methionine has been researched along with heme in 195 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 78 (40.00) | 18.7374 |
| 1990's | 32 (16.41) | 18.2507 |
| 2000's | 54 (27.69) | 29.6817 |
| 2010's | 25 (12.82) | 24.3611 |
| 2020's | 6 (3.08) | 2.80 |
| Authors | Studies |
|---|---|
| Dee, J; McCullough, CH | 1 |
| Kaempfer, R | 1 |
| Giloh, H; Mager, J; Schochot, L | 1 |
| Gupta, RK; Petersen, RL | 1 |
| Cass, RD; Stellwagen, E | 1 |
| Das, A; Dasgupta, A; Gupta, NK; London, IM; Majumdar, A; Ralston, R; Ranu, RS; Roy, R | 1 |
| London, IM; Ranu, RS | 1 |
| Das, A; Das, HK; Ghosh-Dastidar, P; Grace, M; Gupta, NK; Palmieri, S; Ralston, RO; Roy, R; Yaghmai, B | 1 |
| Das, A; Das, H; Grace, M; Gupta, NK; Ralston, RO | 1 |
| Davis, PS; Murphy, MJ; Siegel, LM | 1 |
| Bethge, PH; Czerwinski, EW; Mathews, FS; Xavier, AV | 1 |
| Gross, M | 3 |
| Arnstein, HR; Bonanou-Tzedaki, SA; Sheeran, BA; Smith, KE | 1 |
| Esashi, T; Suzue, R; Yokota, F | 1 |
| Clemens, MJ | 1 |
| Hardesty, B; Kramer, G; Pinphanichakarn, P | 1 |
| Cahn, F; Lubin, M | 1 |
| Carstens, M; Neethling, AC; Percy, VA; Shanley, BC | 1 |
| Clark-Lewis, I; Wallace, CJ | 1 |
| Daldal, F; Davidson, E; Gray, KA | 1 |
| Casey, WM; Keesler, GA; Parks, LW | 1 |
| Chiu, ML; La Mar, GN; Lee, KB; Sligar, SG; Walker, FA; Wu, JZ; Yu, LP | 1 |
| Padmanaban, G; Surolia, N | 1 |
| Baker, DC; Bondoc, LL; Hebbler, A; Timkovich, R; Yap-Bondoc, F | 1 |
| Cheesman, MR; Greenwood, C; Kadir, F; Moore, GR; Thomson, AJ | 1 |
| Bain, MD; Bingham, P; Chalmers, RA; Jones, M; Purkiss, P; Stacey, TE | 1 |
| Gadsby, PM; Hartshorn, RT; Moura, JJ; Sinclair-Day, JD; Sykes, AG; Thomson, AJ | 1 |
| Harel, S; Kanner, J | 1 |
| Gray, HB; Raphael, AL | 1 |
| Senn, H; Wüthrich, K | 2 |
| Moench, S; Satterlee, JD | 1 |
| Cox, TM; Gardner, LC | 1 |
| Bezrukov, NV; Frasch, VN; Novikov, NM; Tikhatchek, ES; Uzhansky, YG | 1 |
| Kon, H | 1 |
| Mathews, MB | 1 |
| Ivanetich, K; Kaminsky, LS; Miller, V | 1 |
| Azzi, A; Folin, M; Jori, G; Tamburro, AM | 1 |
| Brayley, A; Hunt, T; Mathews, MB | 1 |
| Hunt, RT; Hunter, AR; Jackson, RJ; Robertson, HD | 1 |
| Aviram, I; Krauss, Y | 1 |
| Arutyunyan, AM; Sharonov, YA | 1 |
| Brayley, A; Hunt, T; Jackson, RJ; Legon, S | 1 |
| Stellwagen, E; Wilgus, H | 1 |
| Bitar, KG; Lowenkron, S; Vinogradov, SN | 1 |
| Brunori, M; Dupré, S; Greenwood, C; Wilson, MT | 1 |
| Hunt, T; Jackson, RJ; Legon, S | 1 |
| Lodish, HF | 1 |
| Clemens, MJ; Henshaw, EC; London, IM; Rahamimoff, H | 1 |
