heme has been researched along with cysteine in 286 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 59 (20.63) | 18.7374 |
| 1990's | 39 (13.64) | 18.2507 |
| 2000's | 97 (33.92) | 29.6817 |
| 2010's | 76 (26.57) | 24.3611 |
| 2020's | 15 (5.24) | 2.80 |
| Authors | Studies |
|---|---|
| Hopfield, JJ; Ogawa, S; Shulman, RG | 1 |
| Buse, G; Steffens, G | 1 |
| Banerjee, R; Henry, Y; Stetzkowski, F | 1 |
| Kappas, A; Maines, MD | 2 |
| Sugimura, Y; Yakushiji, E | 1 |
| Huestis, WH; Raftery, MA | 1 |
| Morita, M; Mukunoki, M; Okubo, F; Tadokoro, S | 1 |
| Bazile, J; Cordier, JP; Frourin, A; Jondeau, D; Thenot, M | 1 |
| Ogawa, S; Sakurai, H | 1 |
| Kito, M; Sakurai, H | 1 |
| Elliott, T; Roth, JR | 1 |
| Boxer, SG; Lambright, DG; Varadarajan, R | 1 |
| Wilton, DC | 1 |
| Kawasaki, K; Maeda, M; Sakurai, H; Uchikubo, H; Yoshimura, T | 1 |
| Behere, DV; Goff, HM; Gonzalez-Vergara, E | 1 |
| Kuramitsu, S; Matsubara, H; Miyazaki, T; Mukai, K; Wakabayashi, S | 1 |
| Akimoto, S; Kawasaki, K; Maeda, M; Sakurai, H; Shibuya, M; Shimizu, C | 1 |
| Köhler, H; Neupert, W; Nicholson, DW | 1 |
| Akhrem, AA; Chashchin, VL; Pikuleva, IA; Usanov, SA | 1 |
| Ichikawa, Y; Tomita, S; Tsubaki, M; Tsuneoka, Y | 1 |
| Black, SD; Coon, MJ | 1 |
| Kon, H; Makinen, MW | 1 |
| Boccu, E; Fontana, A; Veronese, FM | 1 |
| Chien, CW; Dickinson, LC | 1 |
| Campbell, LL; Trousil, EB | 1 |
| Loock, B; Momenteau, M | 1 |
| Pettigrew, GW | 1 |
| Bryant, MP; Varel, VH | 1 |
| Gunsalus, IC; Yu, C | 1 |
| de Waart, J; Pouw, H | 1 |
| Bryant, MP; Crabill, MR; Eller, C | 1 |
| Hanes, DM; Tappel, AL | 1 |
| Nagai, M; Sugita, Y; Yoneyama, Y | 1 |
| Salhany, JM | 1 |
| Henderson, RW; Morton, TC | 1 |
| Birchmeier, W; Bradshaw, RA; Glatthaar, BE; Winterhalter, KH | 1 |
| Ishiguro, I; Shinoara, R | 1 |
| Heystek, J; Klapper, MH; Uchida, H | 1 |
| Meyer, T; Pettigrew, G | 1 |
| Kubal, J | 1 |
| Sano, S | 1 |
| Björkstén, F | 1 |
| Craigie, JS; Laycock, MV | 1 |
| Ho, YK; Lascelles, J | 1 |
| Bonsignore, D; Cartasegna, C; Vergnano, C | 1 |
| Sawada, H; Sugita, Y; Takeshita, M; Yoneyama, Y | 1 |
| Koul, AK; Nix, PT; Warme, PK; Wasserman, GF | 1 |
| Gunsalus, IC; Haniu, M; Yasunobu, KT | 1 |
| Layrisse, M; Leets, I; Martínez-Torres, C; Ramírez, J; Taylor, P | 1 |
| Drummond, GS; Kappas, A | 1 |
| Balestrieri, C; Bismuto, E; Colonna, G; Irace, G; Servillo, L | 1 |
| Andersson, LA; Dawson, JH; Hahn, JE; Hodgson, KO | 1 |
| Fujitani, K; Hatayama, E; Kato, H; Sakurai, H | 1 |
| Alben, JO; Bare, GH | 1 |
| Baldwin, JM | 1 |
| Kimura, H; Murata, H; Uematsu, H | 1 |
| Büschlen, S; Kuras, R; Wollman, FA | 1 |
| Chen, PF; Tsai, AL; Wu, KK | 1 |
| Masters, BS; McMillan, K | 1 |
| Ferrer, JC; Hildebrand, DP; Mauk, AG; Smith, M; Tang, HL | 1 |
| Barker, PD; Fearnley, IM; Freund, SM; Nerou, EP | 1 |
| Dawson, JH; Hager, LP; Hedman, B; Hodgson, KO; Kadkhodayan, S; Liu, HI; Sono, M | 1 |
| Brinigar, WS; Bucci, JL; Chiancone, E; Fronticelli, C; Gattoni, M; Lu, AL | 1 |
| Boffi, A; Chiancone, E; Colotti, G; Verzili, D | 1 |
| Reed, VD; Smith, RC; Webb, TR | 1 |
| Adachi, S; Egawa, T; Ishimori, K; Kitagawa, T; Makino, R; Morishima, I; Nagano, S; Watanabe, Y | 1 |
| Goldman, BS; Roth, JR | 1 |
| Hu, S; Kincaid, JR | 1 |
| Balasubramanian, S; Boxer, SG; Lambright, DG | 1 |
| Weismann, H | 1 |
| Ishimori, K; Matsui, T; Morishima, I; Nagano, S; Watanabe, Y | 1 |
| Fazzio, TG; Roth, JR | 1 |
| Gorren, AC; Mayer, B; Schmidt, K; Schrammel, A | 1 |
| Behar, S; He, D; Lim, HW; Roberts, JE | 1 |
| Heathcote, P; Rambach, A; Raux, E; Thermes, C; Warren, MJ | 1 |
| Alderton, WK; Boyhan, A; Charles, IG; Cubberley, RR; Lowe, PN; Old, RW | 1 |
| Oganesyan, VS; Sharonov, YA | 1 |
| Bondon, A; Jung, C; Mouro, C; Simonneaux, G | 1 |
| Fan, B; Rousseau, DL; Stuehr, DJ; Wang, J | 1 |
| Cole, JA; Eaves, DJ; Griffiths, I; Grove, J; James, P; Poole, RK; Staudenmann, W; White, SA | 1 |
| Abugo, OO; Balagopalakrishna, C; Horsky, J; Manoharan, PT; Nagababu, E; Rifkind, JM | 1 |
| Gow, AJ; Hausladen, A; Stamler, JS | 1 |
| Arnone, A; Chan, NL; Rogers, PH | 1 |
| Gross, SS; Ikeda-Saito, M; Liu, Q; Martásek, P; Masters, BS; Migita, CT; Miller, RT; Raman, CS; Roman, LJ; Salerno, JC | 1 |
| Král, V; Li, H; Martásek, P; Masters, BS; Poulos, TL; Raman, CS | 1 |
| Beauvais, F; Joly, F | 1 |
| Bonaventura, C; Bonaventura, J; Crumbliss, AL; Godette, G; Holm, DE; Pearce, LL; Peterson, J; Tesh, S | 1 |
| Burstyn, JN; Chung, SY; Kerby, RL; Parks, RB; Reynolds, MF; Roberts, GP; Shelver, D; Thorsteinsson, MV | 1 |
| Hildebrand, DP; Liu, Y; Loehr, TM; Mauk, AG; Moënne-Loccoz, P; Ortiz de Montellano, PR; Wilks, A | 1 |
| Dawson, JH; Lu, Y; Pond, AE; Sigman, JA | 1 |
| Bravo, J; Bujons, J; Ens, W; Fita, I; Hu, B; Loewen, PC; Maté, MJ; Sevinc, MS; Switala, J | 1 |
| Bonaventura, J; Braun, R; Dewhirst, M; Goldberg, DE; Gow, AJ; Minning, DM; Stamler, JS | 1 |
| Hager, LP; Manoj, KM; Mroczko, M; Wang, X; Yi, X | 1 |
| Koesling, D | 1 |
| Barker, PD; Fearnley, IM; Rice, JK | 1 |
| Arnesano, F; Banci, L; Barker, PD; Bertini, I; Ciofi-Baffoni, S; Johnson, CM; Woodyear, TL | 1 |
| Chen, IP; Koepke, J; Mathis, P; Michel, H | 1 |
| Ferguson, SJ; Tomlinson, EJ | 1 |
| Gladwin, MT; Nichols, JS; Ognibene, FP; Pannell, LK; Pease-Fye, ME; Schechter, AN; Shelhamer, JH | 1 |
| Borovok, N; Einarsdóttir, O; Hazani, M; Kotlyar, A; Szundi, I | 1 |
| Alayash, AI; Cashon, RE; Hrinczenko, BW; Pannell, LK; Schechter, AN; Wojtkowski, TL | 1 |
| Finkelstein, JD | 1 |
| Marletta, MA; Rusche, KM | 1 |
| Ishimori, K; Morishima, I; Takahashi, S; Yoshioka, S | 1 |
| Lounnas, V; Lüdemann, SK; Wade, RC | 1 |
| Chapman, SK; Cheesman, MR; Miles, CS; Mowat, CG; Munro, AW; Quaroni, LG; Reid, GA | 1 |
| Aono, S; Honma, Y; Kato, T; Miyatake, H; Nakajima, H; Park, SY; Shiro, Y; Tawara, T | 1 |
| Banerjee, R; Green, EL; Loehr, TM; Taoka, S | 1 |
| Alonso-Alija, C; Apeler, H; Becker, EM; Dembowsky, K; Feurer, A; Gerzer, R; Minuth, T; Perzborn, E; Pleiss, U; Schramm, M; Schröder, H; Schroeder, W; Stahl, E; Stasch, JP; Steinke, W; Straub, A | 1 |
| Adak, S; Stuehr, DJ | 1 |
| Brennan, L; Fareleira, P; Santos, H; Turner, DL | 1 |
| Cox, RL; Donohue, TJ; Ríos-Velázquez, C | 1 |
| Adak, S; Couture, M; Rousseau, DL; Stuehr, DJ | 1 |
| Huang, TJ; Maines, MD; McCoubrey, WK | 1 |
| Adachi, O; Devreese, B; Duine, JA; Hacisalihoglu, A; Iwabuki, H; Jongejan, JA; Kim, JK; Kuroda, S; Okajima, T; Tanizawa, K; Van Beeumen, J; Vandenberghe, I | 1 |
| Benson, DE; Champion, PM; Christian, JF; Macdonald, ID; Sjodin, T; Sligar, SG; Unno, M | 1 |
| Babcock, GT; Berka, V; Schelvis, JP; Tsai, AL | 1 |
| Allen, JW; Ferguson, SJ; Hong, L; Tomlinson, EJ | 1 |
| Mauk, AG; Rosell, FI | 1 |
| Biel, S; Eichler, R; Gross, R; Pisa, R; Simon, J | 1 |
| Bonaventura, C; Ferruzzi, G; Godette, G; Henkens, R; Stevens, RD; Tesh, S | 1 |
| Amiconi, G; Boffi, A; Chiancone, E; Sarti, P | 1 |
| Banerjee, R; Kabil, O; Lepore, BW; Ojha, S; Ringe, D; Taoka, S | 1 |
| Cheng, Y; Ho, C; Shen, TJ; Simplaceanu, V | 1 |
| Kimura, H | 1 |
| Daltrop, O; Ferguson, SJ | 1 |
| Adak, S; Dawson, JH; Goodin, DB; Ikeda-Saito, M; Perera, R; Pond, AE; Sono, M; Stuehr, DJ; Tomita, T; Voegtle, HL | 1 |
| Broell, H; Hammarström, B; Kao, JJ; Lindberg, M; Paigen, B; Stuhlmeier, KM; Wallbrandt, P | 1 |
| Daltrop, O; Ferguson, SJ; Smith, KM | 1 |
| Foster, MW; McMahon, TJ; Stamler, JS | 1 |
| Kots, A; Martin, E; Murad, F; Sharina, I | 1 |
| Davidson, VL; Mathews, FS; Okajima, T; Ono, K; Sun, D; Tanizawa, K; Uchida, M; Yamamoto, Y | 1 |
| BRYANT, MP; PITTMAN, KA | 1 |
| SCHWARTZ, HC; WALTERS, TR | 1 |
| Allen, JW; Barker, PD; Ferguson, SJ | 1 |
| Winge, DR | 1 |
| Arnone, A; Chan, NL; Kavanaugh, JS; Rogers, PH | 1 |
| Detweiler, CD; Guo, Q; Mason, RP | 1 |
| Ferguson, SJ; Redfield, C; Smith, LJ; Wain, R | 1 |
| Huang, ZX; Lu, JX; Wang, WH; Xie, Y; Yao, P | 1 |
| Bolognesi, M; Burmester, T; Dewilde, S; Green, BN; Hamdane, D; Hankeln, T; Kiger, L; Marden, MC; Moens, L; Pesce, A; Uzan, J | 1 |
| de Vitry, C; Desbois, A; Redeker, V; Wollman, FA; Zito, F | 1 |
| Alric, J; Hienerwadel, R; Matsuura, K; Nagashima, KV; Nitschke, W; Schoepp-Cothenet, B; Shimada, K; Tsukatani, Y; Verméglio, A; Yoshida, M | 1 |
| Egawa, T; Hishiki, T; Ichikawa, Y; Ishimura, Y; Kanamori, Y; Kitagawa, T; Shimada, H; Takahashi, S | 1 |
| Botchkareva, AE; Davydov, DR; Halpert, JR; He, YQ; Kumar, S | 1 |
| Bonaventura, J; Frehm, EJ; Gow, AJ | 1 |
| Ishimori, K; Morishima, I; Tosha, T; Yoshioka, S | 1 |
| Leelavanichkul, K; Pitt, BR; St Croix, CM; Stitt, MS; Wasserloos, KJ; Watkins, SC | 1 |
| Bottin, H; Boussac, A; Ducruet, JM; Kirilovsky, D; Ortega, JM; Roncel, M; Rutherford, AW; Sugiura, M; Wilson, A; Zurita, JL | 1 |
| Ferrand, M; Franc, JL; Le Fourn, V | 1 |
| Couture, M; Li, D; Rousseau, DL; Yeh, SR | 1 |
| Coon, MJ; Peng, HM; Vatsis, KP | 1 |
| Das, A; Kurtz, DM; Ljungdahl, LG; Silaghi-Dumitrescu, R | 1 |
| Erwin, PA; Marletta, MA; Michel, T; Mitchell, DA | 1 |
| Kitagawa, T; Sagami, I; Sato, A; Sato, E; Shimizu, T; Uchida, T | 1 |
| Gorren, AC; Koesling, D; Kollau, A; Mayer, B; Russwurm, M; Schmidt, K | 1 |
| Mazumdar, S; Murugan, R | 1 |
| Arhan, P; Bouglé, D; Bureau, F; Guillochon, D; Nedjaoum, F; Vaghefi, N | 1 |
| Fujii, J; Ohba, Y; Sato, K; Suto, D; Yoshimura, T | 1 |
| Hori, H; Ishikawa, H; Ishimori, K; Iwai, K; Kato, M; Kirisako, T; Tokunaga, F | 1 |
| Azuma, K; Fukuba, M; Funasaki, N; Hirota, S; Kuroiwa, S | 1 |
| Bokoch, MP; Perroud, TD; Zare, RN | 1 |
| Azarov, I; Basu, S; Huang, J; Huang, KT; Kim-Shapiro, DB | 1 |
| Morais, F; Pereira, IA; Pires, RH; Teixeira, M; Venceslau, SS; Xavier, AV | 1 |
| Carotti, A; Cavalli, A; Favia, AD; Masetti, M; Recanatini, M | 1 |
| Deng, H; Hayden, EY; Li, D; Panda, K; Rousseau, DL; Stuehr, DJ; Yeh, SR | 1 |
| Chait, BT; Fushitani, K; Gorr, TA; Kao, WY; Knapp, JE; Qin, J; Riggs, AF; Riggs, CK; Smith, SS | 1 |
| Greenburg, AG; Kim, HW | 1 |
| Akazaki, H; Chida, H; Hirano, T; Kawachi, R; Kawai, F; Nakazawa, A; Nishio, T; Oku, T; Park, SY; Satoh, T; Suruga, K; Takayama, Y; Unzai, S; Yamada, S; Yokoyama, T | 1 |
| Bryan, NS; Feelisch, M; Gladwin, MT; MacArthur, PH; Rodriguez, J; Wang, X | 1 |
| Deeb, RS; Hajjar, DP; Upmacis, RK | 1 |
| Chung, SY; Conrad, M; Roberts, GP; Youn, H | 1 |
| Borel, F; de Groot, A; de Rosny, E; Fontecilla-Camps, JC; Gaillard, J; Jouve, HM; Jullian-Binard, C; Pebay-Peyroula, E | 1 |
| Cramer, WA; Gunderson, WA; Hendrich, MP; Zatsman, AI; Zhang, H | 1 |
| Benedict, JB; Dey, A; Kaminsky, W; Kitagawa, T; Kovacs, JA; Lugo-Mas, P; Solomon, E | 1 |
| Kagawa, N; Kelly, SL; Lamb, DC; Lei, L; Rupasinghe, S; Schuler, MA; Waterman, MR; Yuan, H; Zhao, B | 1 |
| Alayash, AI; Boykins, RA; Buehler, PW; Jia, Y; Venable, RM | 1 |
| Adlercreutz, P; Grey, CE; Hedström, M | 1 |
| El-Mashtoly, S; Hirai, K; Igarashi, J; Kitagawa, T; Martinkova, M; Saiful, I; Shimizu, T; Yamauchi, S | 1 |
| Chen, Z; Davis, MF; de Serrano, V; Franzen, S | 1 |
| Hu, RG; Varshavsky, A; Wang, H; Xia, Z | 1 |
| Kanaori, K; Kitajima, S; Kurioka, M; Oda, K; Shindo, M; Tajima, K; Yoshimoto, T | 1 |
| Bröcker, MJ; Ganskow, S; Heathcote, P; Heinz, DW; Jahn, D; Moser, J; Schubert, WD; Virus, S | 1 |
