromes c; Electron Transport; Electrophoresis, Polyacrylamide Gel; Gene Expression Regulation, Fungal; Heme; Lyases; Mitochondria; Mitochondrial Proteins; Mutation; Oxidation-Reduction; Polymerase Chain Reaction; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 2010 |
DsrJ, an essential part of the DsrMKJOP transmembrane complex in the purple sulfur bacterium Allochromatium vinosum, is an unusual triheme cytochrome c.
Topics: Bacterial Proteins; Catalysis; Chromatiaceae; Cytochrome c Group; Cytochromes c; Desulfovibrio vulgaris; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; Mutagenesis, Site-Directed; Oxidation-Reduction; Sulfur | 2010 |
Molecular dynamics simulations of cytochrome c unfolding in AOT reverse micelles: The first steps.
Topics: Binding Sites; Cytochromes c; Dioctyl Sulfosuccinic Acid; Heme; Micelles; Molecular Dynamics Simulation; Protein Denaturation; Protein Structure, Secondary; Protein Unfolding; Solutions; Time Factors; Water | 2010 |
Rate of oxidative modification of cytochrome c by hydrogen peroxide is modulated by Hofmeister anions.
Topics: Amino Acids, Aromatic; Animals; Biophysical Phenomena; Catalase; Circular Dichroism; Cytochromes c; Heme; Horses; Hydrogen Peroxide; In Vitro Techniques; Kinetics; Myocardium; Oxidation-Reduction; Protein Stability; Protein Structure, Secondary; Spectrophotometry | 2010 |
Redox and electrocatalytic properties of mimochrome VI, a synthetic heme peptide adsorbed on gold.
Topics: Adsorption; Amino Acid Sequence; Catalysis; Cytochromes c; Deuteroporphyrins; Electrochemistry; Electrodes; Gold; Heme; Metalloproteins; Molecular Conformation; Molecular Sequence Data; Oxidation-Reduction; Oxygen; Peptides; Protein Conformation | 2010 |
Structural basis of biological N2O generation by bacterial nitric oxide reductase.
Topics: Amino Acid Sequence; Bacterial Proteins; Catalytic Domain; Crystallography, X-Ray; Cytochromes c; Electron Transport; Electron Transport Complex IV; Heme; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Iron; Membrane Proteins; Models, Molecular; Molecular Sequence Data; Nitric Oxide; Nitrous Oxide; Oxidation-Reduction; Oxidoreductases; Protein Conformation; Protein Multimerization; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Subunits; Protons; Pseudomonas aeruginosa | 2010 |
Changes in optical properties of rat cerebral cortical slices during oxygen glucose deprivation.
Topics: Absorption; Animals; Brain Ischemia; Cerebral Cortex; Cerebrospinal Fluid; Cytochromes c; Electron Transport Complex IV; Glucose; Heme; In Vitro Techniques; Light; Male; Models, Biological; Monte Carlo Method; Oxygen; Rats; Rats, Wistar; Scattering, Radiation; Spectrophotometry | 2010 |
Ascorbate peroxidase activity of cytochrome c.
Topics: Animals; Apoptosis; Ascorbic Acid; Cardiolipins; Cattle; Cytochrome-c Peroxidase; Cytochromes c; Free Radicals; Guanidine; Heme; Horses; Hydrogen Peroxide; Iron; Kinetics; Methylation; Mitochondria, Heart; Signal Transduction; Spectrum Analysis; Yeasts | 2011 |
Structure of a novel dodecaheme cytochrome c from Geobacter sulfurreducens reveals an extended 12 nm protein with interacting hemes.
Topics: Bacterial Proteins; Cytochromes c; Geobacter; Heme; Protein Structure, Secondary | 2011 |
Biochemistry. Catalyzing NO to N2O in the nitrogen cycle.
Topics: Bacterial Proteins; Catalytic Domain; Crystallography, X-Ray; Cytochrome b Group; Cytochromes c; Electron Transport; Electron Transport Complex IV; Evolution, Molecular; Heme; Hydrophobic and Hydrophilic Interactions; Models, Molecular; Nitric Oxide; Nitrogen Cycle; Nitrous Oxide; Oxidation-Reduction; Oxidoreductases; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Subunits; Protons; Pseudomonas aeruginosa | 2010 |
Production of recombinant multiheme cytochromes c in Wolinella succinogenes.
Topics: Bacterial Proteins; Cytochrome c Group; Cytochromes a1; Cytochromes c; Cytochromes c1; Denitrification; Heme; Lyases; Nitrate Reductases; Nitrification; Oxidoreductases; Recombinant Proteins; Transformation, Bacterial; Wolinella | 2011 |
The proapoptotic G41S mutation to human cytochrome c alters the heme electronic structure and increases the electron self-exchange rate.
Topics: Apoptosis; Coenzymes; Crystallography, X-Ray; Cytochromes c; Electrons; Heme; Humans; Models, Molecular; Mutation; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Conformation; Quantum Theory | 2011 |
A novel component of the disulfide-reducing pathway required for cytochrome c assembly in plastids.
Topics: Amino Acid Sequence; Chlamydomonas reinhardtii; Chloroplasts; Cytochrome c Group; Cytochromes c; Cytochromes f; Disulfides; Heme; Molecular Sequence Data; Mutant Proteins; Oxidation-Reduction; Photosynthesis; Plastids; Thylakoids | 2011 |
Effects of heme on the thermal stability of mesophilic and thermophilic cytochromes c: comparison between experimental and theoretical results.
Topics: Apolipoproteins; Cytochromes c; Entropy; Heme; Models, Molecular; Protein Conformation; Temperature; Water | 2011 |
Molecular interactions between multihaem cytochromes: probing the protein-protein interactions between pentahaem cytochromes of a nitrite reductase complex.
Topics: Amino Acid Sequence; Cytochrome c Group; Cytochromes; Cytochromes c; Dimerization; Escherichia coli Proteins; Heme; Models, Molecular; Molecular Sequence Data; Multiprotein Complexes; Nitrite Reductases; Oxidation-Reduction; Protein Conformation; Protein Interaction Mapping; Sequence Alignment | 2011 |
Principles and patterns in the interaction between mono-heme cytochrome c and its partners in electron transfer processes.
Topics: Animals; Cytochromes c; Electron Transport; Heme; Humans; Models, Molecular; Protein Conformation; Protein Interaction Domains and Motifs; Protein Interaction Mapping | 2011 |
A small fluorophore reporter of protein conformation and redox state.
Topics: Cytochromes c; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Heme; Kinetics; Oxidation-Reduction; Phthalic Acids; Protein Folding; Protein Structure, Tertiary; Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Vinculin | 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 |
Heterologous synthesis of cytochrome c' by Escherichia coli is not dependent on the System I cytochrome c biogenesis machinery.
Topics: Amino Acid Sequence; Chromatiaceae; Cytochromes c; Cytochromes c'; Escherichia coli; Heme; Hydrogenophilaceae; Molecular Sequence Data; Periplasm; Sequence Homology, Amino Acid | 2011 |
Binding conformation prediction between human acetylcholinesterase and cytochrome c using molecular modeling methods.
Topics: Acetylcholinesterase; Amino Acid Sequence; Anions; Apoptosomes; Binding Sites; Crystallography, X-Ray; Cytochromes c; Heme; Humans; Hydrogen Bonding; Models, Chemical; Models, Molecular; Molecular Dynamics Simulation; Protein Binding; Protein Conformation; Protein Interaction Mapping; Protein Structure, Quaternary; Sequence Alignment | 2011 |
The mitochondrial cytochrome c N-terminal region is critical for maturation by holocytochrome c synthase.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Cytochromes c; Heme; Holoenzymes; Lyases; Mitochondrial Proteins; Substrate Specificity | 2011 |
Highly selective ligand binding by Methylophilus methylotrophus cytochrome c''.
Topics: Bacterial Proteins; Cytochromes c; Diatoms; Disulfides; Ferrous Compounds; Heme; Histidine; Ligands; Methylophilus methylotrophus; Nitric Oxide; Oxidation-Reduction; Protein Binding | 2011 |
Electron transfer function versus oxygen delivery: a comparative study for several hexacoordinated globins across the animal kingdom.
Topics: Amino Acid Sequence; Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Carbon Monoxide; Cytochromes c; Cytoglobin; Electron Transport; Globins; Heme; Histidine; Humans; Iron; Kinetics; Nerve Tissue Proteins; Neuroglobin; Oxygen; Protein Structure, Quaternary; Protein Structure, Tertiary | 2011 |
Electrochemical titrations and reaction time courses monitored in situ by magnetic circular dichroism spectroscopy.
Topics: Animals; Azurin; Circular Dichroism; Copper; Cytochromes c; Electrochemical Techniques; Heme; Horses; Magnetics; Oxidation-Reduction; Paracoccus pantotrophus; Time Factors; Titrimetry | 2011 |
Mitochondrial cytochrome c synthase: CP motifs are not necessary for heme attachment to apocytochrome c.
Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Conserved Sequence; Cytochromes c; Heme; Humans; Lyases; Mice; Mitochondria; Mitochondrial Diseases; Molecular Sequence Data; Mutation; Protein Binding; Saccharomyces cerevisiae | 2011 |
Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III.