| Rabinovitz, M | 1 |
| Byrne, MJ; Davison, AJ; Kaminsky, LS | 1 |
| Desalu, O; Lodish, HF | 1 |
| Goldberg, IH; Kappen, LS | 1 |
| Balkow, K; Fisher, JM; Mizuno, S; Rabinovitz, M | 1 |
| Balkow, K; Mizuno, S; Rabinovitz, M | 1 |
| Noble, RW; Ranney, HM; Sharma, VS | 1 |
| Ben-Hayyim, G; Schejter, A | 1 |
| Bryant, MP; Varel, VH | 1 |
| Folin, M; Galiazzo, G; Gennari, G; Jori, G | 1 |
| Gupta, RK; Koenig, SH | 1 |
| Bäuerlein, E; Klingenfuss, M; Wieland, T | 1 |
| Corradin, G; Harbury, HA | 1 |
| Atassi, MZ | 1 |
| Hager, LP; Warme, PK | 2 |
| Brezík, Z; Neuwirt, J; Ponka, P; Sperl, M | 1 |
| Hillman, K; Krausz, LM; Wainio, WW | 1 |
| Craigie, JS; Laycock, MV | 1 |
| Nanzyo, N; Sano, S | 1 |
| Stellwagen, E | 1 |
| O'Brien, PJ | 1 |
| Galiazzo, G; Jori, G; Scoffone, E | 1 |
| Stellwagen, E; Van Rooyan, S | 1 |
| Billeter, M; Senn, H; Wüthrich, K | 1 |
| Keller, RM; Senn, H; Wüthrich, K | 1 |
| Koul, AK; Nix, PT; Warme, PK; Wasserman, GF | 1 |
| Parr, GR; Taniuchi, H | 1 |
| Bosshard, HR | 1 |
| Krogmann, DW; Markley, JL; Ulrich, EL | 1 |
| Bruschi, M; Guerlesquin, F; Senn, H; Wüthrich, K | 1 |
| Beattie, DS; Clejan, L; Gollub, EG; Liu, KP; Sprinson, DB | 1 |
| Hardesty, B; Kramer, G; Wallis, MH | 1 |
| Banci, L; Bertini, I; Bren, KL; Gray, HB; Sompornpisut, P; Turano, P | 1 |
| Gennis, RB; Georgiou, C; Ghaim, JB; Kaysser, TM | 1 |
| Cheesman, MR; Gennis, RB; Kaysser, T; Peng, Q; Peterson, J; Spinner, F; Thomson, AJ | 1 |
| Costa, HS; Santos, H; Turner, DL | 1 |
| Campos, AP; Canters, GW; Hill, HA; Hunt, NI; Teixeira, M; Ubbink, M | 1 |
| Brinigar, WS; Bucci, JL; Chiancone, E; Fronticelli, C; Gattoni, M; Lu, AL | 1 |
| Conover, RC; Finnegan, MG; Garcia Castillo, MC; Johnson, MK; Knaff, DB | 1 |
| Bren, KL; Casimiro, DR; Gray, HB; Lu, Y; Richards, JH | 1 |
| Bhuyan, A; Chan, CK; Eaton, WA; Henry, ER; Hofrichter, J; Hu, Y; Jones, CM; Luck, SD; Roder, H | 1 |
| Aguiar, AP; Campos, AP; Costa, HS; Santos, H; Teixeira, M; Turner, DL; Xavier, AV | 1 |
| Aguiar, AP; Campos, AP; De La Rosa, MA; Hervás, M; Navarro, JA; Ortega, JM; Regalla, M; Teixeira, M; Xavier, AV | 1 |
| Chapman, SK; Manson, FD; Miles, CS; Reid, GA | 1 |
| Eaton, WA; Hagen, SJ; Hofrichter, J; Szabo, A | 1 |
| Barker, PD; Cheesman, MR; de Oliveira, P; Hill, HA; Nerou, EP; Thomson, AJ | 1 |
| Barker, PD; Freund, SM | 1 |
| Fazzio, TG; Roth, JR | 1 |
| Elöve, GA; Pinheiro, TJ; Roder, H; Watts, A | 1 |
| Ascoli, F; Santucci, R | 1 |
| Englander, SW; Mayne, L; Xu, Y | 1 |