| Allen, JW; Ferguson, SJ; Ginger, ML; Jackson, AP; Rigden, DJ; Willis, AC | 1 |
| Hayasaka, K; Hikage, N; Igarashi, J; Ishimori, K; Kitanishi, K; Saiful, I; Shimizu, T; Uchida, T; Yamauchi, S | 1 |
| Tsoukias, NM | 1 |
| Harada, S; Hirayama, K; Huy, NT; Kamei, K; Nhien, NT; Oida, T; Trang, DT; Uyen, DT | 1 |
| Archer, M; Matias, PM; Oliveira, TF; Pereira, IA; Venceslau, SS; Vonrhein, C | 1 |
| Carvajal, MA; Chen, H; Cho, KB; Cohen, S; Derat, E; Hirao, H; Shaik, S; Thiel, W | 1 |
| Dawson, JH; Goodin, DB; Osborne, RL; Terentis, AC; Vetter, SW | 1 |
| Allen, JW; Barker, PD; Ferguson, SJ; Ginger, ML; Sawyer, EB | 1 |
| de Visser, SP; Straganz, GD | 1 |
| Burstyn, JN; Cherney, MM; Farmer, PJ; Francoleon, NE; Fukuto, JM; Hobbs, AJ; King, SB; Lee, AJ; Miller, TW; Miranda, KM | 1 |
| Couture, M; Driscoll, D; Gélinas, S; Lang, J; Rafferty, SP | 1 |
| Cieluch, E; Osyczka, A; Pietryga, K; Sarewicz, M | 1 |
| Greenburg, AG; Hai, CM; Kim, HW | 1 |
| Allen, JW; Barker, PD; Ferguson, SJ; Sawyer, EB; Stephens, E | 1 |
| Daldal, F; Lee, DW; Sanders, C; Turkarslan, S | 1 |
| Morgan, JT; Ragsdale, SW; Yi, L | 1 |
| Banerjee, R; de Armas, M; Ibba, M; Katz, A; Orellana, O | 1 |
| Ford, PC; Heinecke, J | 1 |
| Lei, HY; Wang, ED; Xia, X; Yang, F | 1 |
| Gupta, N; Ragsdale, SW | 1 |
| Dawson, JH; Perera, R; Sono, M; Voegtle, HL | 1 |
| Bamba, A; Hori, H; Ishikawa, H; Ishimori, K; Iwai, K; Nakagaki, M; O'Brian, MR; Uchida, T | 1 |
| Beckerich, JM; Casaregola, S; Hébert, A | 1 |
| Barr, I; Burstyn, JN; Chen, Y; Guo, F; Scheidemantle, BD; Senturia, R; Smith, AT | 1 |
| Burstyn, JN; Freeman, KM; Kraus, JP; Majtan, T; Smith, AT; Su, Y | 1 |
| Beliaev, AS; Bradley, J; Butt, JN; Clarke, TA; Edwards, MJ; Fredrickson, JK; Gates, AJ; Hall, A; Marshall, MJ; Reardon, CL; Richardson, DJ; Shi, L; Wang, Z; Watmough, NJ; White, GF; Zachara, JM | 1 |
| Ducsay, CA; Myers, DA | 1 |
| Dewilde, S; Ezhevskaya, M; Moens, L; Trandafir, F; Van Doorslaer, S | 1 |
| Hoffmann, C; Hoffmann, LS; Keim, Y; Schmidt, HH; Schmidt, PM; Stasch, JP | 1 |
| Amunugama, H; Cooper, N; Hollenberg, PF; Ney, S; Zhang, H | 1 |
| Ibrahim, SM; Nakajima, H; Naruta, Y; Ohta, T; Ramanathan, K; Takatani, N; Watanabe, Y | 1 |
| Couture, M; Lang, J; Santolini, J | 1 |
| Bendall, DS; Howe, CJ; Mason, JM; Worrall, JA | 1 |
| Shimizu, T | 1 |
| Ishimori, K; Kitagawa, T; Sagami, I; Shimizu, T; Uchida, T | 1 |
| Bild, V; Bild, W; Ciobica, A; Padurariu, M | 1 |
| Lampe, JN; Ortiz de Montellano, PR; Varfaj, F | 1 |
| Derbyshire, ER; Fernhoff, NB; Marletta, MA; Underbakke, ES | 1 |
| Banerjee, R; Yadav, PK | 1 |
| Astudillo, L; Bernad, S; Derrien, V; Miksovska, J; Sebban, P | 1 |
| Knipp, M; Nalepa, AI; Savitsky, A; Taing, JJ | 1 |
| Bouley Ford, ND; Ford, WC; Gray, HB; Keller, GE; Winkler, JR; Yamada, S | 1 |
| Ferguson, SJ; Mavridou, DA; Stevens, JM | 1 |
| Cuypers, B; Desmet, F; Dewilde, S; Giordano, D; Moens, L; Van Doorslaer, S; Van Leuven, W; Verde, C | 1 |
| Aono, S; Ishida, T | 1 |
| Fabre, PL; Ibrahim, H; Najahi, E; Nepveu, F; Perio, P; Reybier, K; Souard, F; Yen, NT | 1 |
| Galler, K; Goradia, N; Heinemann, SH; Imhof, D; Kühl, T; Neugebauer, U; Ohlenschläger, O; Popp, J; Sahoo, N; Wißbrock, A | 1 |
| Austin, CJ; Jamie, JF; Kosim-Satyaputra, P; Smith, JR; Willows, RD | 1 |
| Alvarez, B; Ballou, DP; Banerjee, R; Carballal, S; Cuevasanta, E; Gherasim, C; Kabil, O; Marmisolle, I | 1 |
| Kranz, RG; San Francisco, B; Sutherland, MC | 1 |
| Collins, DP; Dawson, JH; Lisi, GP; Pletneva, EV; Zhong, F | 1 |
| Her, AS; Huo, Y; Liu, P; Raso, F; Song, H; Zhen, Z | 1 |
| Fago, A; Gow, AJ; Helbo, S; Howes, BD; Jamil, A; Smulevich, G | 1 |
| Astashkin, AV; Chen, L; Feng, C; Guillemette, JG; Li, H; Liu, KJ; Poulos, TL; Zhou, X | 1 |
| Babbitt, SE; Bretsnyder, EC; Kranz, RG; Lukat-Rodgers, GS; Mendez, DL; Rodgers, KR; San Francisco, B | 1 |
| Einsle, O; Hermann, B; Kern, M; La Pietra, L; Simon, J | 1 |
| Kelly, DJ; Liu, YW | 1 |
| Gadalla, MM; Kumar, GK; Makarenko, VV; Nanduri, J; Peng, YJ; Prabhakar, NR; Raghuraman, G; Semenza, GL; Snyder, SH; Vasavda, C; Yuan, G | 1 |
| Ferguson, SJ; Redfield, C; Smith, LJ; Tozawa, K | 1 |
| Duthie, F; Florin, N; Hagelueken, G; Henning Brewitz, H; Imhof, D; Kühl, T; Schiemann, O; Schubert, E | 1 |
| Nagaoka, H | 1 |
| Higashimoto, Y; Koga, S; Komatsu, H; Morimatsu, H; Nakashima, Y; Sakamoto, H; Shimizu, H; Sueda, S; Taira, J; Takahashi, T; Tanioka, N; Yoshihara, S | 1 |
| Alayash, AI; Jana, S; Jia, Y; Kassa, T; Meng, F; Strader, MB; Wilson, MT | 1 |
| Chen, W; Chen, Y; Peng, H; Rizzo, AN; Zhuang, Y | 1 |
| Loullis, A; Pinakoulaki, E | 1 |
| Hederstedt, L; Lewin, A | 1 |
| Beuve, A | 1 |
| Bernhardt, PV; Dhouib, R; Hanson, GR; Kappler, U; Kilmartin, JR; Riley, MJ | 1 |
| Amartely, H; Dvir, H; Kornitzer, D; Nasser, L; Pinsky, M; Weissman, Z | 1 |
| Chen, L; Elmore, BO; Fan, W; Feng, C; Lehnert, N; McQuarters, AB; Speelman, AL | 1 |
| Barr, I; Burstyn, JN; Guo, F; Hines, JP; Jacob, JP; Lukat-Rodgers, GS; Rodgers, KR; Smith, AT | 1 |
| Lancaster, JR | 1 |
| Ishimori, K; Uchida, T; Watanabe, Y | 1 |
| Banerjee, R; Filipovic, MR; Kumutima, J; Lehnert, N; Lewis, BE; Ruetz, M; Stemmler, TL | 1 |
| Banerjee, R | 1 |
| Ishimori, K; Kobayashi, N; Muneta, S; Uchida, T | 1 |
| Babbitt, SE; Hsu, J; Kranz, RG; Mendez, DL | 1 |
| Daldal, F; Hwang, J; Khalfaoui-Hassani, B; Khatchikian, CE; Sanders, C; Selamoglu, N; Steimle, S; Verissimo, AF | 1 |
| Battistuzzi, G; Bellei, M; Borsari, M; Bortolotti, CA; Di Rocco, G; Lancellotti, L; Ranieri, A; Sola, M | 1 |
| Reeder, BJ; Ukeri, J | 1 |
| Hamza, I; Yuan, X | 1 |
| Baker, D; Jarodsky, JM; Kranz, RG; Ovchinnikov, S; Sutherland, MC | 1 |
| Berkowitz, DB; Hill, M; Kreinbring, CA; Liu, C; Liu, D; McCune, CD; Petsko, GA; Ringe, D; Tu, Y | 1 |
| Benlekbir, S; Gennis, RB; Hong, S; Hosler, J; Rubinstein, JL; Sun, C; Tajkhorshid, E; Venkatakrishnan, P; Wang, Y | 1 |
| Gray, HB; Winkler, JR | 1 |
| Arnold, FH; Chen, K; Huang, X; Renata, H; Wohlschlager, L; Zhang, RK | 1 |
| Bozinovic, N; Dimitrov, JD; Lacroix-Desmazes, S; Lecerf, M; Noé, R | 1 |
| Brânzanic, AMV; Ryde, U; Silaghi-Dumitrescu, R | 1 |
| Capelletti, MM; Manceau, H; Peoc'h, K; Puy, H | 1 |
| Astegno, A; Conter, C; Dominici, P; Fernández-Rodríguez, C; Fruncillo, S; Martínez-Cruz, LA | 1 |
| Akerström, B; Alvarado, G; Balla, G; Balla, J; Csernátony, Z; Csősz, É; Dankó, K; Édes, I; Gram, M; Kalló, G; Papp, Z; Smith, A; Tóth, A | 1 |
| Demeler, B; Iranzo, O; Ivancich, A; Koebke, KJ; Kühl, T; Lojou, E; Pecoraro, VL; Schoepp-Cothenet, B | 1 |
| Bollinger, JM; Krebs, C; Liu, G; Maio, N; Rouault, TA; Sil, D; Tong, WH | 1 |
| Harvey, JN; Roos, G | 1 |
| Bocharova, OV; Borovok, N; Chertkova, RV; Dolgikh, DA; Groma, GI; Khoroshyy, P; Kirpichnikov, MP; Kotlyar, AB; Tenger, K; Zimányi, L | 1 |
| Nutho, B; Pornsuwan, S; Prasertsuk, P; Samsri, S | 1 |
| Dutra, M; Garashchuk, S; Makris, T; Manley, O; McElhenney, S; Rassolov, V | 1 |
| Alhhazmi, A; Andorfer, MC; Avalos, DM; Babu, VMP; Bian, K; Drennan, CL; Lourido, S; Sankari, S; Smith, TA; Walker, GC; Yaffe, MB; Yoon, K | 1 |
| Chen, T; Cui, Z; He, G; Jiang, M; Sun, X; Wang, Z | 1 |
| Aerts, R; Berghmans, H; Braeckman, BP; Breugelmans, T; Ching, HYV; De Henau, S; Defossé, S; Dewilde, S; Hafideddine, Z; Hammerschmid, D; Herrebout, W; Johannessen, C; Loier, T; Moens, L; Moons, R; Neukermans, S; Sgammato, R; Sobott, F; Van Brempt, N; Van Doorslaer, S | 1 |
| Álvarez-Armenta, A; Corona-Martínez, DO; García-Sánchez, G; López-Zavala, AA; Pacheco-Aguilar, R; Ramírez-Suárez, JC; Sotelo-Mundo, RR | 1 |
| Badgandi, HB; Montfort, WR; Weichsel, A | 1 |
19 review(s) available for heme and cysteine
| Article | Year |
|---|---|
Allosteric interpretation of haemoglobin properties.
Topics: Allosteric Site; Binding Sites; Carbon Monoxide; Chemical Phenomena; Chemistry, Organic; Chemistry, Physical; Cysteine; Diphosphoglyceric Acids; Heme; Hemoglobins; Hemoglobins, Abnormal; Hydrogen-Ion Concentration; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Models, Chemical; Organic Chemistry Phenomena; Organophosphorus Compounds; Oxygen; Protein Conformation; Protons; Spin Labels; Structure-Activity Relationship | 1975 |
Studying the structure and regulation of soluble guanylyl cyclase.
Topics: Animals; Biochemistry; Cysteine; DNA Mutational Analysis; Enzyme Activation; Guanylate Cyclase; Heme; Histidine; Isoenzymes; Solubility | 1999 |
Pathways and regulation of homocysteine metabolism in mammals.
Topics: Animals; Cystathionine; Cystathionine beta-Synthase; Cystathionine gamma-Lyase; Cysteine; Heme; Homocysteine; Isoenzymes; Kinetics; Mammals; Methionine; Methionine Adenosyltransferase; Organ Specificity; Oxidation-Reduction; Pyridoxal Phosphate; S-Adenosylhomocysteine; S-Adenosylmethionine; Sulfur; Tetrahydrofolates | 2000 |
Hydrogen sulfide as a neuromodulator.
Topics: Animals; Brain Chemistry; Calcium; Calmodulin; Cattle; Central Nervous System Diseases; Corticotropin-Releasing Hormone; Cystathionine beta-Synthase; Cystathionine gamma-Lyase; Cysteine; Heme; Hippocampus; Humans; Hydrogen Sulfide; Hypothalamus; Long-Term Potentiation; Mice; Muscle Proteins; Muscle Relaxation; Nerve Tissue Proteins; Neurotransmitter Agents; Nitric Oxide; Pyridoxal Phosphate; Rats; Synaptic Transmission | 2002 |
S-nitrosylation in health and disease.
Topics: Copper; Cysteine; Disease; Heme; Humans; Nitric Oxide; Nitric Oxide Synthase; Nitrites; Nitroso Compounds; Oxidation-Reduction; Sulfur | 2003 |
S-Nitrosohemoglobin: an allosteric mediator of NO group function in mammalian vasculature.
Topics: Allosteric Site; Animals; Biological Transport; Cysteine; Endothelium, Vascular; Heme; Hemoglobins; Humans; Models, Biological; Nitric Oxide | 2004 |
Ligand-protein interactions in nitric oxide synthase.
Topics: Carbon Monoxide; Catalytic Domain; Cysteine; Heme; Hydrogen Bonding; Isoenzymes; Ligands; Molecular Structure; Nitric Oxide Synthase; Oxygen; Spectrum Analysis, Raman | 2005 |
Oxidative alterations of cyclooxygenase during atherogenesis.
Topics: Animals; Arachidonic Acid; Atherosclerosis; Cyclooxygenase Inhibitors; Cysteine; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Enzyme Activation; Heme; Humans; Intramolecular Oxidoreductases; MAP Kinase Signaling System; Nitric Oxide; Nitrogen Oxides; Oxidation-Reduction; Peroxynitrous Acid; Prostaglandin-Endoperoxide Synthases; Tyrosine | 2006 |
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 |
Nitric oxide bioavailability in the microcirculation: insights from mathematical models.
Topics: Animals; Cyclic GMP; Cysteine; Diffusion; Endothelium, Vascular; Erythrocytes; Guanylate Cyclase; Heme; Hemoglobins; Humans; Microcirculation; Microvessels; Models, Cardiovascular; Nitric Oxide; Nitric Oxide Synthase Type III; Reactive Oxygen Species; Receptors, Cytoplasmic and Nuclear; Signal Transduction; Soluble Guanylyl Cyclase; Sulfhydryl Compounds; Vasodilation | 2008 |
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 |
eNOS activation and NO function: differential control of steroidogenesis by nitric oxide and its adaptation with hypoxia.