Topics: Amino Acid Sequence; Apoproteins; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Gene Deletion; Gene Expression; Heme; Humans; Lyases; Maltose-Binding Proteins; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Peptide Fragments; Periplasmic Proteins; Protein Disulfide-Isomerases; Protein Sorting Signals; Recombinant Fusion Proteins; Sulfhydryl Compounds | 2012 |
The effects of ATP and sodium chloride on the cytochrome c-cardiolipin interaction: the contrasting behavior of the horse heart and yeast proteins.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Animals; Cardiolipins; Cattle; Cytochromes c; Heme; Horses; Models, Molecular; Molecular Sequence Data; Multiprotein Complexes; Osmolar Concentration; Protein Binding; Protein Multimerization; Protein Stability; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sodium Chloride; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Titrimetry | 2011 |
CcmI subunit of CcmFHI heme ligation complex functions as an apocytochrome c chaperone during c-type cytochrome maturation.
Topics: Amino Acid Sequence; Binding Sites; Cell Membrane; Cytochromes c; Cytochromes c2; Epitopes; Heme; Models, Molecular; Molecular Chaperones; Molecular Sequence Data; Peptide Fragments; Periplasm; Protein Binding; Protein Processing, Post-Translational; Protein Structure, Secondary; Protein Subunits; Rhodobacter capsulatus; Substrate Specificity | 2011 |
Solution to living cell spectroscopy challenge.
Topics: Cytochromes c; Electron Transport; Heme; Oxidation-Reduction; Oxidative Stress; Spectrophotometry, Ultraviolet; Spectrum Analysis | 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 |
Direct observation of vibrational energy flow in cytochrome c.
Topics: Animals; Cattle; Cytochromes c; Heme; Kinetics; Models, Molecular; Spectrum Analysis, Raman; Ultraviolet Rays | 2011 |
Femtosecond UV studies of the electronic relaxation processes in Cytochrome c.
Topics: Animals; Cytochromes c; Electrons; Energy Transfer; Heme; Horses; Oxidation-Reduction; Spectrophotometry, Ultraviolet; Time Factors; Tryptophan | 2011 |
Modulation of ligand-field parameters by heme ruffling in cytochromes c revealed by EPR spectroscopy.
Topics: Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Ligands; Models, Molecular; Protein Conformation; Pseudomonas aeruginosa | 2011 |
Probing a complex of cytochrome c and cardiolipin by magnetic circular dichroism spectroscopy: implications for the initial events in apoptosis.
Topics: Animals; Apoptosis; Cardiolipins; Circular Dichroism; Cytochromes c; Heme; Horses; Models, Molecular; Oxidation-Reduction; Potentiometry; Protein Binding; Protein Conformation | 2011 |
A pivotal heme-transfer reaction intermediate in cytochrome c biogenesis.
Topics: Bacterial Outer Membrane Proteins; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Multiprotein Complexes; Protein Biosynthesis | 2012 |
A distal pocket Leu residue inhibits the binding of O2 and NO at the distal heme site of cytochrome c'.
Topics: Alcaligenes; Binding Sites; Cytochromes c; Heme; Leucine; Nitric Oxide; Oxygen; Point Mutation | 2012 |
Surface multiheme c-type cytochromes from Thermincola potens and implications for respiratory metal reduction by Gram-positive bacteria.
Topics: Chromatography, Liquid; Cytochromes c; Gram-Positive Bacteria; Heme; Hydrogen-Ion Concentration; Metals; Microscopy, Electron, Transmission; Oxidation-Reduction; Peptococcaceae; Tandem Mass Spectrometry | 2012 |
Spectroscopic characterization of (57)Fe-enriched cytochrome c.
Topics: Cytochromes c; Ferrous Compounds; Heme; Hydrochloric Acid; Iron Isotopes; Models, Molecular; Oxidation-Reduction; Spectroscopy, Mossbauer; Spectrum Analysis, Raman; Vibration | 2012 |
Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors.
Topics: Amino Acid Sequence; Bacterial Proteins; Chemoautotrophic Growth; Copper; Cyanides; Cytochromes c; Electron Transport; Electron Transport Complex IV; Electrons; Energy Metabolism; Heme; Molecular Sequence Data; Multienzyme Complexes; Oxidation-Reduction; Protein Subunits; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Ubiquinone | 2012 |
Redox active molecules cytochrome c and vitamin C enhance heme-enzyme peroxidations by serving as non-specific agents for redox relay.
Topics: Antioxidants; Ascorbic Acid; Chloride Peroxidase; Cytochromes c; Heme; Horseradish Peroxidase; Oxidation-Reduction | 2012 |
Modeling and computations of the intramolecular electron transfer process in the two-heme protein cytochrome c(4).
Topics: Cytochromes c; Electron Transport; Heme; Molecular Dynamics Simulation; Oxidation-Reduction; Protein Structure, Tertiary; Pseudomonas stutzeri; Quantum Theory | 2012 |
Solution NMR structure, backbone dynamics, and heme-binding properties of a novel cytochrome c maturation protein CcmE from Desulfovibrio vulgaris.
Topics: Bacterial Outer Membrane Proteins; Cytochromes c; Desulfovibrio vulgaris; Heme; Hemeproteins; Magnetic Resonance Spectroscopy; Protein Structure, Tertiary | 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 |
Horse heart cytochrome c entrapped into the hydrated liquid-crystalline phases of phytantriol: X-ray diffraction and Raman spectroscopic characterization.
Topics: Animals; Cytochromes c; Enzymes, Immobilized; Fatty Alcohols; Heme; Horses; Liquid Crystals; Muscle Proteins; Myocardium; Nanostructures; Spectrum Analysis, Raman; X-Ray Diffraction | 2012 |
Cytochrome C as an amplifier of ROS release in mitochondria.
Topics: Animals; Apoptosis; Calcium; Cyclosporine; Cytochromes c; Electron Transport; Fluorescent Dyes; Heme; Iron; Liver; Mitochondria, Liver; Mitochondrial Membrane Transport Proteins; Mitochondrial Permeability Transition Pore; Oxidation-Reduction; Oxygen; Rats; Rats, Wistar; Reactive Oxygen Species; Tissue Extracts | 2012 |
Heme-protein vibrational couplings in cytochrome c provide a dynamic link that connects the heme-iron and the protein surface.
Topics: Bacteria; Catalytic Domain; Cytochromes c; Heme; Iron; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Dynamics Simulation; Molecular Structure; Vibration | 2012 |
Ligand binding, reactivity and biological activity of a distal pocket mutant of neuroglobin.
Topics: Apoptosis; Carbon Monoxide; Caspase 9; Cell Line; Cytochromes c; Enzyme Activation; Globins; Heme; Humans; Ligands; Mutant Proteins; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Oxygen; Protein Binding; Protein Conformation | 2012 |
Isolation and preliminary characterization of new cytochrome c from autotrophic haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio nitratireducens.
Topics: Amino Acid Sequence; Bacterial Proteins; Circular Dichroism; Cytochromes c; Ectothiorhodospiraceae; Electron Spin Resonance Spectroscopy; Heme; Molecular Sequence Data; Molecular Weight; Oxidation-Reduction; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sulfur | 2012 |
Maintenance of the secondary structure of horse cytochrome c during the conversion process of monomers to oligomers by addition of ethanol.
Topics: Animals; Chemical Precipitation; Chromatography, Gel; Circular Dichroism; Cytochromes c; Ethanol; Heme; Horses; Magnetic Resonance Spectroscopy; Microscopy, Electron, Transmission; Oxidation-Reduction; Particle Size; Protein Binding; Protein Multimerization; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Unfolding; Solubility | 2012 |
Probing why trypanosomes assemble atypical cytochrome c with an AxxCH haem-binding motif instead of CxxCH.
Topics: Amino Acid Motifs; Base Sequence; Binding Sites; Crithidia fasciculata; Cytochromes c; DNA Primers; Electron Transport; Evolution, Molecular; Heme; Protozoan Proteins; Recombinant Proteins; Spectrometry, Mass, Electrospray Ionization; Trypanosoma brucei brucei | 2012 |
Heme plane orientation dependent direct electron transfer of cytochrome c at SAMs/Au electrodes with different wettability.
Topics: Adsorption; Cytochromes c; Electrochemistry; Electrodes; Gold; Heme; Surface Properties; Wettability | 2012 |
Role of Met(58) in the regulation of electron/proton transfer in trihaem cytochrome PpcA from Geobacter sulfurreducens.
Topics: Bacterial Proteins; Cytochromes c; Electron Transport; Escherichia coli; Geobacter; Heme; Hydrogen-Ion Concentration; Lysine; Magnetic Resonance Spectroscopy; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Solutions; Thermodynamics | 2012 |
Domain swapping of the heme and N-terminal α-helix in Hydrogenobacter thermophilus cytochrome c(552) dimer.
Topics: Animals; Bacteria; Crystallography, X-Ray; Cytochrome c Group; Cytochromes c; Heme; Horses; Models, Molecular; Protein Stability; Protein Structure, Secondary; Protein Structure, Tertiary; Thermodynamics | 2012 |
Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp.