| Rivera, M; Rodríguez, JC | 1 |
| Durham, B; Gennis, RB; Millett, F; Sadoski, RC; Wang, K; Zaslavsky, D | 1 |
| Silkstone, G; Stanway, G; Wilson, MT | 1 |
| Daldal, F; Darrouzet, E; Knaff, DB; Li, J; Mandaci, S; Qin, H | 1 |
| Barker, PD; Fearnley, IM; Rice, JK | 1 |
| Cho, YS; Pakrasi, HB; Whitmarsh, J | 1 |
| Allen, JW; Chapman, SK; Ferguson, SJ; Koppenhöfer, A; Turner, KL | 1 |
| Turner, DL | 1 |
| Finkelstein, JD | 1 |
| Howes, BD; Smith, AT; Smulevich, G; Veitch, NC; White, CG | 1 |
| Carswell, CW; Hagen, SJ; Sjolander, EM | 1 |
| Backgren, C; Jasaitis, A; Morgan, JE; Puustinen, A; Verkhovsky, MI; Wikström, M | 1 |
| Gold, MH; Li, B; Renganathan, V; Rotsaert, FA | 1 |
| Daldal, F; Darrouzet, E; Dutton, PL; Moser, CC; Osyczka, A | 1 |
| de Waal, EC; Louro, RO; Turner, DL; Ubbink, M | 1 |
| Antholine, W; Ferguson-Miller, S; Kang, UG; Schmidt, B; Zhen, Y | 1 |
| Banci, L; Bertini, I; Cavallaro, G; Luchinat, C | 1 |
| Blouin, C; Guillemette, JG; Wallace, CJ | 1 |
| Kitagawa, T; Mizutani, Y; Sagami, I; Sasakura, Y; Sato, A; Shimizu, T; Sugiyama, S | 1 |
| Bartalesi, I; Bertini, I; Ghosh, K; Rosato, A; Turano, P | 1 |
| Hasegawa, J; Igarashi, Y; Kameda, T; Kobayashi, Y; Matsuo, H; Minakawa, K; Sambongi, Y; Tachiiri, N; Terui, N; Uchiyama, S; Yamamoto, Y | 1 |
| Matsui, T; Sagami, I; Sasakura, Y; Shimizu, T; Watanabe, M | 1 |
| Qian, C; Tang, W; Wang, J; Wu, Y; Yao, Y; Ye, K | 1 |
| BABCOCK, KL; DANIEL, JW; RUSCH, HP; SIEVERT, AH | 1 |
| BRYANT, MP; PITTMAN, KA | 1 |
| Kawachi, R; Kume, T; Nagasawa, N; Nishio, T; Oku, T; Satoh, T; Suruga, K; Yamada, S | 1 |
| Chapman, SK; Miles, CS; Mowat, CG; Reid, GA; Rothery, EL; Walkinshaw, MD | 1 |
| Araki, Y; Igarashi, J; Ito, O; Matsui, T; Sagami, I; Sasakura, Y; Shimizu, T; Sugiyama, S; Taguchi, S | 1 |
| Hirata, S; Matsui, T; Sagami, I; Sasakura, Y; Shimizu, T; Sugiyama, S; Yoshimura, T | 1 |
| Ferguson, SJ; Redfield, C; Smith, LJ; Wain, R | 1 |
| Benson, DR; Cowley, AB; Lukat-Rodgers, GS; Rodgers, KR | 1 |
| Kurokawa, H; Lee, DS; Mikami, B; Raman, CS; Sagami, I; Shimizu, T; Watanabe, M | 1 |
| Brunori, M; D'Itri, E; Forte, E; Giuffrè, A; Ludwig, B; Richter, OM; Sarti, P; Scandurra, FM | 1 |
| Bren, KL; Karan, EF; Rabinowitz, TM; Russell, BS; Wen, X; Zhong, L | 1 |
| Dohmae, N; Iizuka, T; Ishida, M; Isogai, Y; Oku, T; Shiro, Y | 1 |
| Alvarez, DE; Buldain, G; de Montellano, PR; Huang, L; Lad, L; Niemevz, F; Poulos, TL; Wang, J | 1 |
| Bottin, H; Boussac, A; Ducruet, JM; Kirilovsky, D; Ortega, JM; Roncel, M; Rutherford, AW; Sugiura, M; Wilson, A; Zurita, JL | 1 |