Topics: Adrenal Glands; Animals; Cyclic GMP; Cysteine; Enzyme Activation; Female; Guanylate Cyclase; Heme; Humans; Hypoxia; Male; Models, Biological; Nitric Oxide; Nitric Oxide Synthase Type III; Ovary; Pregnancy; Protein Processing, Post-Translational; Steroids; Testis; Tyrosine | 2011 |
Binding of cysteine thiolate to the Fe(III) heme complex is critical for the function of heme sensor proteins.
Topics: Animals; Circadian Rhythm; Cysteine; Ferric Compounds; Heme; Humans; Oxidation-Reduction | 2012 |
The interdependence of the reactive species of oxygen, nitrogen, and carbon.
Topics: Arginine; Carbon; Carbon Monoxide; Carbon-Sulfur Lyases; Cysteine; Heme; Heme Oxygenase (Decyclizing); Humans; Hydrogen Sulfide; Nitric Oxide Synthase; Oxidation-Reduction; Oxidative Stress; Reactive Nitrogen Species; Reactive Oxygen Species | 2013 |
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 |
Thiol-Based Redox Modulation of Soluble Guanylyl Cyclase, the Nitric Oxide Receptor.
Topics: Animals; Cardiovascular Diseases; Catalysis; Cysteine; Heme; Humans; Nitric Oxide; Nitrosation; Oxidation-Reduction; Protein Binding; Soluble Guanylyl Cyclase; Solvents; Structure-Activity Relationship; Sulfhydryl Compounds | 2017 |
How are nitrosothiols formed de novo in vivo?
Topics: Animals; Cysteine; Heme; Humans; Ions; Iron; Ligands; Metals; Nitric Oxide; Nitrogen; Nitrosation; Oxidation-Reduction; Oxidative Stress; Oxygen; Protein Processing, Post-Translational; S-Nitrosothiols; Signal Transduction | 2017 |
Catalytic promiscuity and heme-dependent redox regulation of H
Topics: Animals; Biocatalysis; Cysteine; Heme; Humans; Hydrogen Sulfide; Oxidation-Reduction; Substrate Specificity | 2017 |
Ferroptosis in Liver Diseases: An Overview.
Topics: alpha-Tocopherol; Animals; Autophagy; Chemical and Drug Induced Liver Injury; Cyclohexylamines; Cysteine; Ferroptosis; Glutathione; Heme; Humans; Iron; Kelch-Like ECH-Associated Protein 1; Lipid Peroxidation; Lipoxygenase; Liver Diseases; Liver Neoplasms; Oxidative Stress; Phenylenediamines; Phospholipid Hydroperoxide Glutathione Peroxidase; Piperazines; Quinoxalines; Reactive Oxygen Species; Reperfusion Injury; Signal Transduction; Sorafenib; Spiro Compounds; Sulfasalazine; Tumor Suppressor Protein p53 | 2020 |
267 other study(ies) available for heme and cysteine
| Article | Year |
|---|---|
[Studies on cytochrome c oxidase, I. Purification and characterization of bovine myocardial enzyme and identification of peptide chains in the complex].
Topics: Amino Acids; Animals; Cattle; Copper; Cysteine; Electron Transport Complex IV; Heme; Iron; Molecular Weight; Myocardium; Peptide Fragments; Phospholipids | 1976 |
Heme reactivity of hemoglobins. Azide and fluoride binding equilibria of free and mercuriated ferri-gamma chains.
Topics: Azides; Binding Sites; Calorimetry; Cysteine; Electron Spin Resonance Spectroscopy; Female; Ferric Compounds; Fetal Hemoglobin; Fluorides; Heme; Humans; Hydrogen-Ion Concentration; Kinetics; Ligands; Macromolecular Substances; Mercuribenzoates; Mercury; Oxidation-Reduction; Pregnancy; Protein Binding; Protein Conformation; Temperature; Thermodynamics | 1975 |
Regulation of heme pathway enzymes and cellular glutathione content by metals that do not chelate with tetrapyrroles: blockade of metal effects by thiols.
Topics: 5-Aminolevulinate Synthetase; Animals; Binding Sites; Cobalt; Cysteine; Cytochrome P-450 Enzyme System; Enzyme Induction; Glutathione; Heme; Kidney; Liver; Male; Microsomes; Microsomes, Liver; Mixed Function Oxygenases; Nickel; Platinum; Rats; Trace Elements | 1977 |
Purification and properties of cytochrome b-562.5 from Ulva pertusa.
Topics: Ascorbic Acid; Chlorophyta; Cysteine; Cytochromes; Ferricyanides; Heme; Molecular Weight; Oxidation-Reduction; Peroxidases; Potentiometry; Spectrophotometry | 1979 |
Bromotrifluoroacetone alkylates hemoglobin at cysteine beta93.
Topics: Acetone; Amino Acids; Borohydrides; Cysteine; Globins; Heme; Hemoglobins; Humans; Magnetic Resonance Spectroscopy; Peptide Fragments | 1978 |
Studies on the mechanism of induction of haem oxygenase by cobalt and other metal ions.
Topics: 5-Aminolevulinate Synthetase; Animals; Bilirubin; Cations, Divalent; Cobalt; Cysteine; Cytochrome P-450 Enzyme System; Enzyme Induction; Ethylmorphine-N-Demethylase; Glutathione; Heme; Liver; Male; Maleates; Metals; Microsomes, Liver; NADPH-Ferrihemoprotein Reductase; Oxygenases; Rats; Vitamin E | 1976 |
Lipid-oxidation catalyses by substances in water on lipid-water interface.
Topics: Ascorbic Acid; Catalysis; Cysteine; Heme; Lipids; Oxidation-Reduction; Sulfates; Surface Properties; Water | 1976 |
[Structure of nitroso pigments in meats].
Topics: Amino Acids; Ascorbic Acid; Chemical Phenomena; Chemistry; Cysteine; Food Preservation; Heme; Histidine; Meat; Models, Chemical; Nitroso Compounds; Pigments, Biological; Pyrroles | 1976 |
ORTHO-and PARA-selectivity in aromatic hydroxylation by iron-thiol and hemin-thiol complexes.
Topics: Amines; Aminobenzoates; Aniline Compounds; Cysteine; Ferrous Compounds; Heme; Hemin; Hydroxylation; Iron; Phenols; Salicylates; Structure-Activity Relationship; Sulfhydryl Compounds | 1975 |
Aromatic methyl migration by iron-thiol and hemin-thiol systems.
Topics: Cysteine; Cytochrome P-450 Enzyme System; Heme; Hemin; Hydroxylation; Iron; Methylation; Models, Biological; Oxygenases; Pyridines; Sulfhydryl Compounds; Toluidines | 1975 |
Heme-deficient mutants of Salmonella typhimurium: two genes required for ALA synthesis.
Topics: Aminolevulinic Acid; Chromosome Mapping; Cysteine; Cytochromes; Genes, Bacterial; Genetic Complementation Test; Heme; Mutation; Salmonella typhimurium; Transcription, Genetic; Vitamin B 12 | 1989 |
Electrostatic interactions in wild-type and mutant recombinant human myoglobins.
Topics: Codon; Cyanides; Cysteine; Genetic Vectors; Heme; Humans; Kinetics; Molecular Conformation; Mutation; Myoglobin; Protein Binding; Protein Conformation; Recombinant Proteins; Spectrophotometry; Valine | 1989 |
Studies on fatty-acid-binding proteins. The purification of rat liver fatty-acid-binding protein and the role of cysteine-69 in fatty acid binding.
Topics: Animals; Carrier Proteins; Chromatography, Affinity; Cysteine; Dithionitrobenzoic Acid; Fatty Acid-Binding Protein 7; Fatty Acid-Binding Proteins; Fatty Acids; Heme; Ligands; Liver; Neoplasm Proteins; Nerve Tissue Proteins; Rats; Rats, Inbred Strains | 1989 |
Synthetic analogs of the active site of cytochrome P-450cam characterization of thiolpeptide fragment-hemin complexes by optical and ESR spectrometries.
Topics: Amino Acid Sequence; Binding Sites; Cysteine; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Heme; Ligands; Oligopeptides; Pseudomonas; Spectrophotometry | 1985 |
Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon-13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes.
Topics: Carbon Monoxide; Chloride Peroxidase; Cysteine; Cytochrome-c Peroxidase; Heme; Hemeproteins; Histidine; Horseradish Peroxidase; Imidazoles; Isoenzymes; Lactoperoxidase; Magnetic Resonance Spectroscopy; Myoglobin; Peroxidases | 1985 |
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 |
DNA strand scission by hemin-thiolate complexes as models of cytochrome P-450.
Topics: Cysteine; Cytochrome P-450 Enzyme System; DNA, Superhelical; Free Radicals; Glutathione; Heme; Hemin; Mercaptoethanol; Models, Chemical; Sulfhydryl Compounds; Superoxides; Thioglycolates; Tiopronin | 1986 |
Import of cytochrome c into mitochondria. Cytochrome c heme lyase.
Topics: Chromatography, High Pressure Liquid; Cysteine; Cytochrome c Group; Ethylmaleimide; Heme; Hemin; Lyases; Mitochondria; Models, Molecular; NAD; NADP; Neurospora crassa; Peptide Fragments; Protein Conformation; Reticulocytes; Trypsin | 1987 |
[Chemical modification of cysteine residues of cholesterol-hydroxylating cytochrome P-450. Identification of the cysteine residue participating in the formation of a proximal ligand].
Topics: Adrenal Cortex; Amino Acid Sequence; Animals; Cattle; Cholesterol; Cysteine; Cytochrome P-450 Enzyme System; Heme; Kinetics; Ligands; Mitochondria; Peptides; Sulfhydryl Compounds; Sulfhydryl Reagents | 1987 |
Characterization of two cysteine residues in cytochrome P-450scc: chemical identification of the heme-binding cysteine residue.
Topics: Adrenal Cortex; Animals; Binding Sites; Cattle; Cysteine; Cytochrome P-450 Enzyme System; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Heme; Isoenzymes; Kinetics; Mathematics; Molecular Weight; Structure-Activity Relationship | 1986 |
Studies on the identity of the heme-binding cysteinyl residue in rabbit liver microsomal cytochrome P-450 isozyme 2.
Topics: Animals; Binding Sites; Bridged Bicyclo Compounds; Cysteine; Cytochrome P-450 Enzyme System; Dithionitrobenzoic Acid; Heme; Isoenzymes; Kinetics; Microsomes, Liver; Rabbits | 1985 |
Circular dichroism and electron paramagnetic resonance of the haptoglobin-hemoglobin complex.
Topics: Chemical Phenomena; Chemistry; Circular Dichroism; Crystallography; Cyclic N-Oxides; Cysteine; Electron Spin Resonance Spectroscopy; Guaiacol; Haptoglobins; Heme; Hemoglobins; Humans; Hydrogen-Ion Concentration; Iodoacetates; Iron; Oxygen; Peroxidases; Piperidines; Porphyrins; Protein Binding; Protein Denaturation; Spectrophotometry | 1971 |
Reaction of sulfenyl halides with cytochrome c. A novel method for heme cleavage.
Topics: Amino Acid Sequence; Amino Acids; Animals; Autoanalysis; Binding Sites; Chemical Phenomena; Chemistry; Chromatography, Gel; Chromatography, Ion Exchange; Chromatography, Thin Layer; Cysteine; Cytochrome c Group; Heme; Horses; Myocardium; Oligopeptides; Protein Binding; Protein Denaturation; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfenic Acids | 1973 |
Comparative biological chemistry of cobalt hemoglobin.
Topics: Carbon Dioxide; Chloromercuribenzoates; Cobalt; Cyclic N-Oxides; Cysteine; Diphosphoglyceric Acids; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Humans; Hydrogen-Ion Concentration; Iron; Kinetics; Ligands; Mathematics; Oxidation-Reduction; Oxygen; Oxyhemoglobins; Potentiometry; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Sulfhydryl Compounds | 1973 |
Amino acid sequence of cytochrome c3 from Desulfovibrio vulgaris.
Topics: Amino Acid Sequence; Amino Acids; Apoproteins; Binding Sites; Chemical Phenomena; Chemistry; Chromatography, Gel; Chromatography, Paper; Chymotrypsin; Cysteine; Cytochrome c Group; Desulfovibrio; Heme; Histidine; Peptide Fragments; Peptides; Thiocyanates; Trypsin | 1974 |
The physical chemistry of hemes and hemopeptides. 3. Synthesis and physicochemical properties of cytochrome c-related heme--pentapeptide soluble in organic solvents.
Topics: Binding Sites; Chromatography, Ion Exchange; Cysteine; Cytochrome c Group; Drug Stability; Electron Spin Resonance Spectroscopy; Glycine; Heme; Hemeproteins; Histidine; Iron; Ligands; Oligopeptides; Optical Rotation; Oxidation-Reduction; Protein Binding; Protein Conformation; Solubility; Spectrophotometry; Spectrophotometry, Ultraviolet | 1974 |
The purification and amino acid sequence of cytochrome C-552 from Euglena gracilis.
Topics: Amino Acid Sequence; Centrifugation; Chromatography, DEAE-Cellulose; Chromatography, Gel; Cysteine; Cytochrome c Group; Cytochromes; Electrophoresis, Polyacrylamide Gel; Euglena gracilis; Heme; Hydroxylamines; Mitochondria; Tryptophan | 1974 |
Nutritional features of Bacteroides fragilis subsp. fragilis.
Topics: Anaerobiosis; Bacteroides; Bicarbonates; Carbon Dioxide; Culture Media; Cysteine; Glucose; Heme; Methionine; Minerals; Nitrogen; Quaternary Ammonium Compounds; Species Specificity; Sulfides; Sulfur; Vitamin B 12 | 1974 |
Cytochrome P-450cam. III. Removal and replacement of ferriprotoporphyrin IX.
Topics: Animals; Apoproteins; Benzoates; Carbon Monoxide; Cattle; Chloromercuribenzoates; Chromatography, Thin Layer; Cold Temperature; Cysteine; Cytochrome P-450 Enzyme System; Drug Stability; Glycerol; Heme; Hydrogen-Ion Concentration; Iron; Kinetics; Nitro Compounds; Oxidation-Reduction; Porphyrins; Pseudomonas; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfhydryl Compounds; Time Factors | 1974 |
Studies on the suitability of blood-free media for the enumeration of clostridia.
Topics: Agar; Bacteriological Techniques; Blood; Clostridium; Culture Media; Cysteine; Heme; Peptones | 1970 |
Anaerobic roll tube media for nonselective enumeration and isolation of bacteria in human feces.
Topics: Adult; Agar; Anaerobiosis; Analysis of Variance; Bacteria; Bacteriological Techniques; Brain; Carbon Dioxide; Culture Media; Cysteine; Evaluation Studies as Topic; Fatty Acids; Feces; Glucose; Heart; Heme; Humans; Hydrogen Sulfide; Hydrogen-Ion Concentration; Hydrolysis; Liver; Male; Methods; Nitrogen; Saccharomyces; Starch; Thioglycolates | 1971 |
Lysosomal hemochromes and digestion of cytochrome c by the lysosomal protease system.
Topics: Acid Phosphatase; Animals; Cathepsins; Chromatography; Chromatography, Gel; Cysteine; Cytochromes; Heme; Hydrogen-Ion Concentration; Hydroxyapatites; Liver; Lysosomes; Mitochondria, Liver; Pepsin A; Pronase; Rats; Spectrophotometry; Surface-Active Agents | 1971 |
Oxygen equilibrium and circular dichroism of hemoglobin-Rainer ( 2 2 1 45Tyr leads to Cys).
Topics: Amino Acid Sequence; Amino Acids; Chromatography, Ion Exchange; Circular Dichroism; Cysteine; Disulfides; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Oxygen; Peptides; Protein Conformation; Spectrophotometry; Sulfhydryl Compounds; Tyrosine; Ultraviolet Rays | 1972 |
The deoxygenation kinetics of hemoglobin Rainier ( 2 145 tyr change to cys).
Topics: Cysteine; Disulfides; Drug Stability; Glycerophosphates; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Kinetics; Oxygen; Peptides; Protein Binding; Protein Conformation; Tyrosine | 1972 |
Redox potentials of the pyridine-haem c system.
Topics: Chemical Phenomena; Chemistry; Chromatography, Ion Exchange; Cysteine; Heme; Hydrogen-Ion Concentration; Iron; Macromolecular Substances; Mathematics; Oxidation-Reduction; Porphyrins; Potentiometry; Pyridines; Quaternary Ammonium Compounds; Silver; Sulfides | 1972 |
The thiol groups of human hemoglobin carrying heme only on the -chains.
Topics: Acetamides; Amino Acids; Autoanalysis; Binding Sites; Chemical Phenomena; Chemistry; Cysteine; Heme; Hemoglobins, Abnormal; Humans; Iodoacetates; Kinetics; Macromolecular Substances; Mercuribenzoates; Protein Conformation; Structure-Activity Relationship; Sulfhydryl Compounds; Trypsin | 1972 |
Effect of glutathione and cysteine on rat liver tryptophan oxygenase activity.