Topics: Aminoacyltransferases; Bacterial Proteins; Biophysical Phenomena; Chemistry Techniques, Analytical; Cysteine Endopeptidases; Cytochromes c; Electrophoresis, Polyacrylamide Gel; Heme; Kinetics; Maltose; Maltose-Binding Proteins; Point Mutation; Protein Binding; Protein Denaturation; Protein Folding; Protein Stability; Protein Structure, Tertiary; Protein Unfolding; Proteins; Proteolysis; Reproducibility of Results; Temperature; Thermolysin | 2012 |
Versatility of non-native forms of human cytochrome c: pH and micellar concentration dependence.
Topics: Cytochromes c; Heme; Humans; Hydrogen-Ion Concentration; Ligands; Micelles; Molecular Dynamics Simulation; Mutation; Phospholipids; Protein Conformation; Sodium Dodecyl Sulfate | 2013 |
Detection and identification of heme c-modified peptides by histidine affinity chromatography, high-performance liquid chromatography-mass spectrometry, and database searching.
Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Bacterial Proteins; Betaproteobacteria; Cattle; Chromatography, Affinity; Chromatography, High Pressure Liquid; Cytochromes c; Databases, Protein; Escherichia coli; Heme; Histidine; Ions; Molecular Sequence Data; Peptide Mapping; Peptides; Search Engine; Signal-To-Noise Ratio; Tandem Mass Spectrometry | 2012 |
His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosis.
Topics: Apoptosis; Circular Dichroism; Cytochromes c; Heme; Histidine; Models, Molecular; Protons; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman | 2012 |
Human mitochondrial holocytochrome c synthase's heme binding, maturation determinants, and complex formation with cytochrome c.
Topics: Amino Acid Sequence; Bacterial Proteins; Cytochromes c; Heme; Histidine; Humans; Ligands; Lyases; Mitochondria; Models, Molecular; Molecular Sequence Data; Protein Binding; Rhodobacter capsulatus; Spectrophotometry, Ultraviolet | 2013 |
Elucidating the mechanism of ferrocytochrome c heme disruption by peroxidized cardiolipin.
Topics: Animals; Apoproteins; Cardiolipins; Cattle; Cytochromes c; Heme; Kinetics; Lipid Peroxidation; Oxidation-Reduction; Protein Binding; Protein Multimerization; Protein Structure, Quaternary | 2013 |
Conformational properties of polyglutamine sequences in guanidine hydrochloride solutions.
Topics: Alanine; Amino Acid Sequence; Cytochromes c; Guanidine; Heme; Histidine; Lysine; Molecular Sequence Data; Mutagenesis, Insertional; Peptides; Protein Denaturation; Protein Stability; Protein Structure, Tertiary | 2012 |
Clarification of a peak at m/z 1634 from tryptically digested cytochrome c.
Topics: Amino Acid Sequence; Chromatography, High Pressure Liquid; Cytochromes c; Heme; Ions; Molecular Sequence Data; Peptide Fragments; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Trypsin | 2012 |
Recombinant expression, biophysical characterization, and cardiolipin-induced changes of two Caenorhabditis elegans cytochrome c proteins.
Topics: Amino Acid Sequence; Animals; Caenorhabditis elegans Proteins; Cardiolipins; Conserved Sequence; Cytochromes c; Escherichia coli; Fluorescence Resonance Energy Transfer; Guaiacol; Heme; Horses; Kinetics; Liposomes; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Peroxidases; Protein Binding; Protein Stability; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Unfolding; Recombinant Proteins; Sequence Analysis, Protein; Spectrophotometry, Ultraviolet; Thermodynamics | 2013 |
Mutation of trimethyllysine 72 to alanine enhances His79-heme-mediated dynamics of iso-1-cytochrome c.
Topics: Alanine; Amino Acid Substitution; Cytochromes c; Heme; Hydrogen-Ion Concentration; Kinetics; Lysine; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Stability; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics | 2013 |
Multifaceted effects of ATP on cardiolipin-bound cytochrome c.
Topics: Adenosine Triphosphate; Animals; Apoptosis; Cardiolipins; Cytochromes c; Heme; Horses; Liposomes; Models, Molecular; Oxidation-Reduction; Peroxidase; Protein Binding; Protein Conformation; Spectrometry, Fluorescence | 2013 |
A cytochrome C electron transfer switch modulated by heme ligation and isomerization of a peptidyl-prolyl bond.
Topics: Cytochromes c; Electrons; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligation; Protein Conformation | 2013 |
Picosecond binding of the His ligand to four-coordinate heme in cytochrome c': a one-way gate for releasing proximal NO.
Topics: Cytochromes c; Heme; Histidine; Ligands; Models, Molecular; Nitric Oxide; Protein Binding; Spectrum Analysis | 2013 |
An ultrasensitive chemiluminescence turn-on assay for protease and inhibitor screening with a natural substrate.
Topics: Biological Products; Cytochromes c; Enzyme Assays; Heme; Hydrogen Peroxide; Luminescence; Luminescent Measurements; Luminol; Models, Molecular; Peptide Hydrolases; Protease Inhibitors; Structure-Activity Relationship | 2013 |
Ferricytochrome (c) directly oxidizes aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress.
Topics: Acetone; Aerobiosis; Animals; Catalysis; Circular Dichroism; Computer Simulation; Copper; Cytochromes c; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Horses; Ions; Iron; Oxidation-Reduction; Oxygen Consumption; Protein Carbonylation; Pyruvaldehyde; Rats; Spectrophotometry, Ultraviolet; Stress, Physiological; Temperature | 2013 |
Cold crystallisation behaviour of water molecules in ionic liquids as a screening method to evaluate biocompatibility of the hydrated ionic liquids.
Topics: Biocompatible Materials; Catalytic Domain; Crystallization; Cytochromes c; Heme; Ionic Liquids; Polymers; Quantum Theory; Water | 2013 |
Cytochrome C on a gold surface: investigating structural relaxations and their role in protein-surface electron transfer by molecular dynamics simulations.
Topics: Biosensing Techniques; Cytochromes c; Electron Transport; Gold; Heme; Hydrogen Bonding; Immobilized Proteins; Molecular Dynamics Simulation; Mutation; Protein Structure, Tertiary; Recombinant Proteins; Surface Properties; Water | 2013 |
Electron transport via cytochrome c on Si-H surfaces: roles of Fe and heme.
Topics: Apoproteins; Circular Dichroism; Cytochromes c; Electron Transport; Heme; Hydrogen; Iron; Microscopy, Atomic Force; Photoelectron Spectroscopy; Porphyrins; Silicones; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Surface Properties; Temperature | 2013 |
Rate enhancement of bacterial extracellular electron transport involves bound flavin semiquinones.
Topics: Biofilms; Cytochrome c Group; Cytochromes c; Electrochemistry; Electrodes; Electron Spin Resonance Spectroscopy; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Microscopy, Confocal; Nucleotides; Oxidation-Reduction; Shewanella | 2013 |
Direct electron transfer between Cyt c and heme-Aβ relevant to Alzheimer's disease.
Topics: Alzheimer Disease; Amyloid beta-Peptides; Animals; Brain; Cytochromes c; Electron Transport; Electrons; Heme; Humans; Kinetics; Oxidation-Reduction; Oxidative Stress; Reactive Oxygen Species | 2013 |
Enhanced heme function and mitochondrial respiration promote the progression of lung cancer cells.
Topics: Animals; Carcinoma, Non-Small-Cell Lung; Cell Line, Tumor; Cell Movement; Cell Proliferation; Cell Respiration; Cytochromes c; Disease Progression; Energy Metabolism; Glucose; Heme; Hemeproteins; Humans; Lung Neoplasms; Membrane Transport Proteins; Mitochondria; Neoplasm Proteins; Oxygen; Oxygen Consumption; Tumor Stem Cell Assay; Xenograft Model Antitumor Assays | 2013 |
Becoming a peroxidase: cardiolipin-induced unfolding of cytochrome c.
Topics: Animals; Cardiolipins; Cytochromes c; Heme; Horses; Kinetics; Liposomes; Myocardium; Peroxidase; Phosphatidylcholines; Protein Binding; Protein Denaturation | 2013 |
Contrasting catalytic profiles of multiheme nitrite reductases containing CxxCK heme-binding motifs.
Topics: Amino Acid Motifs; Binding Sites; Biocatalysis; Cytochromes c; Ectothiorhodospiraceae; Electrochemical Techniques; Heme; Models, Molecular; Nitrite Reductases | 2013 |
Investigations of the low-frequency spectral density of cytochrome c upon equilibrium unfolding.
Topics: Animals; Cytochromes c; Guanidine; Heme; Horses; Hydrogen-Ion Concentration; Models, Molecular; Protein Denaturation; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Temperature; Thermodynamics | 2013 |
Distance-independent charge recombination kinetics in cytochrome c-cytochrome c peroxidase complexes: compensating changes in the electronic coupling and reorganization energies.
Topics: Cytochrome-c Peroxidase; Cytochromes c; Electron Transport; Electrons; Heme; Kinetics; Models, Molecular; Quantum Theory; Solvents; Thermodynamics; Zinc | 2013 |
Modulation of ligand-heme reactivity by binding pocket residues demonstrated in cytochrome c' over the femtosecond-second temporal range.