Topics: Animals; Ascorbic Acid; Cysteine; Enzyme Activation; Glutathione; Heme; Liver; Mercury; Rats; Tryptophan Oxygenase | 1971 |
Effect of structural perturbations on the ligand-binding properties of human methemoglobin A.
Topics: Bromides; Chemical Phenomena; Chemistry; Chromatography, Gel; Cyanates; Cysteine; Globins; Heme; Humans; Imidazoles; Iron; Macromolecular Substances; Mercuribenzoates; Methemoglobin; Protein Binding; Protein Conformation; Quaternary Ammonium Compounds; Sodium; Spectrophotometry; Sulfhydryl Compounds; Thiocyanates | 1971 |
Evidence for an atypical binding of haem in a protozoan cytochrome.
Topics: Amino Acid Sequence; Amino Acids; Binding Sites; Chromatography; Cysteine; Cytochromes; Eukaryota; Heme | 1971 |
Activating and inhibiting effects of some organic substances on luminol reaction.
Topics: Cysteine; Glucose; Glutathione; Heme; Luminescent Measurements; Nuclear Medicine; Pyridazines; Thiourea | 1971 |
Cytochrome C and porphyrin--peptides. I. Characterization of cytochrome C and status of studies on its chemical synthesis.
Topics: Amino Acids; Animals; Apoproteins; Cattle; Chemical Phenomena; Chemistry; Cysteine; Cytochromes; Heart; Heme; Horses; Hydrolysis; Iron; Peptides; Phenylalanine; Porphyrins | 1971 |
The horseradish peroxidase-catalyzed oxidation of iodide. Outline of the mechanism.
Topics: Chemical Phenomena; Chemistry; Cysteine; Heme; Hydrogen Peroxide; Imidazoles; Iodides; Iron; Kinetics; Peroxidases; Plants; Spectrophotometry; Sulfites | 1970 |
Purification and characterization of cytochrome 553 from the chrysophycean alga Monochrysis lutheri.
Topics: Amino Acids; Arginine; Autoanalysis; Chemical Precipitation; Chromatography, Gel; Chromatography, Ion Exchange; Cysteine; Cytochromes; Dialysis; Electron Transport; Electrophoresis, Disc; Eukaryota; Freeze Drying; Heme; Histidine; Iron; Isoelectric Focusing; Methionine; Methods; Molecular Weight; Oxidation-Reduction; Photosynthesis; Proline; Quaternary Ammonium Compounds; Spectrophotometry; Sulfates; Tryptophan; Ultracentrifugation; Ultraviolet Rays | 1971 |
-aminolevulinic acid dehydratase of Spirillum itersonii and the regulation of tetrapyrrole synthesis.
Topics: Acyltransferases; Amino Acids; Calcium; Calcium Phosphates; Chemical Precipitation; Chromatography, Gel; Cysteine; Cytochromes; Enzyme Activation; Gels; Glutathione; Heme; Hydro-Lyases; Hydrogen-Ion Concentration; Iron; Kinetics; Levulinic Acids; Magnesium; Manganese; Mercaptoethanol; Nitrates; Porphyrins; Potassium; Pyrroles; Quaternary Ammonium Compounds; Spirillum; Succinates; Sulfates; Sulfhydryl Reagents; Tetroses; Zinc | 1971 |
[Allosteric regulation of erythrocyte delta-aminolevulinic dhydratase activity].
Topics: Cysteine; Erythrocytes; Heme; Humans; Hydro-Lyases | 1968 |
Effect of lipid on protoheme ferro-lyase.
Topics: Acetone; Animals; Bile Acids and Salts; Chickens; Chromatography, Thin Layer; Cysteine; Detergents; Egg Yolk; Erythrocytes; Female; Heme; Hydrogen-Ion Concentration; Iron Isotopes; Lipids; Lyases; Lysophosphatidylcholines; Mercaptoethanol; Palmitic Acids; Phosphatidylcholines; Phosphatidylethanolamines; Phospholipases; Phospholipids; Potassium Chloride; Stimulation, Chemical; Triglycerides; Vibration | 1969 |
Semi-synthetic analogs of cytochrome c. Substitutions for methionine at position 80.
Topics: Cyanogen Bromide; Cysteine; Cytochrome c Group; Ethionine; Heme; Methionine; Oxidoreductases; Structure-Activity Relationship; Succinates | 1980 |
Heme binding and substrate-protected cysteine residues in P-450cam.
Topics: Binding Sites; Cysteine; Cytochrome P-450 Enzyme System; Heme; Kinetics; Pseudomonas; Structure-Activity Relationship | 1983 |
Effect of histidine, cysteine, glutathione or beef on iron absorption in humans.
Topics: Absorption; Animals; Cattle; Cysteine; Dose-Response Relationship, Drug; Fabaceae; Female; Glutathione; Heme; Hemoglobins; Histidine; Humans; Iron; Male; Meat; Plants, Medicinal; Zea mays | 1984 |
Potent heme-degrading action of antimony and antimony-containing parasiticidal agents.
Topics: 5-Aminolevulinate Synthetase; Animals; Anti-Infective Agents; Antimony; Cobalt; Cysteine; Deferoxamine; Dose-Response Relationship, Drug; Heme; Heme Oxygenase (Decyclizing); Kidney; Liver; Male; Rats; Time Factors; Zinc | 1981 |
Heme and cysteine microenvironments of tuna apomyoglobin. Evidence of two independent unfolding regions.
Topics: Animals; Apoproteins; Cysteine; Guanidines; Heme; Hemin; Hydrogen-Ion Concentration; Myoglobin; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Tuna | 1982 |
Endogenous cysteine ligation in ferric and ferrous cytochrome P-450. Direct evidence from x-ray absorption spectroscopy.
Topics: Cysteine; Cytochrome P-450 Enzyme System; Fourier Analysis; Heme; Iron; Oxidation-Reduction; Pseudomonas; Spectrometry, Fluorescence; Spectrophotometry | 1982 |
Occurrence of aromatic methyl migration (NIH-shift) during oxidation of p-methylanisole by hemin-thiolester complex as a cytochrome P-450 model.
Topics: Animals; Anisoles; Cysteine; Cytochrome P-450 Enzyme System; Heme; Hemin; Hydrogen-Ion Concentration; Hydroxylation; Kinetics; Microsomes, Liver; Mixed Function Oxygenases; Models, Biological; Oxidation-Reduction; Rabbits; Thioglycolates | 1982 |
Ligand-dependent heme-protein interactions in human hemoglobin studied by Fourier transform infrared spectroscopy. Effects of quaternary structure on alpha chain tertiary structure measured at the alpha-104(G11) cysteine-SH.
Topics: Azides; Carbon Monoxide; Cyanides; Cysteine; Fourier Analysis; Heme; Hemoglobins; Humans; Ligands; Macromolecular Substances; Nitric Oxide; Oxyhemoglobins; Protein Binding; Protein Conformation; Spectrophotometry, Infrared | 1980 |
The structure of human carbonmonoxy haemoglobin at 2.7 A resolution.
Topics: Carboxyhemoglobin; Cysteine; Heme; Hemoglobins; Humans; Methemoglobin; Models, Molecular; Protein Conformation; X-Ray Diffraction | 1980 |
Increase in the susceptibility of hemoglobin to trypsin on treatment with glutathione or cysteine.
Topics: Binding Sites; Cysteine; Cystine; Globins; Glutathione; Heme; Hemoglobin A; Humans; Kinetics; Oxidation-Reduction; Protein Binding; Protein Conformation; Trypsin | 1980 |
Maturation of pre-apocytochrome f in vivo. A site-directed mutagenesis study in Chlamydomonas reinhardtii.
Topics: Amino Acid Sequence; Animals; Base Sequence; Chlamydomonas reinhardtii; Chloroplasts; Cysteine; Cytochromes; Cytochromes f; Genes, Plant; Heme; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Plasmids; Point Mutation; Protein Precursors; Recombinant Proteins | 1995 |
Cysteine 184 of endothelial nitric oxide synthase is involved in heme coordination and catalytic activity.
Topics: Amino Acid Oxidoreductases; Amino Acid Sequence; Base Sequence; Cysteine; Endothelium, Vascular; Heme; Humans; Ligands; Molecular Sequence Data; Mutation; Nitric Oxide Synthase | 1994 |
Prokaryotic expression of the heme- and flavin-binding domains of rat neuronal nitric oxide synthase as distinct polypeptides: identification of the heme-binding proximal thiolate ligand as cysteine-415.
Topics: Amino Acid Oxidoreductases; Animals; Base Sequence; Cloning, Molecular; Cysteine; DNA Primers; Escherichia coli; Flavins; Heme; Hemeproteins; Histidine; Molecular Sequence Data; Mutagenesis, Site-Directed; Neurons; Nitric Oxide Synthase; Peptides; Rats | 1995 |
Trans effects on cysteine ligation in the proximal His93Cys variant of horse heart myoglobin.
Topics: Animals; Circular Dichroism; Cysteine; Cytochrome P-450 Enzyme System; Electrochemistry; Electron Spin Resonance Spectroscopy; Ferric Compounds; Heme; Histidine; Horses; Humans; Magnetic Resonance Spectroscopy; Magnetics; Myocardium; Myoglobin | 1995 |
Conversion of cytochrome b562 to c-type cytochromes.
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Chromatography, Ion Exchange; Cloning, Molecular; Computer Simulation; Cysteine; Cytochrome b Group; Cytochrome c Group; Escherichia coli; Escherichia coli Proteins; Gene Expression; Heme; Magnetic Resonance Spectroscopy; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Mutagenesis; Structure-Activity Relationship | 1995 |
X-ray absorption near edge studies of cytochrome P-450-CAM, chloroperoxidase, and myoglobin. Direct evidence for the electron releasing character of a cysteine thiolate proximal ligand.
Topics: Camphor 5-Monooxygenase; Chloride Peroxidase; Cysteine; Cytochrome P-450 Enzyme System; Ferric Compounds; Ferrous Compounds; Heme; Mixed Function Oxygenases; Myoglobin; Oxidation-Reduction; Pseudomonas putida; Spectrum Analysis; X-Rays | 1995 |
The dimer-tetramer equilibrium of recombinant hemoglobins. Stabilization of the alpha 1 beta 2 interface by the mutation beta(Cys112-->Gly) at the alpha 1 beta 1 interface.
Topics: 2,3-Diphosphoglycerate; Amino Acid Sequence; Base Sequence; Binding Sites; Carboxyhemoglobin; Chromatography, Gel; Cysteine; Diphosphoglyceric Acids; Drug Stability; Globins; Glycine; Heme; Hemoglobin A; Humans; Macromolecular Substances; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Point Mutation; Protein Folding; Recombinant Proteins; Sequence Deletion; Valine | 1994 |
Identification of the site of ferrocyanide binding involved in the intramolecular electron transfer process to oxidized heme in Scapharca dimeric hemoglobin.
Topics: Animals; Binding Sites; Bivalvia; Chloromercuribenzoates; Chloromercurinitrophenols; Circular Dichroism; Cysteine; Electron Transport; Ferrocyanides; Heme; Hemoglobins; Macromolecular Substances; Oxidation-Reduction; p-Chloromercuribenzoic Acid; Phenylmercuric Acetate; Spectrophotometry | 1994 |
Reversal of copper(II)-induced methemoglobin formation by thiols.
Topics: Copper; Cysteine; Edetic Acid; Ferric Compounds; Ferrous Compounds; Glutathione; Heme; Methemoglobin; Oxidation-Reduction; Oxyhemoglobins; Sulfhydryl Compounds | 1993 |
Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase.
Topics: Benzene Derivatives; Binding Sites; Catalase; Chloride Peroxidase; Cysteine; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Heme; Histidine; Humans; Iron; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Myoglobin; Spectrophotometry; Spectrum Analysis, Raman; Tyrosine | 1993 |
Genetic structure and regulation of the cysG gene in Salmonella typhimurium.
Topics: Cysteine; DNA Transposable Elements; Genes, Bacterial; Genetic Complementation Test; Heme; Nitrite Reductases; Nitrites; Operon; Phenotype; Salmonella typhimurium; Transcription, Genetic | 1993 |
Heme active-site structural characterization of chloroperoxidase by resonance Raman spectroscopy.
Topics: Binding Sites; Chloride Peroxidase; Cysteine; Electrochemistry; Heme; Hydrogen-Ion Concentration; Peroxidase; Protein Conformation; Spectrum Analysis, Raman | 1993 |
Dynamics of protein relaxation in site-specific mutants of human myoglobin.
Topics: Alanine; Amino Acid Sequence; Cysteine; Heme; Humans; Kinetics; Mathematics; Mutagenesis, Site-Directed; Myoglobin; Protein Conformation; Recombinant Proteins; Spectrophotometry; Time Factors | 1993 |
[Newly discovered functions of hemoglobin].
Topics: Animals; Blood Pressure; Blood Vessels; Cysteine; Heme; Hemoglobins; Humans; In Vitro Techniques; Nitric Oxide; Rats | 1996 |
Preparation and reactions of myoglobin mutants bearing both proximal cysteine ligand and hydrophobic distal cavity: protein models for the active site of P-450.
Topics: Acetophenones; Aniline Compounds; Benzene Derivatives; Binding Sites; Cysteine; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Histidine; Humans; Kinetics; Magnetic Resonance Spectroscopy; Models, Chemical; Mutagenesis, Site-Directed; Myoglobin; Protein Conformation; Recombinant Proteins; Spectrophotometry, Ultraviolet; Sulfoxides | 1996 |
Evidence that the CysG protein catalyzes the first reaction specific to B12 synthesis in Salmonella typhimurium, insertion of cobalt.
Topics: Chromosome Mapping; Cobalt; Culture Media; Cysteine; Heme; Iron; Methionine; Methyltransferases; Mutagenesis; Operon; Oxidation-Reduction; Phenotype; Point Mutation; Salmonella typhimurium; Sulfites; Vitamin B 12 | 1996 |
Thiols and neuronal nitric oxide synthase: complex formation, competitive inhibition, and enzyme stabilization.
Topics: Animals; Arginine; Biopterins; Calmodulin; Cysteine; Dithiothreitol; Enzyme Inhibitors; Enzyme Stability; Flavin-Adenine Dinucleotide; Heme; Mercaptoethanol; NADP; Neurons; Nitric Oxide Synthase; Protein Binding; Rats; Spectrometry, Fluorescence; Spectrophotometry; Sulfhydryl Compounds; Temperature | 1997 |
The effect of L-cysteine and N-acetylcysteine on porphyrin/heme biosynthetic pathway in cells treated with 5-aminolevulinic acid and exposed to radiation.
Topics: Acetylcysteine; Aminolevulinic Acid; Cells, Cultured; Cysteine; Endothelium, Vascular; Ferrochelatase; Heme; Humans; Porphyrins; Ultraviolet Rays | 1996 |
A role for Salmonella typhimurium cbiK in cobalamin (vitamin B12) and siroheme biosynthesis.
Topics: Cobalt; Corrinoids; Cysteine; Escherichia coli; Gene Deletion; Genes, Bacterial; Genetic Complementation Test; Heme; Methyltransferases; Mutagenesis, Site-Directed; Porphyrins; Salmonella typhimurium; Species Specificity; Spectrophotometry, Ultraviolet; Vitamin B 12 | 1997 |
Cysteine-200 of human inducible nitric oxide synthase is essential for dimerization of haem domains and for binding of haem, nitroarginine and tetrahydrobiopterin.
Topics: Animals; Antioxidants; Binding Sites; Biopterins; Cysteine; Dimerization; DNA; Enzyme Induction; Heme; Humans; Nitric Oxide Synthase; Nitroarginine; Protein Conformation; Recombinant Fusion Proteins; Xenopus | 1997 |
A 4-term energy level scheme for the high-spin ferrous hemoproteins: evidence for the 5E eta, and 5B2 terms as the ground multiplets in hemoproteins with a histidine and a cysteine protein-derived heme ligand, respectively.
Topics: Animals; Chloride Peroxidase; Circular Dichroism; Computer Simulation; Cysteine; Cytochrome P-450 Enzyme System; Heme; Histidine; Horseradish Peroxidase; Imidazoles; In Vitro Techniques; Magnetic Resonance Spectroscopy; Models, Chemical; Myoglobin; Spectroscopy, Mossbauer; Temperature; Thermodynamics | 1997 |
1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate beta proton.
Topics: Binding Sites; Camphor 5-Monooxygenase; Carbon Monoxide; Cysteine; Heme; Hydrogen; Iron; Magnetic Resonance Spectroscopy; Magnetics; Models, Molecular; Oxidation-Reduction; Protein Conformation; Recombinant Proteins; Substrate Specificity | 1997 |
NO synthase isozymes have distinct substrate binding sites.
Topics: Animals; Arginine; Binding Sites; Brain; Carbon Monoxide; Cattle; Cysteine; Endothelium, Vascular; Heme; Isoenzymes; Mice; Nitric Oxide Synthase; Protein Conformation; Rats; Spectrum Analysis, Raman | 1997 |
Involvement of products of the nrfEFG genes in the covalent attachment of haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli.