Topics: Arginine; Binding Sites; Crystallography, X-Ray; Cytochromes c; Heme; Humans; Kinetics; Leucine; Models, Chemical; Nitric Oxide; Photolysis; Protein Binding; Spectrophotometry, Infrared | 2013 |
Probing heme delivery processes in cytochrome c biogenesis System I.
Topics: Bacterial Outer Membrane Proteins; Biological Transport; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Membrane Proteins | 2013 |
Perturbation of cytochrome c maturation reveals adaptability of the respiratory chain in Mycobacterium tuberculosis.
Topics: Animals; Bacterial Proteins; Cytochromes c; Electron Transport; Electron Transport Complex IV; Female; Heme; Humans; Male; Mice, Inbred C57BL; Mycobacterium tuberculosis; Oxygen; Thioredoxins; Tuberculosis | 2013 |
Charge transfer through a cytochrome multiheme chain: theory and simulation.
Topics: Amino Acids; Cytochromes c; Electron Transport; Electrons; Energy Metabolism; Heme; Kinetics; Molecular Dynamics Simulation; Rhodopseudomonas; Thermodynamics | 2014 |
Perturbation of apoptosis upon binding of tRNA to the heme domain of cytochrome c.
Topics: Animals; Apoptosis; Caspases; Cattle; Cytochromes c; HEK293 Cells; Heme; Humans; Protein Binding; Protein Structure, Tertiary; RNA, Transfer | 2014 |
Hydrogen/hydride ion relay--a mechanism for early electron transfer in cytochrome c oxidases.
Topics: Amino Acid Sequence; Animals; Cattle; Cytochromes c; Electron Transport; Electron Transport Complex IV; Escherichia coli; Heme; Hydrogen; Oxidation-Reduction; Paracoccus denitrificans; Protons; Rhodobacter sphaeroides; Thermus thermophilus | 2013 |
The influence of heme ruffling on spin densities in ferricytochromes c probed by heme core 13C NMR.
Topics: Bacteria; Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Pseudomonas aeruginosa | 2013 |
Differential calmodulin-modulatory and electron transfer properties of neuronal nitric oxide synthase mu compared to the alpha variant.
Topics: Amino Acid Sequence; Animals; Calmodulin; Cytochromes c; Electron Transport; Flavin Mononucleotide; Heme; Isoenzymes; Nitric Oxide; Nitric Oxide Synthase Type I; Protein Binding; Rats | 2013 |
Long-range electron transfer with myoglobin immobilized at Au/mixed-SAM junctions: mechanistic impact of the strong protein confinement.
Topics: Animals; Cytochromes c; Deuterium Oxide; Electrochemistry; Electron Transport; Heme; Horses; Hydrogen-Ion Concentration; Immobilized Proteins; Kinetics; Models, Molecular; Myoglobin; Pressure; Protein Conformation; Temperature; Thermodynamics | 2014 |
The CcmFH complex is the system I holocytochrome c synthetase: engineering cytochrome c maturation independent of CcmABCDE.
Topics: Amino Acid Sequence; Amino Acid Substitution; Conserved Sequence; Cysteine; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Lyases; Molecular Sequence Data; Multiprotein Complexes; Protein Engineering | 2014 |
Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins.
Topics: Animals; Cysteine; Cytochromes c; Electron Transport; Fungal Proteins; Heme; Hemeproteins; Horses; Hydrogen-Ion Concentration; Iron; Kinetics; Ligands; Models, Molecular; Mutation; Myocardium; Oxidation-Reduction; Peroxidases; Spectrophotometry; Sulfhydryl Compounds; Thermodynamics | 2014 |
Spatially resolved confocal resonant Raman microscopic analysis of anode-grown Geobacter sulfurreducens biofilms.
Topics: Biofilms; Cytochromes c; Electrochemical Techniques; Electrodes; Electron Transport; Geobacter; Heme; Microscopy, Confocal; Oxidation-Reduction; Spectrum Analysis, Raman | 2014 |
Control of cytochrome c redox reactivity through off-pathway modifications in the protein hydrogen-bonding network.
Topics: Cytochromes c; Electron Transport; Heme; Humans; Hydrogen Bonding; Iron; Kinetics; Molecular Dynamics Simulation; Mutation; Oxidation-Reduction; Protein Conformation; Ruthenium | 2014 |
Subclinical carbon monoxide limits apoptosis in the developing brain after isoflurane exposure.
Topics: Anesthetics, Inhalation; Animals; Animals, Newborn; Apoptosis; Brain; Carbon Monoxide; Carboxyhemoglobin; Caspase 3; Cytochrome-c Peroxidase; Cytochromes c; Female; Heme; Immunohistochemistry; In Situ Nick-End Labeling; Isoflurane; Mice; Mitochondria; Pregnancy | 2014 |
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 |
Interaction of holoCcmE with CcmF in heme trafficking and cytochrome c biosynthesis.
Topics: Amino Acid Sequence; Bacterial Outer Membrane Proteins; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Genetic Complementation Test; Heme; Hemeproteins; Holoenzymes; Imidazoles; Molecular Sequence Data; Plasmids; Protein Transport; Spectrophotometry, Ultraviolet | 2014 |
Effect of motional restriction on the unfolding properties of a cytochrome c featuring a His/Met-His/His ligation switch.
Topics: Cytochromes c; Fungal Proteins; Heme; Immobilized Proteins; Kinetics; Models, Molecular; Motion; Protein Conformation; Protein Unfolding; Solutions; Static Electricity; Urea; Yeasts | 2014 |
Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR.
Topics: Cytochromes c; Electrons; Heme; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Shewanella | 2014 |
Solid-state electron transport via cytochrome c depends on electronic coupling to electrodes and across the protein.
Topics: Animals; Cytochromes c; Electric Conductivity; Electrodes; Electron Transport; Escherichia coli; Heme; Horses; Mutagenesis, Site-Directed; Mutation; Protein Binding; Temperature | 2014 |
Investigations of heme distortion, low-frequency vibrational excitations, and electron transfer in cytochrome c.
Topics: Amino Acid Substitution; Animals; Bacterial Proteins; Crystallography, X-Ray; Cytochrome c Group; Cytochromes c; Electron Transport; Heme; Horses; Kinetics; Models, Molecular; Mutation; Oxidation-Reduction; Photochemical Processes; Pseudomonas aeruginosa; Spectrum Analysis, Raman; Vibration | 2014 |
Characterization of the enhanced peroxidatic activity of amyloid β peptide-hemin complexes towards neurotransmitters.
Topics: Alzheimer Disease; Amyloid beta-Peptides; Angiotensins; Benzidines; Biosensing Techniques; Cytochromes c; Dopamine; Electrochemistry; Electrodes; Gold; Heme; Hemin; Humans; Neurotransmitter Agents; Oxidation-Reduction; Peroxidases; Protein Binding; Serotonin; Surface Properties | 2014 |
Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity.
Topics: Amino Acid Sequence; Amino Acid Substitution; Apoptosis; Crystallography, X-Ray; Cytochromes c; Electron Transport; Heme; Hydrogen Bonding; Lipid Peroxidation; Mitochondria; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Peroxidase; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 2014 |
Evolutionary history of redox metal-binding domains across the tree of life.
Topics: Adrenodoxin; Amino Acid Sequence; Archaea; Bacteria, Anaerobic; Cytochromes c; Ecosystem; Energy Metabolism; Evolution, Molecular; Ferrous Compounds; Heme; Iron; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Oxygen; Prokaryotic Cells; Protein Structure, Tertiary; Sequence Analysis, Protein | 2014 |
Investigations of the low frequency modes of ferric cytochrome c using vibrational coherence spectroscopy.
Topics: Animals; Cytochromes c; Heme; Horses; Ions; Iron; Motion; Protein Conformation; Spectrum Analysis, Raman; Vibration | 2014 |
Cofactor-dependent structural and binding properties of yeast cytochrome C peroxidase.
Topics: Coenzymes; Cytochrome-c Peroxidase; Cytochromes c; Heme; Multienzyme Complexes; Nuclear Magnetic Resonance, Biomolecular; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; X-Ray Diffraction | 2014 |
Cardiolipin modulates allosterically the nitrite reductase activity of horse heart cytochrome c.
Topics: Allosteric Regulation; Animals; Cardiolipins; Cytochromes c; Heme; Horses; Models, Molecular; Myocardium; Nitric Oxide; Nitrite Reductases; Nitrites; Nitrogen Dioxide; Protein Structure, Tertiary | 2014 |
Reductive nitrosylation of the cardiolipin-ferric cytochrome c complex.
Topics: Animals; Apoptosis; Cardiolipins; Cattle; Cytochromes c; Heme; Horses; Hydrogen-Ion Concentration; Iron; Kinetics; Models, Biological; Multiprotein Complexes; Myocardium; Nitric Oxide; Oxidation-Reduction | 2014 |
Dynamics of the heme-binding bacterial gas-sensing dissimilative nitrate respiration regulator (DNR) and activation barriers for ligand binding and escape.