Topics: Anaerobiosis; Chromatography, High Pressure Liquid; Cysteine; Cytochrome c Group; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Gene Deletion; Genes, Bacterial; Heme; Lysine; Mass Spectrometry; Mutagenesis, Site-Directed; Mutation; Nitrite Reductases; Operon; Oxidation-Reduction; Plasmids | 1998 |
Superoxide produced in the heme pocket of the beta-chain of hemoglobin reacts with the beta-93 cysteine to produce a thiyl radical.
Topics: Cysteine; Electron Spin Resonance Spectroscopy; Ethylmaleimide; Free Radicals; Heme; Hemoglobins; Humans; Kinetics; Macromolecular Substances; Models, Chemical; Peroxides; Spectrometry, Fluorescence; Sulfhydryl Compounds; Superoxides | 1998 |
Nitrosative stress: metabolic pathway involving the flavohemoglobin.
Topics: Biological Evolution; Cysteine; Diethylamines; Enzyme Inhibitors; Escherichia coli; Heme; Hemeproteins; Kinetics; Nitric Oxide; Nitrogen Oxides; Nitroso Compounds; S-Nitrosothiols; Signal Transduction; Spectrophotometry; Tryptophan Oxygenase | 1998 |
Crystal structure of the S-nitroso form of liganded human hemoglobin.
Topics: Carboxyhemoglobin; Computer Simulation; Crystallization; Crystallography, X-Ray; Cysteine; Heme; Hemoglobins; Humans; Ligands; Models, Molecular; Nitric Oxide; Nitroso Compounds; Protein Structure, Tertiary; S-Nitrosothiols; Stereoisomerism | 1998 |
The C331A mutant of neuronal nitric-oxide synthase is defective in arginine binding.
Topics: Animals; Arginine; Biopterins; Calmodulin; Carbon Monoxide; Catalytic Domain; Conserved Sequence; Cysteine; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Mutation; NADP; Neurons; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Rats; Recombinant Proteins; Spectrophotometry; Structure-Activity Relationship | 1998 |
Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center.
Topics: Amino Acid Sequence; Animals; Binding Sites; Biopterins; Catalysis; Cations; Cattle; Crystallization; Crystallography, X-Ray; Cysteine; Dimerization; Heme; Hydrogen Bonding; Models, Molecular; Molecular Mimicry; Nitric Oxide Synthase; Nitric Oxide Synthase Type III; Protein Structure, Secondary; Pterins; Sequence Alignment; Zinc | 1998 |
Effects of nitric oxide on the eosinophil survival in vitro. A role for nitrosyl-heme.
Topics: Apoptosis; Cell Survival; Cysteine; Cytokines; Eosinophils; Guanylate Cyclase; Heme; Hemin; Humans; Interleukin-5; Nitric Oxide; Nitric Oxide Donors; Nitroso Compounds; Penicillamine; S-Nitroso-N-Acetylpenicillamine; S-Nitrosothiols | 1999 |
Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxide.
Topics: Adult; Carbon Monoxide; Copper; Cysteine; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; Humans; Kinetics; Methemoglobin; Oxidation-Reduction | 1999 |
Identification of two important heme site residues (cysteine 75 and histidine 77) in CooA, the CO-sensing transcription factor of Rhodospirillum rubrum.
Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Carbon Monoxide; Cysteine; Escherichia coli; Ferric Compounds; Ferrous Compounds; Heme; Hemeproteins; Histidine; Ligands; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Rhodospirillum rubrum; Trans-Activators | 1999 |
Replacement of the proximal histidine iron ligand by a cysteine or tyrosine converts heme oxygenase to an oxidase.
Topics: Amino Acid Substitution; Catalysis; Cysteine; Electron Transport; Ferric Compounds; Ferrous Compounds; Heme; Heme Oxygenase (Decyclizing); Histidine; Humans; Iron; Ligands; Mutagenesis; Oxidation-Reduction; Oxidoreductases; Peroxides; Spectrum Analysis, Raman; Tyrosine | 1999 |
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 |
Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli.
Topics: Amino Acid Sequence; Amino Acid Substitution; Base Sequence; Catalase; Crystallography, X-Ray; Cysteine; Escherichia coli; Genetic Variation; Glutamic Acid; Heme; Histidine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Conformation; Recombinant Proteins; Restriction Mapping | 1999 |
Ascaris haemoglobin is a nitric oxide-activated 'deoxygenase'.
Topics: Anaerobiosis; Animals; Ascaris lumbricoides; Cloning, Molecular; Cysteine; Enzyme Activation; Evolution, Molecular; Heme; Hemoglobins; Ligands; Mutagenesis; Nitric Oxide; Nitroso Compounds; Oxidoreductases; Oxygen; S-Nitrosothiols; Spectrum Analysis; Swine | 1999 |
Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue.
Topics: Amino Acid Substitution; Chloride Peroxidase; Cysteine; Epoxy Compounds; Escherichia coli; Genetic Vectors; Heme; Histidine; Mutagenesis, Site-Directed | 1999 |
Coupled oxidation of heme covalently attached to cytochrome b562 yields a novel biliprotein.
Topics: Arginine; Bacterial Proteins; Biliverdine; Cloning, Molecular; Cysteine; Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrolysis; Methionine; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Pyrroles; Tetrapyrroles | 1999 |
Structural consequences of b- to c-type heme conversion in oxidized Escherichia coli cytochrome b562.
Topics: Amino Acid Sequence; Arginine; Cysteine; Cytochrome b Group; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Enzyme Stability; Escherichia coli; Escherichia coli Proteins; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Structure, Secondary; Solutions | 2000 |
Uphill electron transfer in the tetraheme cytochrome subunit of the Rhodopseudomonas viridis photosynthetic reaction center: evidence from site-directed mutagenesis.
Topics: Amino Acid Substitution; Cysteine; Cytochrome c Group; Electron Transport; Heme; Kinetics; Lysine; Mutagenesis, Site-Directed; Oxidation-Reduction; Photosynthetic Reaction Center Complex Proteins; Plasmids; Rhodopseudomonas; Spectrophotometry | 2000 |
Loss of either of the two heme-binding cysteines from a class I c-type cytochrome has a surprisingly small effect on physicochemical properties.
Topics: Amino Acid Sequence; Amino Acid Substitution; Bacteria, Aerobic; Base Sequence; Binding Sites; Cloning, Molecular; Cysteine; Cytochrome c Group; Escherichia coli; Guanidine; Heme; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Denaturation; Protein Folding; Recombinant Proteins; Templates, Genetic | 2000 |
Relative role of heme nitrosylation and beta-cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation.
Topics: Administration, Inhalation; Cysteine; Heme; Hemoglobins; Humans; Kinetics; Luminescent Measurements; Nitrates; Nitric Oxide; Nitrites; Nitroso Compounds; Ozone; Potassium Cyanide; Reproducibility of Results; Sensitivity and Specificity | 2000 |
Photoinduced intracomplex electron transfer between cytochrome c oxidase and TUPS-modified cytochrome c.
Topics: Animals; Azurin; Catalase; Cattle; Coloring Agents; Cysteine; Cytochrome c Group; Electron Transport Complex IV; Electrons; Glucose; Glucose Oxidase; Heme; Kinetics; Light; Myocardium; Pyrenes; Spectrophotometry; Time Factors | 2000 |
Nitric oxide-mediated heme oxidation and selective beta-globin nitrosation of hemoglobin from normal and sickle erythrocytes.
Topics: Anemia, Sickle Cell; Cysteine; Diethylamines; Erythrocytes; Globins; Heme; Hemoglobin A; Hemoglobin, Sickle; Humans; Kinetics; Mass Spectrometry; Methemoglobin; Nitric Oxide; Nitrogen Oxides; Nitroso Compounds; Oxidation-Reduction; Oxygen; S-Nitrosothiols; Spectrophotometry; Thermodynamics | 2000 |
Reconstitution of pterin-free inducible nitric-oxide synthase.
Topics: Animals; Apoenzymes; Biopterins; Cysteine; Glutathione; Heme; Holoenzymes; Mice; Molecular Structure; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Pterins; Spectrophotometry; Zinc | 2001 |
Roles of the axial push effect in cytochrome P450cam studied with the site-directed mutagenesis at the heme proximal site.
Topics: Binding Sites; Camphor; Camphor 5-Monooxygenase; Cysteine; Electrons; Escherichia coli; Ferricyanides; Ferrous Compounds; Heme; Hydroxylation; Magnetic Resonance Spectroscopy; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Oxygen; Plasmids; Protein Conformation; Protons; Spectrophotometry; Sulfur | 2000 |
How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms.
Topics: Bacterial Proteins; Binding Sites; Camphor; Camphor 5-Monooxygenase; Computer Simulation; Cysteine; Cytochrome P-450 Enzyme System; Ethers; Fatty Acids, Monounsaturated; Heme; Kinetics; Ligands; Mixed Function Oxygenases; Models, Molecular; Mutation; NADPH-Ferrihemoprotein Reductase; Protein Structure, Secondary; Pseudomonas putida; Static Electricity; Substrate Specificity | 2000 |
Changing the heme ligation in flavocytochrome b2: substitution of histidine-66 by cysteine.
Topics: Amino Acid Substitution; Circular Dichroism; Cysteine; Electron Spin Resonance Spectroscopy; Flavin Mononucleotide; Heme; Histidine; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Mutation; Oxidation-Reduction; Protein Binding; Saccharomyces cerevisiae; Spectrophotometry; Spectrum Analysis, Raman | 2000 |
Redox properties and coordination structure of the heme in the co-sensing transcriptional activator CooA.
Topics: Alanine; Bacterial Proteins; Cysteine; Electrochemistry; Escherichia coli Proteins; Fimbriae Proteins; Heme; Histidine; Iron; Ligands; Models, Chemical; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxygen; Spectrum Analysis, Raman; Transcriptional Activation | 2001 |
Resonance Raman characterization of the heme cofactor in cystathionine beta-synthase. Identification of the Fe-S(Cys) vibration in the six-coordinate low-spin heme.
Topics: Binding, Competitive; Carbon Monoxide; Cystathionine beta-Synthase; Cysteine; Ferric Compounds; Ferrous Compounds; Heme; Homocysteine; Humans; Iron-Sulfur Proteins; Ligands; Mercuric Chloride; Molybdenum; Oxidation-Reduction; Protein Binding; Pyridoxal Phosphate; Spectrum Analysis, Raman | 2001 |
NO-independent regulatory site on soluble guanylate cyclase.
Topics: Amino Acid Sequence; Animals; Antihypertensive Agents; Binding Sites; Blood Pressure; Cyclic N-Oxides; Cysteine; Disease Models, Animal; Enzyme Activation; Female; Guanylate Cyclase; Heme; Humans; Imidazoles; In Vitro Techniques; Indazoles; Molecular Sequence Data; Nitric Oxide; Photoaffinity Labels; Platelet Aggregation Inhibitors; Pyrazoles; Pyridines; Rats; Solubility | 2001 |
A proximal tryptophan in NO synthase controls activity by a novel mechanism.
Topics: Amino Acid Substitution; Cysteine; Heme; Hydrogen Bonding; Models, Molecular; Molecular Conformation; Mutagenesis, Site-Directed; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Protein Conformation; Recombinant Proteins; Spectrophotometry; Tryptophan | 2001 |
Solution structure of Methylophilus methylotrophus cytochrome c": insights into the structural basis of haem-ligand detachment.
Topics: Amino Acid Sequence; Binding Sites; Cysteine; Cytochrome c Group; Disulfides; Heme; Histidine; Ligands; Methylophilus methylotrophus; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation | 2001 |
Characterization of Rhodobacter sphaeroides cytochrome c(2) proteins with altered heme attachment sites.
Topics: Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cysteine; Cytochrome c Group; Cytochromes c2; Electron Transport; Escherichia coli; Heme; Ligands; Mutagenesis, Site-Directed; Photosynthesis; Protein Processing, Post-Translational; Protein Sorting Signals; Recombinant Proteins; Rhodobacter sphaeroides; Spectrophotometry | 2001 |
Regulation of the properties of the heme-NO complexes in nitric-oxide synthase by hydrogen bonding to the proximal cysteine.
Topics: Cysteine; Heme; Hydrogen Bonding; Models, Molecular; Mutation; Nitric Oxide; Nitric Oxide Synthase; Protein Conformation; Spectrum Analysis, Raman; Tryptophan | 2001 |
Heme oxygenase-2 interaction with metalloporphyrins: function of heme regulatory motifs.
Topics: Amino Acid Motifs; Amino Acid Substitution; Catalytic Domain; Circular Dichroism; Cysteine; Heme; Heme Oxygenase (Decyclizing); Humans; Hydrogen-Ion Concentration; Metalloporphyrins; Peptide Fragments; Proline; Protein Binding; Protoporphyrins; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfhydryl Reagents | 2001 |
The covalent structure of the small subunit from Pseudomonas putida amine dehydrogenase reveals the presence of three novel types of internal cross-linkages, all involving cysteine in a thioether bond.
Topics: Amino Acid Sequence; Amino Acids; Cloning, Molecular; Cross-Linking Reagents; Cysteine; Glutamic Acid; Heme; Indolequinones; Mass Spectrometry; Models, Chemical; Models, Genetic; Molecular Sequence Data; Open Reading Frames; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Peptides; Protein Binding; Protein Processing, Post-Translational; Pseudomonas putida; Quinones; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization; Sulfides; Tryptophan; X-Rays | 2001 |
Complex formation of cytochrome P450cam with Putidaredoxin. Evidence for protein-specific interactions involving the proximal thiolate ligand.
Topics: Animals; Binding Sites; Camphor 5-Monooxygenase; Cysteine; Electrons; Escherichia coli; Ferredoxins; Heme; Iron; Ligands; Liver; Organometallic Compounds; Protein Binding; Protein Conformation; Rats; Spectrum Analysis, Raman | 2002 |
Resonance Raman detection of the Fe-S bond in endothelial nitric oxide synthase.
Topics: Cell Line; Cysteine; Endothelium; Heme; Iron; Nitric Oxide Synthase; Nitric Oxide Synthase Type III; Spectrum Analysis, Raman; Sulfur | 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 |
Modification of heme c binding motifs in the small subunit (NrfH) of the Wolinella succinogenes cytochrome c nitrite reductase complex.
Topics: Amino Acid Motifs; Bacterial Proteins; Binding Sites; Culture Media; Cysteine; Cytochrome c Group; Cytochromes a1; Cytochromes c1; Heme; Mutagenesis, Site-Directed; Nitrate Reductases; Nitrites; Oxidation-Reduction; RNA-Binding Proteins; Serine; Transcription Factors; Wolinella | 2002 |
Responses of normal and sickle cell hemoglobin to S-nitroscysteine: implications for therapeutic applications of NO in treatment of sickle cell disease.
Topics: Anemia, Sickle Cell; Animals; Chelating Agents; Cysteine; Dolphins; Heme; Hemoglobin, Sickle; Hemoglobins; Humans; Nitric Oxide; Oxidation-Reduction; Oxygen; Protein Binding; S-Nitrosothiols; Spectrometry, Mass, Electrospray Ionization; Vasodilator Agents | 2002 |
The interplay between heme iron and protein sulfhydryls in the reaction of dimeric Scapharca inaequivalvis hemoglobin with nitric oxide.
Topics: Animals; Bivalvia; Cysteine; Ferric Compounds; Ferrous Compounds; Heme; Hemoglobins; Humans; Kinetics; Ligands; Nitric Oxide; Nitrosation; Protein Binding; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Sulfhydryl Compounds | 2002 |
Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme.
Topics: Amino Acid Motifs; Binding Sites; Catalysis; Catalytic Domain; Crystallization; Crystallography, X-Ray; Cystathionine beta-Synthase; Cysteine; Heme; Humans; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Pyridoxal Phosphate; Sequence Deletion | 2002 |
Ligand binding properties and structural studies of recombinant and chemically modified hemoglobins altered at beta 93 cysteine.
Topics: 2,3-Diphosphoglycerate; Allosteric Regulation; Amino Acid Substitution; Cysteine; Globins; Heme; Hemoglobin A; Hemoglobins; Histidine; Humans; Ligands; Methemoglobin; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Oxygen; Phytic Acid; Protein Subunits; Recombinant Proteins; Structure-Activity Relationship; Thermodynamics | 2002 |
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 |
Spectroscopic characterization of five- and six-coordinate ferrous-NO heme complexes. Evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide synthase.
Topics: Circular Dichroism; Cysteine; Electron Spin Resonance Spectroscopy; Ferric Compounds; Ferrous Compounds; Heme; Humans; Iron-Sulfur Proteins; Ligands; Mutagenesis, Site-Directed; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Phenylalanine; Protein Structure, Tertiary; Solvents; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine | 2003 |
Antioxidant protein 2 prevents methemoglobin formation in erythrocyte hemolysates.
Topics: Animals; Blotting, Western; Cysteine; Endothelium, Vascular; Erythrocytes; Heme; Hemoglobins; Methemoglobin; Peroxidases; Peroxiredoxin VI; Peroxiredoxins; Protein Binding; Protein Biosynthesis; Proteins; Swine | 2003 |
Stereoselective in vitro formation of c-type cytochrome variants from Hydrogenobacter thermophilus containing only a single thioether bond.
Topics: Bacteria, Aerobic; Cysteine; Cytochrome c Group; Heme; Hydrogen Bonding; Molecular Conformation; Protein Binding; Protein Conformation | 2003 |
A constitutively activated mutant of human soluble guanylyl cyclase (sGC): implication for the mechanism of sGC activation.
Topics: Animals; Cell Line; Cysteine; Detergents; Dithiothreitol; DNA, Complementary; Dose-Response Relationship, Drug; Enzyme Activation; Genetic Vectors; Guanylate Cyclase; Heme; Hemin; Humans; Insecta; Iron; Ligands; Models, Chemical; Mutation; Nitric Oxide; Protein Binding; Protein Conformation; Receptors, Cytoplasmic and Nuclear; Soluble Guanylyl Cyclase; Spectrophotometry; Transfection; Tumor Cells, Cultured | 2003 |
Chemical and kinetic reaction mechanisms of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.
Topics: Amines; Crystallography, X-Ray; Cysteine; Heme; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Phenethylamines; Stereoisomerism; Time Factors | 2003 |
PEPTIDES AND OTHER NITROGEN SOURCES FOR GROWTH OF BACTEROIDES RUMINICOLA.
Topics: Amino Acids; Ammonia; Ascorbic Acid; Bacteroides; Caseins; Cysteine; Heme; Metabolism; Methionine; Minerals; Nitrogen; Peptides; Pharmacology; Prevotella ruminicola; Proteins; Research; Vitamins | 1964 |
FORMATION OF HEME IN EMBRYONIC AVIAN TISSUE.
Topics: Chick Embryo; Cysteine; Dialysis; Heme; Iron; Iron Isotopes; Levulinic Acids; Ligases; Metabolism; Porphyrins; Renal Dialysis; Research | 1964 |
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 |
Let's Sco1, Oxidase! Let's Sco!
Topics: Adenosine Triphosphate; Amino Acid Motifs; Bacillus subtilis; Bacterial Proteins; Binding Sites; Cell Membrane; Copper; Cysteine; Electron Transport Complex IV; Heme; Intracellular Membranes; Ligands; Mitochondria; Molecular Chaperones; Mutation; Oxidation-Reduction; Protein Binding; Protein Structure, Tertiary | 2003 |
Crystallographic analysis of the interaction of nitric oxide with quaternary-T human hemoglobin.
Topics: Anaerobiosis; Crystallization; Crystallography, X-Ray; Cysteine; Heme; Hemoglobins; Histidine; Humans; Iron; Ligands; Nitric Oxide; Protein Conformation; Protein Structure, Quaternary; Protein Structure, Tertiary; Protein Subunits; Sulfhydryl Compounds | 2004 |
Protein radical formation during lactoperoxidase-mediated oxidation of the suicide substrate glutathione: immunochemical detection of a lactoperoxidase radical-derived 5,5-dimethyl-1-pyrroline N-oxide nitrone adduct.
Topics: Amino Acids; Ascorbic Acid; Azides; Blotting, Western; Catalase; Cyclic N-Oxides; Cysteine; Dose-Response Relationship, Drug; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Free Radicals; Glutathione; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Immunochemistry; Iodides; Lactoperoxidase; Models, Chemical; Nitrites; Nitrogen Oxides; Oxygen; Oxygen Consumption; Phenol; Spin Labels; Thiocyanates; Time Factors; Tyrosine | 2004 |
NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.
Topics: Alanine; Amino Acid Sequence; Bacteria, Aerobic; Cysteine; Cytochrome c Group; Heme; Hydrogen; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Molecular Sequence Data; Mutagenesis; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Protons; Temperature | 2004 |
The distinct heme coordination environments and heme-binding stabilities of His39Ser and His39Cys mutants of cytochrome b5.
Topics: Animals; Cattle; Cysteine; Cytochromes b5; Electrophoresis, Polyacrylamide Gel; Heme; Histidine; Mass Spectrometry; Mutation; Protein Denaturation; Serine; Temperature | 2003 |
Coupling of the heme and an internal disulfide bond in human neuroglobin.
Topics: Cysteine; Disulfides; Globins; Heme; Humans; Mass Spectrometry; Nerve Tissue Proteins; Neuroglobin; Oxygen | 2004 |
Biochemical and spectroscopic characterization of the covalent binding of heme to cytochrome b6.
Topics: Amino Acid Sequence; Animals; Binding Sites; Chlamydomonas reinhardtii; Conserved Sequence; Cysteine; Cytochromes b6; Dimerization; Electrophoresis, Polyacrylamide Gel; Endopeptidases; Heme; Hydrolysis; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Peroxidase; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrum Analysis, Raman; Valine | 2004 |
Structural and functional characterization of the unusual triheme cytochrome bound to the reaction center of Rhodovulum sulfidophilum.
Topics: Amino Acid Motifs; Binding Sites; Cell Division; Cysteine; Cytochromes; Electron Spin Resonance Spectroscopy; Heme; Ligands; Models, Biological; Models, Genetic; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Plasmids; Protein Binding; Rhodovulum; Spectrophotometry; Structure-Activity Relationship | 2004 |
Refolding processes of cytochrome P450cam from ferric and ferrous acid forms to the native conformation. Formations of folding intermediates with non-native heme coordination state.
Topics: Camphor 5-Monooxygenase; Circular Dichroism; Cysteine; Escherichia coli; Heme; Hydrogen-Ion Concentration; Iron; Kinetics; Ligands; Protein Conformation; Protein Folding; Spectrometry, Fluorescence; Spectrophotometry; Spectrum Analysis, Raman; Temperature; Thermodynamics; Ultraviolet Rays | 2004 |
An electrostatically driven conformational transition is involved in the mechanisms of substrate binding and cooperativity in cytochrome P450eryF.
Topics: Allosteric Site; Amino Acid Substitution; Bacterial Proteins; Binding Sites; Cysteine; Cytochrome P-450 Enzyme System; Fluorescence Resonance Energy Transfer; Glutamic Acid; Heme; Mixed Function Oxygenases; Osmolar Concentration; Protein Conformation; Protein Structure, Secondary; Pyrenes; Static Electricity | 2004 |
L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: the structural changes trigger electron transfer to oxy-P450cam from electron donors.
Topics: Ascorbic Acid; Bacterial Proteins; Camphor; Camphor 5-Monooxygenase; Chromatography; Crystallography, X-Ray; Cysteine; Dose-Response Relationship, Drug; Electron Transport; Electrons; Escherichia coli; Ferredoxins; Heme; Hydroxylation; Kinetics; Magnetic Resonance Spectroscopy; Models, Chemical; Models, Molecular; Mutation; Oxygen; Protein Binding; Protons; Signal Transduction; Temperature; Time Factors | 2004 |
Nitric oxide-induced modification of protein thiolate clusters as determined by spectral fluorescence resonance energy transfer in live endothelial cells.
Topics: Animals; Cells, Cultured; Cyclic GMP; Cysteine; Dithiothreitol; Endothelium, Vascular; Enzyme Activation; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Free Radicals; Genes, Reporter; Green Fluorescent Proteins; Guanylate Cyclase; Heme; Microscopy, Fluorescence; Nitric Oxide; Nitroso Compounds; Peptides; Protein Conformation; Proteins; Receptors, Cytoplasmic and Nuclear; Recombinant Fusion Proteins; Sheep; Signal Transduction; Soluble Guanylyl Cyclase; Spectrometry, Fluorescence; Sulfhydryl Compounds | 2004 |
Cytochrome c550 in the cyanobacterium Thermosynechococcus elongatus: study of redox mutants.
Topics: Calcium; Chlorine; Cloning, Molecular; Cyanobacteria; Cysteine; Cytochrome c Group; DNA; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hot Temperature; Ligands; Methionine; Models, Genetic; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Oxygen; Plasmids; Point Mutation; Polymerase Chain Reaction; Synechocystis; Temperature; Thylakoids; Time Factors | 2004 |
Endoproteolytic cleavage of human thyroperoxidase: role of the propeptide in the protein folding process.
Topics: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Arginine; Autoantigens; Biotinylation; Brefeldin A; CHO Cells; Cricetinae; Cysteine; Cytoplasm; DNA, Complementary; Electrophoresis, Polyacrylamide Gel; Endoplasmic Reticulum; Furin; Gene Deletion; Glycosylation; Heme; Humans; Immunoprecipitation; Iodide Peroxidase; Iron-Binding Proteins; Lysine; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; Models, Genetic; Molecular Chaperones; Molecular Sequence Data; Monensin; Mutagenesis; Mutagenesis, Site-Directed; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; Peptides; Protein Folding; Protein Processing, Post-Translational; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Thyroid Gland; Time Factors; Transfection | 2005 |
Abolition of oxygenase function, retention of NADPH oxidase activity, and emergence of peroxidase activity upon replacement of the axial cysteine-436 ligand by histidine in cytochrome P450 2B4.
Topics: Amino Acid Substitution; Aryl Hydrocarbon Hydroxylases; Base Sequence; Catalytic Domain; Chromatography, High Pressure Liquid; Cysteine; Cytochrome P450 Family 2; DNA, Complementary; Escherichia coli; Heme; Histidine; Hydrogen Peroxide; In Vitro Techniques; Ligands; Molecular Weight; Mutagenesis, Site-Directed; Recombinant Proteins; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry | 2005 |
Cytochrome bd oxidase, oxidative stress, and dioxygen tolerance of the strictly anaerobic bacterium Moorella thermoacetica.
Topics: Amino Acid Sequence; Bacteria, Anaerobic; Cell Membrane; Cysteine; Cysteine Synthase; Cytochromes; Electron Transport Chain Complex Proteins; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Heme; Molecular Sequence Data; Operon; Oxidative Stress; Oxidoreductases; Oxygen | 2005 |
S-Nitrosation and regulation of inducible nitric oxide synthase.
Topics: Animals; Avidin; Biotinylation; Cell Line; Chromogenic Compounds; Cysteine; Enzyme Activation; Heme; Horseradish Peroxidase; Isoenzymes; Macrophages; Mice; Mutagenesis, Site-Directed; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Nitrosation; Protein Binding; Quaternary Ammonium Compounds; Recombinant Proteins; Resorcinols; S-Nitrosothiols; Sensitivity and Specificity; Zinc | 2005 |
CO-dependent activity-controlling mechanism of heme-containing CO-sensor protein, neuronal PAS domain protein 2.
Topics: Amino Acid Sequence; Animals; Basic Helix-Loop-Helix Transcription Factors; Carbon Monoxide; Cysteine; Cytochrome c Group; Dimerization; DNA; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Iron; Ligands; Liver; Mice; Mice, Inbred C57BL; Models, Chemical; Molecular Sequence Data; Mutation; Nerve Tissue Proteins; Neurons; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protons; Sequence Homology, Amino Acid; Signal Transduction; Spectrum Analysis, Raman; Time Factors; Transcription Factors | 2005 |
Effects of nitroglycerin/L-cysteine on soluble guanylate cyclase: evidence for an activation/inactivation equilibrium controlled by nitric oxide binding and haem oxidation.
Topics: Animals; Cattle; Cysteine; Enzyme Activation; Guanylate Cyclase; Heme; Hydrazines; Light; Lung; Nitric Oxide; Nitrogen Oxides; Nitroglycerin; Oxidation-Reduction; Protein Binding; Receptors, Cytoplasmic and Nuclear; Soluble Guanylyl Cyclase | 2005 |
Structure and redox properties of the haem centre in the C357M mutant of cytochrome P450cam.
Topics: Amino Acid Sequence; Camphor 5-Monooxygenase; Circular Dichroism; Cysteine; Heme; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Structure-Activity Relationship | 2005 |
Iron absorption from concentrated hemoglobin hydrolysate by rat.
Topics: Animals; Cysteine; Diffusion Chambers, Culture; Female; Heme; Hemoglobins; Hydrolysis; Intestinal Absorption; Iron; Rats; Rats, Sprague-Dawley; Solubility | 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 |
Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2.
Topics: Amino Acid Motifs; Cell Line, Tumor; Cysteine; Heme; Histidine; Humans; Iron; Iron Regulatory Protein 2; Ubiquitin | 2005 |
Heme reduction by intramolecular electron transfer in cysteine mutant myoglobin under carbon monoxide atmosphere.
Topics: Animals; Carbon Monoxide; Cysteine; Dimerization; Disulfides; Electron Transport; Heme; Metmyoglobin; Mutagenesis, Site-Directed; Myoglobin; Oxidation-Reduction; Spectrophotometry, Ultraviolet; Static Electricity; Whales | 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 |
Lack of allosterically controlled intramolecular transfer of nitric oxide from the heme to cysteine in the beta subunit of hemoglobin.
Topics: Adult; Allosteric Regulation; Biological Transport; Cysteine; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Humans; Kinetics; Nitric Oxide; Oxyhemoglobins; Protein Subunits | 2006 |
Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex--a membrane-bound redox complex involved in the sulfate respiratory pathway.
Topics: Bacterial Proteins; Catalysis; Cysteine; Cytochrome c Group; Desulfovibrio desulfuricans; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Genomics; Heme; Histidine; Iron-Sulfur Proteins; Membranes; Methionine; Oxidation-Reduction; Respiratory System; Spectrophotometry, Ultraviolet; Sulfates | 2006 |
Three-dimensional model of the human aromatase enzyme and density functional parameterization of the iron-containing protoporphyrin IX for a molecular dynamics study of heme-cysteinato cytochromes.
Topics: Animals; Aromatase; Calorimetry; Cysteine; Cytochrome P-450 Enzyme System; Cytochromes; Heme; Humans; Iron; Mammals; Models, Molecular; Protein Structure, Secondary; Protoporphyrins | 2006 |
Regulation of the monomer-dimer equilibrium in inducible nitric-oxide synthase by nitric oxide.
Topics: Amino Acid Motifs; Animals; Arginine; Biopterins; Chelating Agents; Chromatography; Cysteine; Dimerization; Disulfides; Escherichia coli; Heme; Iron; Mass Spectrometry; Mice; Models, Chemical; Models, Molecular; Molecular Conformation; Nitric Oxide; Nitric Oxide Synthase Type II; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Spectrophotometry; Spectrum Analysis, Raman; Structure-Activity Relationship; Sulfhydryl Compounds; Time Factors; Urea; Zinc | 2006 |
Linker chains of the gigantic hemoglobin of the earthworm Lumbricus terrestris: primary structures of linkers L2, L3, and L4 and analysis of the connectivity of the disulfide bonds in linker L1.
Topics: Amino Acid Sequence; Animals; Aspartic Acid; Base Sequence; Binding Sites; Calcium; Chromatography, High Pressure Liquid; Cysteine; Disulfides; Dithiothreitol; DNA, Complementary; Glutamic Acid; Heme; Hemoglobins; Histidine; Humans; Ligands; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Oligochaeta; Protein Binding; Protein Processing, Post-Translational; Protein Structure, Tertiary; Receptors, LDL; RNA, Messenger; Sequence Homology, Amino Acid; Sodium Dodecyl Sulfate; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Superoxide Dismutase | 2006 |
Mechanisms for vasoconstriction and decreased blood flow following intravenous administration of cell-free native hemoglobin solutions.
Topics: Alkylation; Animals; Aorta, Thoracic; Binding Sites; Blood Flow Velocity; Blood Substitutes; Cysteine; Heme; Hemoglobins; In Vitro Techniques; Injections, Intravenous; Male; Nitric Oxide; Oxygen; Rats; Rats, Sprague-Dawley; Sulfhydryl Compounds; Vasoconstriction | 2005 |
Crystal structure of oxidized cytochrome c(6A) from Arabidopsis thaliana.
Topics: Arabidopsis; Arabidopsis Proteins; Binding Sites; Crystallography, X-Ray; Cysteine; Cytochromes c6; Heme; Models, Molecular; Oxidation-Reduction; Protein Structure, Tertiary; Structural Homology, Protein | 2006 |
Measurement of nitric oxide levels in the red cell: validation of tri-iodide-based chemiluminescence with acid-sulfanilamide pretreatment.
Topics: Albumins; Cysteine; Glutathione; Heme; Hemoglobins; Humans; Iodides; Luminescence; Luminescent Measurements; Nitric Oxide; Spectrophotometry; Sulfanilamide; Sulfanilamides | 2006 |
Roles of the heme and heme ligands in the activation of CooA, the CO-sensing transcriptional activator.
Topics: Amino Acid Sequence; Bacterial Proteins; Cysteine; Heme; Hemeproteins; Histidine; Ligands; Trans-Activators | 2006 |
Drosophila nuclear receptor E75 is a thiolate hemoprotein.
Topics: Alanine; Amino Acid Sequence; Animals; Cysteine; DNA-Binding Proteins; Drosophila melanogaster; Drosophila Proteins; Electron Spin Resonance Spectroscopy; Gene Expression; Heme; Hemeproteins; Histidine; Humans; Ligands; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Tertiary; Receptors, Cytoplasmic and Nuclear; Sequence Alignment; Solubility; Spectrophotometry, Ultraviolet; Sulfur; Transcription Factors | 2006 |
Heme-heme interactions in the cytochrome b6f complex: EPR spectroscopy and correlation with structure.