Topics: Animals; Bacterial Proteins; Binding Sites; Carbon Monoxide; Cytochromes c; DNA, Bacterial; Fluorescence Polarization; Gene Expression Regulation, Bacterial; Heme; Horses; Kinetics; Ligands; Nitric Oxide; Promoter Regions, Genetic; Protein Binding; Pseudomonas aeruginosa; Transcription Factors | 2014 |
Mechanisms of mitochondrial holocytochrome c synthase and the key roles played by cysteines and histidine of the heme attachment site, Cys-XX-Cys-His.
Topics: Binding Sites; Catalytic Domain; Conserved Sequence; Cysteine; Cytochromes c; Escherichia coli; Heme; Histidine; Humans; Ligands; Lyases; Mitochondria; Oligonucleotides; Plasmids; Protein Folding; Pyridines; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Sulfhydryl Compounds | 2014 |
Structural basis for cytochrome c Y67H mutant to function as a peroxidase.
Topics: Cardiolipins; Cytochromes c; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Lipid Peroxidation; Models, Molecular; Mutation, Missense; Nuclear Magnetic Resonance, Biomolecular; Peroxidases; Protein Structure, Secondary; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 2014 |
Self-oxidation of cytochrome c at methionine80 with molecular oxygen induced by cleavage of the Met-heme iron bond.
Topics: Cytochromes c; Dithiothreitol; Heme; Humans; Iron; Liposomes; Methionine; Oxidation-Reduction; Oxygen; Protein Conformation; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | 2014 |
Configurational changes of heme followed by cytochrome c folding reaction.
Topics: Cytochromes c; Heme; Models, Molecular; Molecular Conformation; Protein Folding; Spectrum Analysis, Raman | 2015 |
Shewanella oneidensis cytochrome c maturation component CcmI is essential for heme attachment at the non-canonical motif of nitrite reductase NrfA.
Topics: Amino Acid Motifs; Cytochrome c Group; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Lyases; Molecular Chaperones; Nitrite Reductases; Oxidoreductases Acting on Sulfur Group Donors; Periplasm; Protein Structure, Tertiary; Shewanella | 2015 |
Methionine ligand lability of homologous monoheme cytochromes c.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins; Cytochromes c; Electrochemical Techniques; Electrodes; Escherichia coli; Gene Expression; Heme; Histidine; Kinetics; Ligands; Methionine; Molecular Sequence Data; Nitrosomonas europaea; Oxidation-Reduction; Protein Folding; Pseudomonas aeruginosa; Recombinant Proteins; Sequence Alignment; Shewanella; Temperature; Thermodynamics | 2015 |
Investigating protein folding and unfolding in electrospray nanodrops upon rapid mixing using theta-glass emitters.
Topics: Animals; Cytochromes c; Heme; Horses; Kinetics; Myoglobin; Protein Denaturation; Protein Folding; Protein Unfolding; Spectrometry, Mass, Electrospray Ionization | 2015 |
Ferric microperoxidase-11 catalyzes peroxynitrite isomerization.
Topics: Biocatalysis; Cardiolipins; Cyanides; Cytochromes c; Ferric Compounds; Heme; Isomerism; Kinetics; Peroxidases; Peroxynitrous Acid | 2015 |
Change in structure and ligand binding properties of hyperstable cytochrome c555 from Aquifex aeolicus by domain swapping.
Topics: Bacteria; Bacterial Proteins; Cytochromes c; Enzyme Stability; Heme; Hydrogen Bonding; Hydrogen-Ion Concentration; Models, Molecular; Protein Structure, Tertiary; Temperature | 2015 |
Immobilized cytochrome c bound to cardiolipin exhibits peculiar oxidation state-dependent axial heme ligation and catalytically reduces dioxygen.
Topics: Cardiolipins; Cytochromes c; Electrochemistry; Enzymes, Immobilized; Genetic Variation; Heme; Oxidation-Reduction; Oxygen; Protein Binding; Spectrum Analysis, Raman | 2015 |
Cytochrome c biogenesis in Campylobacter jejuni requires cytochrome c6 (CccA; Cj1153) to maintain apocytochrome cysteine thiols in a reduced state for haem attachment.
Topics: Bacterial Proteins; Campylobacter jejuni; Cysteine; Cytochromes c; Cytochromes c6; Electron Transport; Escherichia coli; Heme; Mutagenesis, Site-Directed; Oxidoreductases; Sulfhydryl Compounds | 2015 |
During Cytochrome c Maturation CcmI Chaperones the Class I Apocytochromes until the Formation of Their b-Type Cytochrome Intermediates.
Topics: Bacterial Proteins; Cytochrome b Group; Cytochromes c; Heme; Molecular Chaperones; Protein Binding; Rhodobacter capsulatus | 2015 |
A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch.
Topics: Animals; Apoptosis; Cardiolipins; Crystallization; Cytochromes c; Electron Spin Resonance Spectroscopy; Fungal Proteins; Heme; Horses; Hydrogen Bonding; Ions; Iron; Ligands; Lysine; Oxidation-Reduction; Oxygen; Peroxidases; Protein Binding; Protein Folding; Protein Structure, Secondary; Saccharomyces cerevisiae; Spectrophotometry, Ultraviolet | 2015 |
Ultrafast Heme Dynamics of Ferric Cytochrome c in Different Environments: Electronic, Vibrational, and Conformational Relaxation.
Topics: Animals; Circular Dichroism; Cytochromes c; Heme; Horses; Models, Molecular; Protein Conformation; Spectrophotometry, Ultraviolet | 2015 |
Design and engineering of a man-made diffusive electron-transport protein.
Topics: Amino Acid Sequence; Cytochromes c; Diffusion; Electron Transport; Electron Transport Chain Complex Proteins; Heme; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Photolysis; Protein Engineering; Protein Structure, Tertiary; Sequence Homology, Amino Acid | 2016 |
Transcriptomic profiling of Methylococcus capsulatus (Bath) during growth with two different methane monooxygenases.
Topics: Bacterial Proteins; Cluster Analysis; Computational Biology; Copper; Cytochromes c; Gene Expression Profiling; Gene Expression Regulation, Bacterial; Gene Order; Genetic Loci; Heme; Mass Spectrometry; Metabolic Networks and Pathways; Methane; Methylococcus capsulatus; Multigene Family; Oxygenases; Proteome; Transcriptome | 2016 |
Disruption of a hydrogen bond network in human versus spider monkey cytochrome c affects heme crevice stability.
Topics: Amino Acid Substitution; Animals; Atelinae; Circular Dichroism; Crystallography, X-Ray; Cytochromes c; Heme; Humans; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Protein Folding; Protein Stability | 2016 |
Effects of cycle duration of an external electrostatic field on anammox biomass activity.
Topics: Ammonium Compounds; Anaerobiosis; Bacteria; Biomass; Bioreactors; Cytochromes c; Flow Cytometry; Gene Dosage; Heme; Hydrazines; Microscopy, Electron, Transmission; Nitrogen; Oxidation-Reduction; Oxidoreductases; Peroxidase; Polymerase Chain Reaction; RNA, Ribosomal, 16S; Static Electricity | 2016 |
Internal switches modulating electron tunneling currents in respiratory complex III.
Topics: Crystallography, X-Ray; Cytochromes c; Electron Transport; Electron Transport Complex III; Electrons; Heme; Models, Chemical; Models, Molecular; Molecular Structure; Mutation; Oxidation-Reduction; Phenylalanine; Protein Binding; Protein Conformation | 2016 |
Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins.
Topics: Cytochromes c; Escherichia coli; Heme; Immunoblotting; Lyases; Membrane Proteins; Molecular Chaperones; Oxidation-Reduction; Protein Transport | 2016 |
Increased dynamics in the 40-57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation.
Topics: Amides; Apoptosis; Cytochromes c; Heme; Humans; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Mutation; Protein Structure, Secondary; Thermodynamics | 2016 |
In meso crystal structure of a novel membrane-associated octaheme cytochrome c from the Crenarchaeon Ignicoccus hospitalis.
Topics: Archaeal Proteins; Binding Sites; Conserved Sequence; Crystallography, X-Ray; Cytochromes a1; Cytochromes c; Cytochromes c1; Desulfurococcaceae; Evolution, Molecular; Genes, Archaeal; Heme; Models, Molecular; Nitrate Reductases; Protein Structure, Quaternary; Protein Subunits; Static Electricity | 2016 |
Chiral Selectivity in Inter-reactant Recognition and Electron Transfer of the Oxidation of Horse Heart Cytochrome c by Trioxalatocobaltate(III).
Topics: Animals; Cobalt; Coordination Complexes; Cytochromes c; Electron Transport; Heme; Horses; Kinetics; Models, Molecular; Oxalic Acid; Oxidation-Reduction; Stereoisomerism | 2016 |
Comparative study on stabilization mechanism of monomeric cytochrome c
Topics: Crystallography, X-Ray; Cytochromes c; Enzyme Stability; Heme; Hydrogen Bonding; Models, Molecular; Mutagenesis; Mutation; Protein Conformation; Shewanella; Temperature | 2016 |
Effect of Bioconjugation on the Reduction Potential of Heme Proteins.
Topics: Anions; Arsenicals; Circular Dichroism; Cytochromes c; Heme; Myoglobin; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Static Electricity; Temperature; Water | 2016 |
The Dynamics Behind the Affinity: Controlling Heme-Gas Affinity via Geminate Recombination and Heme Propionate Conformation in the NO Carrier Cytochrome c'.
Topics: Alcaligenes; Carbon Monoxide; Cytochromes c; Heme; Kinetics; Molecular Conformation; Molecular Dynamics Simulation; Nitric Oxide; Propionates; Recombination, Genetic | 2016 |
Photoacoustic calorimetry studies of CO photo-dissociation from chloramine-T modified horse heart cytochrome-c.
Topics: Acoustics; Animals; Binding Sites; Calorimetry; Carbon Monoxide; Chloramines; Cytochromes c; Heme; Horses; Iron; Kinetics; Ligands; Light; Myocardium; Photolysis; Protein Conformation; Spectrophotometry, Ultraviolet; Sulfoxides; Thermodynamics; Tosyl Compounds | 2016 |
Influence of haem environment on the catalytic properties of the tetrathionate reductase TsdA from Campylobacter jejuni.
Topics: Bacterial Proteins; Campylobacter jejuni; Catalysis; Cytochromes c; Electron Transport; Heme; Oxidoreductases | 2016 |
Conformational status of cytochrome c upon N-homocysteinylation: Implications to cytochrome c release.
Topics: Animals; Apoptosis; Cardiolipins; Cattle; Circular Dichroism; Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Homocysteine; Iron; Ligands; Methionine; Myocardium; Oxygen; Peroxidase; Peroxidases; Protein Conformation; Protein Processing, Post-Translational; Spectrophotometry, Ultraviolet | 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 |
Engineered holocytochrome
Topics: Amino Acid Motifs; Amino Acid Substitution; Catalytic Domain; Cloning, Molecular; Coenzymes; Cytochromes c; Electron Transport; Escherichia coli; Gene Expression; Heme; Humans; Lyases; Mutation; Oxidation-Reduction; Protein Binding; Protein Engineering; Protein Interaction Domains and Motifs; Protein Structure, Secondary; Recombinant Proteins; Substrate Specificity | 2017 |
Effect of methionine80 heme coordination on domain swapping of cytochrome c.
Topics: Calorimetry; Cytochromes c; Heme; Humans; Kinetics; Methionine | 2017 |
Remote Perturbations in Tertiary Contacts Trigger Ligation of Lysine to the Heme Iron in Cytochrome c.
Topics: Amino Acid Substitution; Animals; Biocatalysis; Circular Dichroism; Cytochromes c; Electron Spin Resonance Spectroscopy; Electron Transport; Enzyme Stability; Heme; Horses; Hot Temperature; Hydrogen Bonding; Hydrogen-Ion Concentration; Ligands; Lysine; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Point Mutation; Protein Conformation; Protein Denaturation; Recombinant Proteins | 2017 |
NMR studies of the interaction between inner membrane-associated and periplasmic cytochromes from Geobacter sulfurreducens.
Topics: Algorithms; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Cytochrome-c Peroxidase; Cytochromes c; Databases, Protein; Electron Transport; Geobacter; Heme; Kinetics; Membrane Proteins; Models, Molecular; Molecular Docking Simulation; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Periplasmic Proteins; Protein Conformation; Protein Interaction Domains and Motifs; Protein Multimerization; Recombinant Proteins | 2017 |
Biosynthesis of Single Thioether c-Type Cytochromes Provides Insight into Mechanisms Intrinsic to Holocytochrome c Synthase (HCCS).
Topics: Amino Acid Motifs; Amino Acid Sequence; Amino Acid Substitution; Circular Dichroism; Conserved Sequence; Cysteine; Cytochromes c; Glutathione Transferase; Heme; Humans; Lyases; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Oxygen; Protein Conformation; Protein Engineering; Protein Folding; Recombinant Fusion Proteins; Stereoisomerism | 2017 |
The thioreduction component CcmG confers efficiency and the heme ligation component CcmH ensures stereo-specificity during cytochrome
Topics: Amino Acid Substitution; Apoenzymes; Bacterial Outer Membrane Proteins; Bacterial Proteins; Binding Sites; Cysteine; Cystine; Cytochromes c; Heme; Models, Biological; Mutation; Oxidation-Reduction; Peptide Fragments; Protein Disulfide Reductase (Glutathione); Protein Interaction Domains and Motifs; Protein Multimerization; Recombinant Fusion Proteins; Recombinant Proteins; Rhodobacter capsulatus; Stereoisomerism | 2017 |
Structural changes and picosecond to second dynamics of cytochrome c in interaction with nitric oxide in ferrous and ferric redox states.
Topics: Animals; Cytochromes c; Ferric Compounds; Ferrous Compounds; Heme; Horses; Kinetics; Mitochondria; Nitric Oxide; Oxidation-Reduction; Spectrum Analysis, Raman | 2017 |
The mechanism for oxygen reduction in cytochrome c dependent nitric oxide reductase (cNOR) as obtained from a combination of theoretical and experimental results.
Topics: Bacterial Proteins; Biocatalysis; Catalytic Domain; Cytochromes c; Electron Transport Complex IV; Heme; Kinetics; Molecular Dynamics Simulation; Nitric Oxide; Oxidation-Reduction; Oxidoreductases; Oxygen; Paracoccus denitrificans; Protein Conformation; Quantum Theory; Thermodynamics | 2017 |
From B to A: making an essential cofactor in a human parasite.
Topics: Animals; Cytochromes c; Electron Transport Complex IV; Heme; Humans; Parasites; Trypanosoma cruzi | 2017 |
Computational Insight into the Interaction of Cytochrome C with Wet and PVP-Coated Ag Surfaces.
Topics: Adsorption; Animals; Cattle; Coated Materials, Biocompatible; Cytochromes c; Heme; Molecular Dynamics Simulation; Nanostructures; Povidone; Silver; Surface Properties; Water; Wettability | 2017 |
Electrochemistry and electron paramagnetic resonance spectroscopy of cytochrome c and its heme-disrupted analogs.
Topics: Animals; Cattle; Cytochromes c; Electrochemistry; Electron Spin Resonance Spectroscopy; Heme; Horses; Models, Molecular; Protein Conformation | 2018 |
The FNR modules contribute to control nitric oxide synthase catalysis revealed by chimera enzymes.
Topics: Animals; Biocatalysis; Cytochromes c; Ferredoxin-NADP Reductase; Ferricyanides; Flavins; Heme; Kinetics; NADP; Nitric Oxide; Nitric Oxide Synthase; Oxidation-Reduction; Oxygenases; Rats; Recombinant Fusion Proteins; Spectrum Analysis; Time Factors | 2017 |
Heightened Dynamics of the Oxidized Y48H Variant of Human Cytochrome c Increases Its Peroxidatic Activity.
Topics: Crystallography, X-Ray; Cytochromes c; Enzyme Stability; Heme; Humans; Molecular Dynamics Simulation; Oxidation-Reduction; Peroxidase; Point Mutation; Protein Conformation; Protein Folding; Thermodynamics | 2017 |
Helical Propensity Affects the Conformational Properties of the Denatured State of Cytochrome c'.
Topics: Cytochromes c; Guanidine; Heme; Kinetics; Models, Molecular; Mutagenesis; Protein Conformation, alpha-Helical; Protein Denaturation; Rhodopseudomonas | 2018 |
A cross-domain charge interaction governs the activity of NO synthase.
Topics: Animals; Catalysis; Cytochromes c; Electron Transport; Electrons; Flavin Mononucleotide; Heme; Kinetics; Models, Molecular; Mutation; Nitric Oxide; Nitric Oxide Synthase Type I; Oxidation-Reduction; Protein Domains; Rats | 2018 |
The heme auxotroph Caenorhabditis elegans can cleave the thioether bonds of c-type cytochromes.
Topics: Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Cytochromes c; Heme | 2018 |
Anammox Organism KSU-1 Expresses a Novel His/DOPA Ligated Cytochrome c.
Topics: Ammonium Compounds; Bacteria; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Cytochromes c; Dihydroxyphenylalanine; Electron Transport; Heme; Models, Molecular; Nitrites; Oxidation-Reduction; Protein Conformation | 2018 |
Cys Links Heme: Stereo-orientation of Heme Transfer in Cytochrome c Biogenesis.
Topics: Cysteine; Cytochromes c; Heme | 2018 |
Structurally Mapping Endogenous Heme in the CcmCDE Membrane Complex for Cytochrome c Biogenesis.
Topics: Bacterial Outer Membrane Proteins; Bacterial Proteins; Binding Sites; Cysteine; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Membrane Proteins; Models, Molecular; Multiprotein Complexes; Mutation; Protein Binding; Protein Transport | 2018 |
Polyethylene glycol promotes autoxidation of cytochrome c.
Topics: Cytochromes c; Electron Transport; Heme; Humans; Oxidation-Reduction; Oxygen; Polyethylene Glycols; Protein Conformation | 2018 |
Cryo-EM structure of the RC-LH core complex from an early branching photosynthetic prokaryote.