Topics: Cysteine; Cytochrome b6f Complex; Electron Spin Resonance Spectroscopy; Heme; Histidine; Molecular Structure | 2006 |
A functional model for the cysteinate-ligated non-heme iron enzyme superoxide reductase (SOR).
Topics: Catalysis; Cysteine; Heme; Models, Molecular; Oxidoreductases; Spectrum Analysis, Raman | 2006 |
The cytochrome P450 gene family CYP157 does not contain EXXR in the K-helix reducing the absolute conserved P450 residues to a single cysteine.
Topics: Amino Acid Motifs; Bacterial Proteins; Cysteine; Cytochrome P-450 Enzyme System; Heme; Models, Molecular; Mutagenesis, Site-Directed; Protein Structure, Quaternary; Spectrophotometry, Ultraviolet; Streptomyces coelicolor | 2006 |
Structural basis of peroxide-mediated changes in human hemoglobin: a novel oxidative pathway.
Topics: Blood Substitutes; Cysteine; Heme; Hemoglobin A; Hemolysis; Humans; Hydrogen Peroxide; Methionine; Models, Molecular; Oxidation-Reduction; Protein Structure, Tertiary | 2007 |
A mass spectrometric investigation of native and oxidatively inactivated chloroperoxidase.
Topics: Chloride Peroxidase; Cysteine; Cystine; Enzymes, Immobilized; Heme; Hydrogen Peroxide; Indoles; Mass Spectrometry; Oxidants; Spectrometry, Mass, Electrospray Ionization; Stereoisomerism | 2007 |
Identification of Cys385 in the isolated kinase insertion domain of heme-regulated eIF2 alpha kinase (HRI) as the heme axial ligand by site-directed mutagenesis and spectral characterization.
Topics: Animals; Cysteine; eIF-2 Kinase; Electron Spin Resonance Spectroscopy; Gene Expression Regulation; Heme; Ligands; Mice; Mutagenesis, Insertional; Protein Binding; Protein Structure, Tertiary; Serine; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman | 2007 |
X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata.
Topics: Animals; Binding Sites; Crystallography, X-Ray; Cysteine; Escherichia coli; Heme; Hemoglobins; Hydrogen Bonding; Models, Chemical; Models, Molecular; Molecular Conformation; Peroxidases; Polychaeta; Protein Conformation; Recombinant Proteins; Serine | 2007 |
The N-end rule pathway is a sensor of heme.
Topics: 3T3 Cells; Amino Acid Sequence; Aminoacyltransferases; Animals; Arginine; Binding Sites; Catalysis; Cysteine; Heme; Hemin; Mice; Models, Biological; Molecular Sequence Data; Nitric Oxide; Oxygen; Peptides; Saccharomyces cerevisiae; Substrate Specificity; Transcription, Genetic | 2008 |
A cysteine residue near the propionate side chain of heme is the radical site in ascorbate peroxidase.
Topics: Ascorbate Peroxidases; Crystallography, X-Ray; Cysteine; Enzyme Activation; Heme; Hydrogen Peroxide; Isoenzymes; Models, Molecular; Molecular Structure; Nicotiana; Oxidation-Reduction; Peroxidases; Propionates; Protein Structure, Tertiary; Recombinant Proteins; Rhodophyta; Tandem Mass Spectrometry | 2008 |
ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis.
Topics: Adenosine Triphosphate; Catalysis; Chlorobium; Cysteine; Dithionite; Electrons; Escherichia coli; Heme; Kinetics; Leucine; Light; Lysine; Nitrogenase; Oxidoreductases; Protochlorophyllide | 2008 |
Heme-binding characteristics of the isolated PAS-A domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms.
Topics: Animals; Basic Helix-Loop-Helix Transcription Factors; Binding Sites; Brain; Cell Cycle Proteins; Circadian Rhythm; Cloning, Molecular; Cysteine; DNA Primers; Heme; Iron; Mercury; Mice; Nerve Tissue Proteins; Nuclear Proteins; Peptide Fragments; Period Circadian Proteins; Recombinant Proteins; Spectrum Analysis, Raman; Transcription Factors | 2008 |
Effects of amino acids on malarial heme crystallization.
Topics: Amino Acids; Chemical Phenomena; Chemistry, Physical; Crystallization; Cysteine; Heme; Hemeproteins; Hemin; Humans; Hydrogen-Ion Concentration; Kinetics; Malaria; Polysorbates; Solutions; Surface Tension; Surface-Active Agents | 2008 |
The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration.
Topics: Carrier Proteins; Catalytic Domain; Cell Membrane; Crystallography, X-Ray; Cysteine; Desulfovibrio vulgaris; Heme; Iron-Sulfur Proteins; Models, Molecular; Molecular Conformation; Oxidoreductases Acting on Sulfur Group Donors; Protein Binding; Protein Structure, Tertiary; Sulfates; Sulfites; Sulfur | 2008 |
Compound I in heme thiolate enzymes: a comparative QM/MM study.
Topics: Amino Acid Sequence; Amino Acid Substitution; Cysteine; Cytochrome P-450 Enzyme System; Glutamine; Heme; Hydrogen Bonding; Kinetics; Models, Molecular; Potassium; Protein Conformation; Quantum Theory; Spectroscopy, Mossbauer | 2008 |
Replacement of the axial histidine heme ligand with cysteine in nitrophorin 1: spectroscopic and crystallographic characterization.
Topics: Circular Dichroism; Crystallography, X-Ray; Cysteine; Heme; Hemeproteins; Histidine; Ligands; Models, Molecular; Mutation; Protein Conformation; Protein Engineering; Salivary Proteins and Peptides; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman | 2009 |
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 |
Why do cysteine dioxygenase enzymes contain a 3-His ligand motif rather than a 2His/1Asp motif like most nonheme dioxygenases?
Topics: Amino Acid Motifs; Aspartic Acid; Biocatalysis; Catalytic Domain; Cysteine; Cysteine Dioxygenase; Heme; Histidine; Humans; Ligands; Models, Chemical; Models, Molecular | 2009 |
The effects of nitroxyl (HNO) on soluble guanylate cyclase activity: interactions at ferrous heme and cysteine thiols.
Topics: Animals; Binding Sites; Cattle; Cysteine; Dose-Response Relationship, Drug; Guanylate Cyclase; Heme; Iron; Lung; Models, Biological; Models, Chemical; Nitric Oxide; Nitrogen Oxides; Receptors, Cytoplasmic and Nuclear; Soluble Guanylyl Cyclase; Sulfhydryl Compounds; Vasodilator Agents | 2009 |
Trp180 of endothelial NOS and Trp56 of bacterial saNOS modulate sigma bonding of the axial cysteine to the heme.
Topics: Animals; Cloning, Molecular; Cysteine; Endothelium; Heme; Hydrogen Bonding; Mutation; Nitric Oxide; Nitric Oxide Synthase Type III; Spectrum Analysis, Raman; Staphylococcus aureus; Tryptophan | 2009 |
Visualizing changes in electron distribution in coupled chains of cytochrome bc(1) by modifying barrier for electron transfer between the FeS cluster and heme c(1).
Topics: Cysteine; Electron Transport; Electron Transport Complex III; Electrons; Heme; Iron-Sulfur Proteins; Kinetics; Oxidation-Reduction; Rhodobacter | 2010 |
Relative roles of heme-irons and globin-thiols in the genesis of acellular hemoglobin mediated vasoconstriction.
Topics: Animals; Aorta, Thoracic; Binding Sites; Cells, Cultured; Cysteine; Heme; Hemoglobins; Humans; Iron; Male; Mutation; Nitric Oxide; Organ Culture Techniques; Rats; Rats, Sprague-Dawley; Sulfhydryl Compounds; Vasoconstriction | 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 |
Identification of a thiol/disulfide redox switch in the human BK channel that controls its affinity for heme and CO.
Topics: Amino Acid Motifs; Amino Acid Sequence; Binding Sites; Binding, Competitive; Carbon Monoxide; Cysteine; Disulfides; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Ferric Compounds; Ferrous Compounds; Heme; Heme Oxygenase (Decyclizing); Humans; Large-Conductance Calcium-Activated Potassium Channel alpha Subunits; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Protein Binding; Sulfhydryl Compounds | 2010 |
Redox status affects the catalytic activity of glutamyl-tRNA synthetase.
Topics: Acidithiobacillus; Catalysis; Cysteine; Glutamate-tRNA Ligase; Heme; Oxidation-Reduction; Zinc | 2010 |
Formation of cysteine sulfenic acid by oxygen atom transfer from nitrite.
Topics: Cysteine; Ferric Compounds; Heme; Kinetics; Nitrites; Oxygen; Sulfenic Acids | 2010 |
Hemin binds to human cytoplasmic arginyl-tRNA synthetase and inhibits its catalytic activity.
Topics: Adenosine Triphosphate; Arginine-tRNA Ligase; Catalysis; Crystallography, X-Ray; Cysteine; Cytoplasm; Escherichia coli; Heme; Hemin; Humans; Kinetics; Ligands; Molecular Conformation; Mutagenesis, Site-Directed; Protein Binding | 2010 |
Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor rev-erb{beta}.
Topics: Cysteine; Disulfides; Heme; Humans; Iron; Ligands; Oxidation-Reduction; Oxidative Stress; Protein Binding; Protein Structure, Tertiary; Receptors, Cytoplasmic and Nuclear; Repressor Proteins; Transcription, Genetic | 2011 |
Molecular basis for the inability of an oxygen atom donor ligand to replace the natural sulfur donor heme axial ligand in cytochrome P450 catalysis. Spectroscopic characterization of the Cys436Ser CYP2B4 mutant.
Topics: Animals; Aryl Hydrocarbon Hydroxylases; Carbon Monoxide; Circular Dichroism; Cysteine; Cytochrome P450 Family 2; Heme; Iron; Ligands; Models, Molecular; Nitrogen Oxides; Oxygen; Point Mutation; Spectrophotometry; Sulfur | 2011 |
Unusual heme binding in the bacterial iron response regulator protein: spectral characterization of heme binding to the heme regulatory motif.
Topics: Amino Acid Motifs; Bacterial Proteins; Binding Sites; Bradyrhizobium; Cysteine; Heme; Iron; Models, Molecular; Spectrum Analysis, Raman; Transcription Factors | 2011 |
Biodiversity in sulfur metabolism in hemiascomycetous yeasts.
Topics: Amino Acids, Sulfur; Biodiversity; Cysteine; Genetic Variation; Glucosephosphate Dehydrogenase; Glutathione; Heme; Homocysteine; Methionine; NADP; Phylogeny; Sequence Alignment; Sequence Analysis, Protein; Sulfur; Yeasts | 2011 |
DiGeorge critical region 8 (DGCR8) is a double-cysteine-ligated heme protein.
Topics: Animals; Circular Dichroism; Cysteine; Electron Spin Resonance Spectroscopy; Heme; Horses; Humans; MicroRNAs; Muscle, Skeletal; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Porphyrins; Proline; Proteins; RNA-Binding Proteins; Selenomethionine; Spectrophotometry; Xenopus laevis | 2011 |
Cobalt cystathionine β-synthase: a cobalt-substituted heme protein with a unique thiolate ligation motif.
Topics: Circular Dichroism; Cloning, Molecular; Cobalt; Coordination Complexes; Cystathionine beta-Synthase; Cysteine; Escherichia coli; Heme; Hemeproteins; Histidine; Humans; Hydrogen-Ion Concentration; Ligands; Models, Molecular; Oxidation-Reduction; Protein Binding; Protein Structure, Tertiary; Pyridoxal Phosphate; Recombinant Proteins; Spectrophotometry, Atomic | 2011 |
Structure of a bacterial cell surface decaheme electron conduit.
Topics: Amino Acid Sequence; Bacterial Outer Membrane Proteins; Binding Sites; Crystallography, X-Ray; Cysteine; Cytochrome c Group; Cytochromes; Disulfides; Electron Spin Resonance Spectroscopy; Electron Transport; Flavin Mononucleotide; Heme; Iron; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Potentiometry; Protein Binding; Protein Structure, Tertiary; Shewanella | 2011 |
EPR investigation of the role of B10 phenylalanine in neuroglobin - evidence that B10Phe mediates structural changes in the heme region upon disulfide-bridge formation.
Topics: Brain; Cloning, Molecular; Cysteine; Disulfides; Electron Spin Resonance Spectroscopy; Escherichia coli; Globins; Heme; Humans; Hydrogen Peroxide; Kinetics; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Phenylalanine; Protein Binding; Protein Conformation; Recombinant Proteins; Spectrometry, Fluorescence; Transformation, Bacterial | 2011 |
Fluorescence dequenching makes haem-free soluble guanylate cyclase detectable in living cells.
Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Benzoates; CHO Cells; Cricetinae; Cricetulus; Cyclic GMP; Cysteine; Enzyme Activation; Enzyme Activators; Fluorescence; Fluorescent Dyes; Guanylate Cyclase; Heme; Humans; Molecular Sequence Data; Mutation; Nitric Oxide; Oxadiazoles; Oxazines; Oxidation-Reduction; Protein Engineering; Receptors, Cytoplasmic and Nuclear; Rotenone; Signal Transduction; Soluble Guanylyl Cyclase; Spectrometry, Fluorescence | 2011 |
Mechanism-based inactivation of human cytochrome P450 2B6 by clopidogrel: involvement of both covalent modification of cysteinyl residue 475 and loss of heme.
Topics: Aryl Hydrocarbon Hydroxylases; Base Sequence; Chromatography, High Pressure Liquid; Clopidogrel; Cysteine; Cytochrome P-450 CYP2B6; DNA Primers; Enzyme Inhibitors; Heme; Humans; Kinetics; Mutagenesis, Site-Directed; Oxidoreductases, N-Demethylating; Spectrometry, Mass, Electrospray Ionization; Tandem Mass Spectrometry; Ticlopidine | 2011 |
Cytochrome c(552) from Thermus thermophilus engineered for facile substitution of prosthetic group.
Topics: Amino Acid Substitution; Bacterial Proteins; Base Sequence; Cysteine; Cytochrome c Group; DNA Primers; Heme; Mutagenesis, Site-Directed; Protein Engineering; Protoporphyrins; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrophotometry; Thermus thermophilus | 2011 |
The conserved Trp-Cys hydrogen bond dampens the "push effect" of the heme cysteinate proximal ligand during the first catalytic cycle of nitric oxide synthase.
Topics: Cysteine; Heme; Hydrogen Bonding; Ligands; Mutagenesis, Site-Directed; Nitric Oxide Synthase; Oxidation-Reduction; Potentiometry; Spectrum Analysis, Raman; Staphylococcus aureus | 2011 |
The role of a disulfide bridge in the stability and folding kinetics of Arabidopsis thaliana cytochrome c(6A).
Topics: Amino Acid Sequence; Arabidopsis; Cyanobacteria; Cysteine; Cytochromes c6; Disulfides; Heme; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Oxidation-Reduction; Protein Folding; Protein Structure, Tertiary; Serine; Thermodynamics | 2012 |
Effects of the bHLH domain on axial coordination of heme in the PAS-A domain of neuronal PAS domain protein 2 (NPAS2): conversion from His119/Cys170 coordination to His119/His171 coordination.
Topics: Cysteine; Heme; Histidine; Protein Structure, Tertiary; Transcription Factors | 2012 |
Role of cysteine residues in heme binding to human heme oxygenase-2 elucidated by two-dimensional NMR spectroscopy.
Topics: Carbon Isotopes; Cysteine; Heme; Heme Oxygenase (Decyclizing); Humans; Isotope Labeling; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Binding; Protein Folding; Protein Structure, Tertiary | 2012 |
Heme-assisted S-nitrosation desensitizes ferric soluble guanylate cyclase to nitric oxide.
Topics: Alkylation; Animals; Catalytic Domain; Cysteine; Guanylate Cyclase; Heme; Humans; Hydroxides; Iron; Kinetics; Mutant Proteins; Nitric Oxide; Nitrosation; Nucleotides; Oxidation-Reduction; Protein Binding; Rats; Receptors, Cytoplasmic and Nuclear; Soluble Guanylyl Cyclase; Sulfhydryl Compounds | 2012 |
Detection of reaction intermediates during human cystathionine β-synthase-monitored turnover and H2S production.
Topics: Cystathionine beta-Synthase; Cysteine; Heme; Homocysteine; Humans; Hydrogen Sulfide; Kinetics; Serine | 2012 |
Conformational dynamics in human neuroglobin: effect of His64, Val68, and Cys120 on ligand migration.
Topics: Amino Acid Sequence; Calorimetry; Carbon Monoxide; Cysteine; Globins; Heme; Humans; Hydrophobic and Hydrophilic Interactions; Kinetics; Ligands; Models, Molecular; Molecular Conformation; Nerve Tissue Proteins; Neuroglobin; Protein Conformation; Thermodynamics | 2012 |
Preparation of cysteine-34-nitroxide spin labeled human α₁-microglobulin.
Topics: Alpha-Globulins; Amino Acid Sequence; Circular Dichroism; Cyclic N-Oxides; Cysteine; Electron Spin Resonance Spectroscopy; Heme; Humans; Protein Conformation; Protein Folding; Protein Structure, Secondary; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spin Labels | 2013 |
Snapshots of a protein folding intermediate.
Topics: Bacterial Proteins; Circular Dichroism; Crystallography, X-Ray; Cysteine; Cytochrome c Group; Heme; Kinetics; Models, Molecular; Molecular Structure; Mutation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Unfolding; Spectrometry, Fluorescence; Thermus thermophilus; Time Factors | 2013 |
Is the heme pocket region modulated by disulfide-bridge formation in fish and amphibian neuroglobins as in humans?
Topics: Amino Acid Sequence; Animals; Cysteine; Disulfides; Electron Spin Resonance Spectroscopy; Fishes; Globins; Heme; Humans; Hydrogen Peroxide; Molecular Sequence Data; Nerve Tissue Proteins; Neuroglobin; Protein Binding; Protein Folding; Sequence Homology, Amino Acid; Xenopus | 2013 |
A model theoretical study on ligand exchange reactions of CooA.
Topics: Bacterial Proteins; Carbon Monoxide; Cysteine; Ferric Compounds; Ferrous Compounds; Gases; Heme; Hemeproteins; Ligands; Models, Molecular; Quantum Theory; Rhodospirillum rubrum; Trans-Activators | 2013 |
Pro-oxidant properties of indolone-N-oxides in relation to their antimalarial properties.
Topics: Antimalarials; Artemisinins; Chloroquine; Cyclic N-Oxides; Cysteine; Electron Spin Resonance Spectroscopy; Enzyme Activation; Erythrocyte Membrane; Heme; Hemin; Humans; Indoles; Intracellular Signaling Peptides and Proteins; Iron; Models, Biological; Models, Chemical; Oxidation-Reduction; Protein-Tyrosine Kinases; Reactive Oxygen Species; Solutions; Syk Kinase | 2013 |
Analysis of Fe(III) heme binding to cysteine-containing heme-regulatory motifs in proteins.
Topics: Amino Acid Sequence; Cysteine; Ferric Compounds; Heme; Magnetic Resonance Spectroscopy; Molecular Structure; Peptides; Protein Binding; Protein Structure, Tertiary; Proteins; Spectrum Analysis, Raman | 2013 |
Mutation of cysteine residues alters the heme-binding pocket of indoleamine 2,3-dioxygenase-1.
Topics: Binding Sites; Catalysis; Cysteine; Enzyme Stability; Heme; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Recombinant Proteins | 2013 |
Kinetics of reversible reductive carbonylation of heme in human cystathionine β-synthase.
Topics: Carbon Monoxide; Cystathionine beta-Synthase; Cysteine; Heme; Histidine; Humans; Kinetics; Ligands; Oxygen; Protein Binding; Protein Carbonylation; Signal Transduction; Spectrum Analysis, Raman; Sulfur Dioxide; Superoxides | 2013 |
The 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 |
Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis.
Topics: Betaine; Catalysis; Cysteine; Cysteine Dioxygenase; Heme; Histidine; Humans; Methylhistidines; Models, Biological; Molecular Structure; Mycobacterium smegmatis; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction | 2014 |
Oxygen-linked S-nitrosation in fish myoglobins: a cysteine-specific tertiary allosteric effect.
Topics: Allosteric Regulation; Amino Acid Sequence; Animals; Biotin; Cysteine; Fish Proteins; Fishes; Heme; Humans; Kinetics; Molecular Sequence Data; Myocardium; Myoglobin; Nitric Oxide; Nitrosation; Oxygen; Species Specificity | 2014 |
Pulsed electron paramagnetic resonance study of domain docking in neuronal nitric oxide synthase: the calmodulin and output state perspective.
Topics: Animals; Calcium; Calmodulin; Computer Simulation; Cysteine; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Kinetics; Magnetic Phenomena; Models, Molecular; Nitric Oxide Synthase Type I; Rats; Spin Labels; Transfection | 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 |
The octahaem MccA is a haem c-copper sulfite reductase.
Topics: Bacterial Proteins; Biocatalysis; Catalytic Domain; Copper; Crystallography, X-Ray; Cysteine; Heme; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Sulfites; Sulfur Dioxide; Wolinella | 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 |
Protein kinase G-regulated production of H2S governs oxygen sensing.
Topics: Amino Acid Motifs; Animals; Calcium; Carotid Body; Cyclic GMP-Dependent Protein Kinases; Cystathionine gamma-Lyase; Cysteine; Female; Gases; HEK293 Cells; Heme; Heme Oxygenase (Decyclizing); Humans; Hydrogen Sulfide; Hypoxia; Male; Mice; Mice, Knockout; Oxygen; Phosphorylation; Protein Isoforms; Respiration | 2015 |
Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c(552) and its b-type variant.
Topics: Alanine; Bacteria; Bacterial Proteins; Cysteine; Cytochrome c Group; Heme; Hydrogen; Models, Molecular; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Conformation | 2015 |
Spectroscopic studies on peptides and proteins with cysteine-containing heme regulatory motifs (HRM).
Topics: Amino Acid Motifs; Amino Acid Sequence; Aquaporins; Cation Transport Proteins; Cell Membrane; Crystallography, X-Ray; Cysteine; Electron Spin Resonance Spectroscopy; Escherichia coli Proteins; Heme; Hemeproteins; Models, Molecular; Molecular Sequence Data; Peptides; Protein Structure, Tertiary; Proteins; Sequence Homology, Amino Acid; Spectrophotometry | 2015 |
An HASApf-redoxin complex causing asymmetric catalytic oxidation via the regenerative formation of a reactive oxygen species.
Topics: Alginates; Amino Acid Sequence; Bacterial Proteins; Cysteine; Gels; Glucuronic Acid; Heme; Hexuronic Acids; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Pseudomonas fluorescens; Reactive Oxygen Species | 2015 |
Improvement of heme oxygenase-1-based heme sensor for quantifying free heme in biological samples.
Topics: Acetates; Amino Acid Substitution; Animals; Biosensing Techniques; Catalytic Domain; Chromones; Cysteine; Fluorescent Dyes; Heme; Heme Oxygenase (Decyclizing); Hydrolysis; Japan; Kinetics; Microsomes, Liver; Mutant Proteins; Peptide Fragments; Rats; Recombinant Proteins; Rhodamines; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Sulfonic Acids; Titrimetry | 2015 |
Sickle Cell Hemoglobin in the Ferryl State Promotes βCys-93 Oxidation and Mitochondrial Dysfunction in Epithelial Lung Cells (E10).
Topics: Anemia, Hemolytic; Anemia, Sickle Cell; Catalysis; Cyclic N-Oxides; Cysteine; Energy Metabolism; Heme; Heme Oxygenase (Decyclizing); Hemoglobin, Sickle; Humans; Hydrogen Peroxide; Iron; Lung; Methemoglobin; Mitochondria; Oxidation-Reduction; Oxygen Consumption; Respiratory Mucosa | 2015 |
The Characteristics and Regulatory Mechanisms of Superoxide Generation from eNOS Reductase Domain.
Topics: Animals; Biopterins; Calmodulin; Cattle; Cysteine; Electron Spin Resonance Spectroscopy; Heme; Mutation; Nitric Oxide Synthase Type III; Oxidation-Reduction; Phosphorylation; Protein Structure, Tertiary; Serine; Superoxides | 2015 |
Probing the nitrite and nitric oxide reductase activity of cbb3 oxidase: resonance Raman detection of a six-coordinate ferrous heme-nitrosyl species in the binuclear b3/CuB center.
Topics: Copper; Cysteine; Electron Transport Complex IV; Heme; Iron; Nitric Oxide; Nitrites; Nitrous Oxide; Oxidation-Reduction; Pseudomonas stutzeri; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman | 2015 |
Heme A synthase in bacteria depends on one pair of cysteinyls for activity.
Topics: Aeropyrum; Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Cysteine; Cytochrome b Group; Gene Expression; Heme; Membrane Proteins; Molecular Sequence Data; Mutation; Oxygen; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity | 2016 |
Effects of mutations in active site heme ligands on the spectroscopic and catalytic properties of SoxAX cytochromes.
Topics: Amino Acid Substitution; Bacterial Proteins; Biocatalysis; Catalytic Domain; Cloning, Molecular; Copper; Cysteine; Cytochromes; Escherichia coli; Gene Expression; Heme; Kinetics; Ligands; Mutation; Oxidation-Reduction; Recombinant Proteins; Rhizobiaceae; Rhodobacter capsulatus; Structure-Activity Relationship; Thiosulfates | 2016 |
Structural basis of haem-iron acquisition by fungal pathogens.
Topics: Aspartic Acid; Biological Transport; Candida albicans; Crystallography, X-Ray; Cysteine; Fungal Proteins; Heme; Hemeproteins; Histidine; Iron; Membrane Proteins; Molecular Conformation | 2016 |
Exploring second coordination sphere effects in nitric oxide synthase.
Topics: Animals; Binding Sites; Catalytic Domain; Circular Dichroism; Coordination Complexes; Cysteine; Cytochrome P-450 Enzyme System; Heme; Hydrogen Bonding; Iron; Ligands; Models, Molecular; Mutation; Nitric Oxide; Nitric Oxide Synthase Type I; Oxidation-Reduction; Rats; Spectrophotometry; Static Electricity; Thermodynamics | 2016 |
CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity.
Topics: Binding Sites; Carbon Monoxide; Circular Dichroism; Cysteine; Ferric Compounds; Ferrous Compounds; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Ligands; Lysine; MicroRNAs; Models, Biological; Nitric Oxide; Protein Binding; RNA-Binding Proteins; Spectrum Analysis, Raman | 2016 |
Dual role of the active-center cysteine in human peroxiredoxin 1: Peroxidase activity and heme binding.
Topics: Amino Acid Substitution; Animals; Catalytic Domain; Cysteine; Cytosol; Heme; Hemin; Humans; Models, Biological; Mutagenesis, Site-Directed; Peroxiredoxins; Protein Binding; Rats; Recombinant Proteins; Spectrophotometry | 2017 |
A distal ligand mutes the interaction of hydrogen sulfide with human neuroglobin.
Topics: Catalysis; Crystallography, X-Ray; Cysteine; Electron Spin Resonance Spectroscopy; Globins; Heme; Hemoglobins; Histidine; Humans; Hydrogen Sulfide; Hydrogen-Ion Concentration; Kinetics; Ligands; Mass Spectrometry; Mutation; Myoglobin; Nerve Tissue Proteins; Neuroglobin; Oxygen; Protein Conformation; Spectrometry, Mass, Electrospray Ionization; Spectrum Analysis, Raman; Sulfides; Thiosulfates; Thrombin | 2017 |
The Iron Chaperone Protein CyaY from Vibrio cholerae Is a Heme-Binding Protein.
Topics: Amino Acid Motifs; Bacterial Proteins; Binding Sites; Cloning, Molecular; Cysteine; Escherichia coli; Gene Expression; Heme; Hemeproteins; Ion Transport; Iron; Kinetics; Models, Molecular; Molecular Chaperones; Mutation; Protein Binding; Protein Interaction Domains and Motifs; Protein Multimerization; Protein Structure, Secondary; Recombinant Proteins; Tyrosine; Vibrio cholerae | 2017 |
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 |
The influence of the Cys46/Cys55 disulfide bond on the redox and spectroscopic properties of human neuroglobin.
Topics: Cysteine; Disulfides; Electrochemistry; Globins; Heme; Humans; Hydrogen-Ion Concentration; Models, Molecular; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Spectrometry, Fluorescence; Spectrum Analysis; Thermodynamics | 2018 |
Strong modulation of nitrite reductase activity of cytoglobin by disulfide bond oxidation: Implications for nitric oxide homeostasis.
Topics: Cysteine; Cytoglobin; Disulfides; Heme; Humans; Iron; Nitric Oxide; Nitrite Reductases; Oxidation-Reduction; Oxygenases; Protein Multimerization; Recombinant Proteins | 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 |
Crystal Structures of Cystathionine β-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time.
Topics: Catalysis; Cystathionine beta-Synthase; Cysteine; Heme; Humans; Kinetics; Models, Molecular; Oxidation-Reduction; Pyridoxal Phosphate; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 2018 |
Structure of the alternative complex III in a supercomplex with cytochrome oxidase.
Topics: Cryoelectron Microscopy; Cysteine; Cytochrome c Group; Cytochromes a; Cytochromes a3; Electron Transport Complex III; Flavobacterium; Heme; Lipid Bilayers; Lipids; Models, Molecular; Nanostructures; Oxidation-Reduction; Protein Subunits | 2018 |
Living with Oxygen.
Topics: Catalytic Domain; Coordination Complexes; Cysteine; Cytochrome P-450 Enzyme System; Heme; Metals, Heavy; Methionine; Oxidation-Reduction; Oxygen; Protein Structural Elements; Tryptophan; Tyrosine | 2018 |
Enzymatic assembly of carbon-carbon bonds via iron-catalysed sp
Topics: Alkylation; Animals; Biocatalysis; Carbon; Coenzymes; Cysteine; Cytochrome P-450 Enzyme System; Directed Molecular Evolution; Heme; Hydrogen; Iron; Male; Methane; Serine; Substrate Specificity; Vitamin B 12 | 2019 |
Use of cysteine as a spectroscopic probe for determination of heme-scavenging capacity of serum proteins and whole human serum.
Topics: Blood Proteins; Cysteine; Heme; Hemoglobins; Hemolysis; Hemopexin; Humans; Oxidation-Reduction; Protein Binding; Spectrum Analysis | 2019 |
Importance of the iron-sulfur component and of the siroheme modification in the resting state of sulfite reductase.
Topics: Catalytic Domain; Cysteine; Ferric Compounds; Heme; Iron-Sulfur Proteins; Molecular Dynamics Simulation; Oxidoreductases Acting on Sulfur Group Donors; Protein Binding | 2020 |
Cystathionine β-synthase is involved in cysteine biosynthesis and H
Topics: Biocatalysis; Cystathionine; Cystathionine beta-Synthase; Cystathionine gamma-Lyase; Cysteine; DNA, Complementary; Genes, Protozoan; Heme; Homocysteine; Hydrogen Sulfide; Kinetics; Serine; Toxoplasma | 2020 |
Heme-Induced Oxidation of Cysteine Groups of Myofilament Proteins Leads to Contractile Dysfunction of Permeabilized Human Skeletal Muscle Fibres.
Topics: Amino Acid Sequence; Calcium; Cysteine; Heme; Humans; Mass Spectrometry; Muscle Contraction; Muscle Fibers, Skeletal; Muscle Proteins; Myofibrils; Oxidation-Reduction | 2020 |
The pH-Induced Selectivity Between Cysteine or Histidine Coordinated Heme in an Artificial α-Helical Metalloprotein.
Topics: Amino Acid Sequence; Catalysis; Cysteine; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Metalloproteins; Oxidation-Reduction; Oxygen; Peptides; Protein Conformation, alpha-Helical | 2021 |
Heme biosynthesis depends on previously unrecognized acquisition of iron-sulfur cofactors in human amino-levulinic acid dehydratase.
Topics: Amino Acid Motifs; Biosynthetic Pathways; Cell Line; Coenzymes; Cysteine; Heme; Humans; Iron; Iron-Sulfur Proteins; Porphobilinogen Synthase; Recombinant Proteins; Sulfur | 2020 |
Histidine
Topics: Chlorides; Cysteine; Halogens; Heme; Histidine; Oxidation-Reduction; Peroxidase; Peroxidases | 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 |
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 |
Modeling the Ligand Effect on the Structure of CYP 450 Within the Density Functional Theory.
Topics: Cysteine; Density Functional Theory; Heme; Iron; Ligands | 2022 |
A haem-sequestering plant peptide promotes iron uptake in symbiotic bacteria.
Topics: Bacteria; Cysteine; Heme; Humans; Iron; Nitrogen; Nitrogenase; Peptides; Rhizobium; Symbiosis | 2022 |
Construction of 5-aminolevulinic acid synthase variants by cysteine-targeted mutation to release heme inhibition.
Topics: 5-Aminolevulinate Synthetase; Aminolevulinic Acid; COVID-19; Cysteine; Heme; Hemin; Humans; Mutation | 2022 |
GLB-3: A resilient, cysteine-rich, membrane-tethered globin expressed in the reproductive and nervous system of Caenorhabditis elegans.
Topics: Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Cysteine; Globins; Heme; Hydrogen Peroxide; Nervous System | 2023 |
Sulfmyoglobin production by free cysteine during thermal treatment: Involvement of heme iron in the production of free radicals.
Topics: Animals; Cysteine; Free Radicals; Heme; Horses; Hydrogen Peroxide; Iron; Metmyoglobin; Myoglobin; Oxidation-Reduction | 2023 |
Nitric oxide delivery and heme-assisted S-nitrosation by the bedbug nitrophorin.
Topics: Animals; Bedbugs; Cysteine; Ferric Compounds; Ferrous Compounds; Heme; Iron; Nitric Oxide; Nitrosation | 2023 |