Topics: Bacterial Proteins; Chloroflexi; Cryoelectron Microscopy; Cytochromes c; Heme; Light; Light-Harvesting Protein Complexes; Models, Molecular; Photosynthetic Reaction Center Complex Proteins | 2018 |
Properties and structure of a low-potential, penta-heme cytochrome c
Topics: Chromatiaceae; Crystallography, X-Ray; Cytochrome c Group; Cytochromes c; Electron Transport; Heme | 2019 |
Ligation and Reactivity of Methionine-Oxidized Cytochrome c.
Topics: Amino Acid Sequence; Binding Sites; Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Imidazoles; Iron; Ligands; Methionine; Models, Biological; Oxidation-Reduction; Spectrum Analysis, Raman; Sulfoxides; Yeasts | 2018 |
Probing Cytochrome c Folding Transitions upon Phototriggered Environmental Perturbations Using Time-Resolved X-ray Scattering.
Topics: Animals; Cytochromes c; Heme; Light; Models, Molecular; Protein Conformation; Protein Folding; Protein Unfolding; Time Factors; X-Ray Diffraction | 2018 |
Bacterial denitrifying nitric oxide reductases and aerobic respiratory terminal oxidases use similar delivery pathways for their molecular substrates.
Topics: Amino Acid Sequence; Catalysis; Catalytic Domain; Crystallography, X-Ray; Cytochromes c; Denitrification; Electron Transport Complex IV; Heme; Models, Molecular; Molecular Dynamics Simulation; Nitric Oxide; Oxidation-Reduction; Oxidoreductases; Protein Conformation; Pseudomonas aeruginosa; Sequence Homology; Substrate Specificity | 2018 |
Upon further analysis, neither cytochrome c
Topics: Catalysis; Cytochromes c; Electron Transport; Heme; Hydrophobic and Hydrophilic Interactions; Kinetics; Nitric Oxide; Nitrosomonas europaea; Oxidation-Reduction; Oxidoreductases; Protein Binding | 2018 |
Selective staining and eradication of cancer cells by protein-carrying DARPin-functionalized liposomes.
Topics: Adenocarcinoma; ADP Ribose Transferases; Animals; Ankyrin Repeat; Bacterial Toxins; Breast Neoplasms; Cell Line, Tumor; CHO Cells; Cricetinae; Cricetulus; Cytochromes c; Exotoxins; Female; Heme; Humans; Liposomes; Luminescent Proteins; Ovarian Neoplasms; Particle Size; Pseudomonas aeruginosa Exotoxin A; Receptor, ErbB-2; Red Fluorescent Protein; Virulence Factors | 2018 |
The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c.
Topics: Amino Acid Substitution; Cytochromes c; Heme; Mutation, Missense; Oxidation-Reduction; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 2018 |
The CcmC-CcmE interaction during cytochrome
Topics: Amino Acid Substitution; Apoproteins; Bacterial Outer Membrane Proteins; Binding Sites; Crystallography, X-Ray; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Membrane Proteins; Mutagenesis, Site-Directed; Protein Conformation; Protein Interaction Domains and Motifs | 2018 |
Alternative pathway linked by hydrogen bonds connects heme-Fe of cytochrome c with subunit II-CuA of cytochrome a.
Topics: Amino Acids; Cytochromes a; Cytochromes c; Electron Transport; Electrons; Heme; Hydrogen Bonding; Iron; Water | 2018 |
Peroxidase activity of cytochrome c in its compact state depends on dynamics of the heme region.
Topics: Animals; Cytochromes c; Ferrous Compounds; Heme; Horses; Hydrogen-Ion Concentration; Iron; Mitochondria; Models, Molecular; Molecular Dynamics Simulation; Molecular Structure; Oxidation-Reduction; Peroxidase; Protein Conformation; Protein Unfolding | 2018 |
Utility of fluorescent heme analogue ZnPPIX to monitor conformational heterogeneity in vertebrate hexa-coordinated globins.
Topics: Animals; Circular Dichroism; Cytochromes c; Globins; Heme; Horses; Humans; Protein Conformation; Protoporphyrins; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Vertebrates | 2019 |
Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics.
Topics: Animals; Apoptosis; Cardiolipins; Cell Membrane; Cytochromes c; Fatty Acids, Unsaturated; Heme; Horses; Lipidomics; Magnetic Resonance Spectroscopy; Myocardium; Nanotechnology; Oxygen; Peroxidases; Protein Conformation; Protein Domains; Protein Folding | 2019 |
Covalent Modification by Glyoxals Converts Cytochrome c Into its Apoptotically Competent State.
Topics: Apoptosis; Cytochromes c; Glyoxal; Heme; Peroxidase; Polymerization | 2019 |
5,7,3',4'-Hydroxy substituted flavonoids reduce the heme of cytochrome c with a range of rate constants.
Topics: Animals; Antioxidants; Cytochromes c; Flavonoids; Heme; Oxidation-Reduction; Plants; Structure-Activity Relationship | 2019 |
Crystal Structure of Dihydro-Heme d
Topics: Amino Acids; Bacterial Proteins; Binding Sites; Catalysis; Cytochromes c; Heme; Humans; Models, Molecular; Nitric Oxide; Nitrite Reductases; Nitrites; Oxidation-Reduction; Oxidoreductases; Protein Conformation; Protein Domains; Pseudomonas aeruginosa; Transition Temperature | 2019 |
A Solid-State Protein Junction Serves as a Bias-Induced Current Switch.
Topics: Cytochromes c; Electric Conductivity; Electrochemistry; Electrodes; Electron Transport; Heme; Humans; Iron; Oxidation-Reduction; Protein Conformation | 2019 |
Comparison of the Size and Properties of the Cytochrome c/Cardiolipin Nanospheres in a Sediment and Non-polar Medium.
Topics: Animals; Apoptosis; Cardiolipins; Crystallization; Cytochromes c; Dynamic Light Scattering; Fluorescence Resonance Energy Transfer; Heme; Horses; Hydrogen Bonding; Hydrogen-Ion Concentration; Lipid Bilayers; Lipid Peroxidation; Methanol; Methionine; Mitochondria, Heart; Mitochondrial Membranes; Nanospheres; Protein Conformation; Protein Unfolding | 2019 |
Definition of the Interaction Domain and Electron Transfer Route between Cytochrome c and Cytochrome Oxidase.
Topics: Animals; Cattle; Coordination Complexes; Copper; Cytochromes c; Electron Transport; Electron Transport Complex IV; Ethylene Glycol; Heme; Horses; Mutation; Photolysis; Protein Domains; Ruthenium | 2019 |
A Heme Propionate Staples the Structure of Cytochrome
Topics: Coordination Complexes; Cytochromes c; Heme; Humans; Hydrogen-Ion Concentration; Iron; Kinetics; Ligands; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Propionates | 2019 |
Comparison of the structural dynamic and mitochondrial electron-transfer properties of the proapoptotic human cytochrome c variants, G41S, Y48H and A51V.
Topics: Animals; Apoptosis; Cattle; Cell Respiration; Cytochromes c; Electrons; Heme; Humans; Iron; Molecular Dynamics Simulation; Mutation, Missense; Peroxidase; Thrombocytopenia | 2020 |
Ultrafast Heme Relaxation Dynamics Probing the Unfolded States of Cytochrome c Induced by Liposomes: Effect of Charge of Phospholipids.
Topics: Cardiolipins; Cytochromes c; Heme; Liposomes; Phospholipids | 2020 |
Unfolding cytochromes c-b
Topics: Apoproteins; Crystallography, X-Ray; Cytochrome b Group; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Kinetics; Models, Molecular; Protein Folding | 2020 |
Primary Electronic and Vibrational Dynamics of Cytochrome
Topics: Cytochromes c; Electronics; Heme; Lasers; Vibration | 2020 |
Hydroxylamine Complexes of Cytochrome
Topics: Alcaligenes; Cytochromes c; Heme; Hydroxylamine; Iron; Kinetics; Oxidation-Reduction; Spectrum Analysis | 2020 |
Insights into the Enhanced Catalytic Activity of Cytochrome c When Encapsulated in a Metal-Organic Framework.
Topics: Benzothiazoles; Biocatalysis; Catalytic Domain; Cytochromes c; Density Functional Theory; Heme; Metal-Organic Frameworks; Molecular Dynamics Simulation; Oxidation-Reduction; Spectrophotometry; Sulfonic Acids | 2020 |
Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c.
Topics: Cytochromes c; Electron Transport; Ferrous Compounds; Heme; Iron; Metals; Methionine; Molecular Dynamics Simulation; Photolysis; Spectrometry, X-Ray Emission | 2021 |
In vitro reconstitution reveals major differences between human and bacterial cytochrome c synthases.
Topics: Bacteria; Catalytic Domain; Cytochromes c; Escherichia coli; Heme; Humans; In Vitro Techniques; Lyases; Mitochondria; Peptides; Substrate Specificity | 2021 |
Structural evaluation of cytochrome c by Raman spectroscopy and its relationship with apoptosis and protein degradation in postmortem bovine muscle.
Topics: Amides; Animals; Apoptosis; Cattle; Cytochromes c; Desmin; Heme; Male; Muscle Proteins; Muscle, Skeletal; Porphyrins; Proteolysis; Spectrum Analysis, Raman; Time Factors; Troponin T | 2021 |
Heme is responsible for enhanced singlet oxygen deactivation in cytochrome
Topics: Amino Acid Sequence; Cytochromes c; Flavin Mononucleotide; Heme; Kinetics; Models, Molecular; Oxygen; Photochemistry; Protein Binding; Singlet Oxygen | 2021 |
Supramolecular organization of Cytochrome-C into quantum-dot decorated macromolecular network under pH and thermal stress.
Topics: Amyloid; Circular Dichroism; Cytochromes c; Heme; Hydrogen-Ion Concentration; Oxidation-Reduction; Protein Folding; Quantum Theory | 2021 |
Kinetics and Energetics of Intramolecular Electron Transfer in Single-Point Labeled TUPS-Cytochrome
Topics: Animals; Cysteine; Cytochromes c; Electron Transport; Heme; Horses; Kinetics; Models, Molecular; Oxidation-Reduction; Point Mutation; Protein Conformation; Pyrenes | 2021 |
Cryo-EM of CcsBA reveals the basis for cytochrome c biogenesis and heme transport.
Topics: Cryoelectron Microscopy; Cytochromes c; Heme; Protein Transport | 2022 |
Molecular insights on the conformational dynamics of a P76C mutant of human cytochrome c and the enhancement on its peroxidase activity.
Topics: Amino Acid Sequence; Cardiolipins; Cysteine; Cytochromes c; Enzyme Activation; Heme; Humans; Molecular Dynamics Simulation; Mutant Proteins; Mutation; Peroxidases; Protein Conformation; Structure-Activity Relationship | 2022 |
[Enhanced heterologous expression of the cytochrome c from uncultured anaerobic methanotrophic archaea].
Topics: Anaerobiosis; Archaea; Cytochromes c; Escherichia coli; Heme | 2022 |
High-Repetition-Rate Transient Absorption Spectroscopy of Respiratory Supercomplexes.
Topics: Animals; Cytochromes c; Heme; Humans; Mice; Mitochondrial Membranes; Oxidation-Reduction; Spectrum Analysis | 2022 |
Effect on intrinsic peroxidase activity of substituting coevolved residues from Ω-loop C of human cytochrome c into yeast iso-1-cytochrome c.
Topics: Animals; Cytochromes c; Heme; Horses; Humans; Hydrogen-Ion Concentration; Peroxidase; Peroxidases; Protein Conformation; Saccharomyces cerevisiae | 2022 |
Investigation of the Molecular Mechanisms of the Eukaryotic Cytochrome-
Topics: Cytochromes c; Eukaryota; Eukaryotic Cells; Heme; Lyases | 2022 |
Cofactor Dynamics Couples the Protein Surface to the Heme in Cytochrome
Topics: Cytochromes c; Electron Transport; Electrons; Heme; Ruthenium | 2022 |
Singlet oxygen quenching as a probe for cytochrome
Topics: Chlorides; Circular Dichroism; Cytochromes c; Heme; Hydrogen-Ion Concentration; Perchlorates; Protein Conformation; Protein Denaturation; Protein Folding; Singlet Oxygen; Sulfates | 2022 |
Multiple Mutations in the Non-Ordered Red Ω-Loop Enhance the Membrane-Permeabilizing and Peroxidase-like Activity of Cytochrome
Topics: Antioxidants; Cardiolipins; Cytochromes c; Heme; Liposomes; Mutation; Peroxidases | 2022 |
Coordination of metal center biogenesis in human cytochrome c oxidase.
Topics: Copper; Cytochromes c; Electron Transport Complex IV; Heme; Humans; Molecular Chaperones; Oxidoreductases | 2022 |
Crystal structure of Trypanosoma cruzi heme peroxidase and characterization of its substrate specificity and compound I intermediate.
Topics: Antioxidants; Ascorbate Peroxidases; Ascorbic Acid; Chagas Disease; Cytochrome-c Peroxidase; Cytochromes c; Heme; Humans; Peroxidase; Peroxidases; Substrate Specificity; Trypanosoma cruzi | 2022 |
Evolution of quinol oxidation within the heme‑copper oxidoreductase superfamily.
Topics: Copper; Cytochromes c; Heme; Hydroquinones; Nitric Oxide; Oxidoreductases; Oxygen | 2022 |
Pleiotropic Effects of Hfq on the Cytochrome
Topics: Cytochromes c; Heme; HMGA Proteins; Homogentisic Acid; Iron; Melanins; RNA; Shewanella | 2022 |
Binding Interface and Electron Transfer Between Nicotine Oxidoreductase and Its Cytochrome c Electron Acceptor.
Topics: Amines; Amino Acids; Cytochromes c; Electron Transport; Electrons; Flavins; Flavoproteins; Heme; Nicotine; Oxidants; Oxidation-Reduction; Oxidoreductases; Oxygen | 2022 |
Engineering Human Neuroglobin into a Cytochrome c-Like Protein with a Single Thioether Bond in Non-native State.
Topics: Cytochromes c; Heme; Humans; Neuroglobin; Oxidation-Reduction; Protein Engineering; Sulfides | 2022 |
Radical Mediated Rapid
Topics: Alanine; Cytochromes c; Escherichia coli; Heme; Manganese; Protoporphyrins; Sulfhydryl Compounds; Zinc | 2022 |
Radical in the Peroxide-Produced F-Type Ferryl Form of Bovine Cytochrome
Topics: Animals; Cattle; Cytochromes c; Electron Transport Complex IV; Heme; Hydrogen Peroxide; Oxidation-Reduction; Peroxides; Protons | 2022 |
Structures of the CcmABCD heme release complex at multiple states.
Topics: Adenosine Triphosphate; Bacterial Outer Membrane Proteins; Bacterial Proteins; Cytochromes c; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins | 2022 |
Alkaline State of the Domain-Swapped Dimer of Human Cytochrome
Topics: Cardiolipins; Cytochromes c; Heme; Humans; Hydrogen-Ion Concentration; Peroxidases; Protein Conformation | 2022 |
De novo sequencing and construction of a unique antibody for the recognition of alternative conformations of cytochrome
Topics: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Cytochromes c; Heme; Hybridomas; Melanoma, Experimental; Mice; Oxidation-Reduction | 2022 |
A Common Target of Nitrite and Nitric Oxide for Respiration Inhibition in Bacteria.
Topics: Cytochromes c; Heme; Nitric Oxide; Nitrites; Respiration | 2022 |
SERS uncovers the link between conformation of cytochrome c heme and mitochondrial membrane potential.
Topics: Adenosine Triphosphate; Cytochromes c; Heme; Membrane Potential, Mitochondrial; Mitochondria | 2023 |
Ultrafast Energy Transfer from Photoexcited Tryptophan to the Haem in Cytochrome c.
Topics: Cytochromes c; Electron Transport; Energy Transfer; Heme; Iron; Tryptophan | 2023 |
Resonance Raman Studies on Heme Ligand Stretching Modes in Methionine80-Depleted Cytochrome
Topics: Animals; Cytochromes c; Heme; Horses; Iron; Ligands; Peroxidases; Spectrum Analysis, Raman | 2023 |
Cytochrome P460 Cofactor Maturation Proceeds via Peroxide-Dependent Post-translational Modification.
Topics: Cytochromes c; Enzyme Precursors; Escherichia coli; Heme; Spectrum Analysis | 2023 |
Bacterial TANGO2 homologs are heme-trafficking proteins that facilitate biosynthesis of cytochromes
Topics: Bacterial Proteins; Catalase; Cytochromes c; Heme; Hemeproteins; Shewanella | 2023 |
Ferrous nitrosylated cytochrome c: The unusual strength of the proximal His18-Fe bond.
Topics: Animals; Cytochromes c; Electron Spin Resonance Spectroscopy; Ferrous Compounds; Heme; Horses; Oxidation-Reduction | 2023 |
Architecture of the Heme-translocating CcmABCD/E complex required for Cytochrome c maturation.
Topics: Apoproteins; ATP-Binding Cassette Transporters; Cytochromes c; Escherichia coli; Heme | 2023 |
A Comparative Multi-Frequency EPR Study of Dipolar Interaction in Tetra-Heme Cytochromes.
Topics: Cell Movement; Computer Simulation; Cytochromes c; Electron Transport; Heme | 2023 |
Hemoglobin and cytochrome c. reinterpreting the origins of oxygenation and oxidation in erythrocytes and in vivo cancer lung cells.
Topics: Cytochromes c; Erythrocytes; Heme; Hemeproteins; Hemoglobins; Humans; Lung; Lung Neoplasms; Oxidation-Reduction | 2023 |
Genetically Encoded Fluorescent Probe for Detection of Heme-Induced Conformational Changes in Cytochrome c.
Topics: Apoptosis; Cytochromes c; Energy Metabolism; Fluorescent Dyes; Heme | 2023 |
An engineered thermally tolerant apo-cytochrome scaffold for metal-less incorporation of heme derivative.
Topics: Alanine; Cytochromes c; Heme; Ligands; Methionine; Molecular Docking Simulation; Oxidation-Reduction | 2023 |