| Anderson, VE; Nukuna, BN; Sun, G | 1 |
| Ascoli, F; Caroppi, P; Ferri, T; Fiorucci, L; Howes, BD; Santoni, E; Santucci, R; Sinibaldi, F; Smulevich, G | 1 |
| Cianetti, S; Kruglik, SG; Martin, JL; Négrerie, M; Vos, MH | 1 |
| Andrews, H; Burnap, RL; Eaton-Rye, JJ; Li, Z | 1 |
| Chung, MC; Leow, CK; Low, TY; Salto-Tellez, M | 1 |
| Goff, HM; Metcalfe, CL; Mistry, SC; Ott, M; Patel, N; Raven, EL; Singh, K | 1 |
| Bren, KL; Wen, X | 2 |
| Ghiladi, RA; Knudsen, GM; Medzihradszky, KF; Ortiz de Montellano, PR | 1 |
| Furtmüller, PG; Jakopitsch, C; Jantschko, W; Moguilevsky, N; Neugschwandtner, K; Obinger, C; Zederbauer, M | 1 |
| Canters, GW; Ubbink, M; van Roon, AM; Worrall, JA | 1 |
| Morais, F; Pereira, IA; Pires, RH; Teixeira, M; Venceslau, SS; Xavier, AV | 1 |
| Akutsu, H; Higuchi, Y; Ogata, H; Ozawa, K; Saitoh, T; Takayama, Y; Yahata, N | 1 |
| Cartron, ML; Ferguson, SJ; Zajicek, RS | 1 |
| Brusnichkin, AV; Izmailov, DY; Kagan, VE; Novikov, AA; Osipov, AN; Proskurnina, EV; Vladimirov, YA | 1 |
| Buchenau, B; Heinemann, IU; Jahn, D; Kahnt, J; Thauer, RK | 1 |
| Arciero, DM; Chen, Y; Hooper, AB; Liang, Q; Timkovich, R | 1 |
| Alayash, AI; Boykins, RA; Buehler, PW; Jia, Y; Venable, RM | 1 |
| Shimizu, T; Takahashi, H; Tanaka, A | 1 |
| Bendall, DS; Hirst, J; Howe, CJ; Luisi, BF; Marcaida, MJ; Moorlen, RJ; Reda, T; Schlarb-Ridley, BG; Wastl, J; Worrall, JA | 1 |
| Aranda, R; Dooley, DM; Fabian, M; Lei, B; Liu, M; Olson, JS; Phillips, GN; Ran, Y; Zhu, H | 1 |
| Cheesman, MR; Ekanem, IS; Girvan, HM; Leys, D; Littleford, RE; Munro, AW; Seward, HE; Smith, WE; Toogood, HS | 1 |
| Shimizu, T; Tanaka, A | 1 |
| Ferguson, SJ; Harvat, EM; Redfield, C; Stevens, JM | 1 |
| Brindley, AA; Ferguson, SJ; Rigby, SE; Warren, MJ; Zajicek, R | 1 |
| Beckerich, JM; Casaregola, S; Hébert, A | 1 |
| Andersson, KK; Harbitz, E | 1 |
| De La Rosa, MÁ; Díaz-Moreno, I; García-Heredia, JM; Hildebrandt, P; Ly, HK; Utesch, T | 1 |
| Dantas, JM; Londer, YY; Morgado, L; Pokkuluri, PR; Salgueiro, CA; Simões, T | 1 |
| Goodwin, DC; Ndontsa, EN; Njuma, OJ | 1 |
| Davidson, VL; Higgins, L; Williamson, HR; Wilmot, CM; Yukl, ET | 1 |
| Alayash, AI; Hicks, WA; Kassa, T; Mollan, TL; Olson, JS; Singleton, E; Soman, J; Strader, MB; Weiss, MJ; Wilson, MT | 1 |
| Ando, Y; Hirota, S; Nagao, S; Nugraheni, AD; Ren, C; Wang, Z | 1 |
| Bren, KL; Elliott, SJ; Levin, BD; Sullivan, KK; Walsh, KA | 1 |
| Goodwin, DC; Huang, J; Panizzi, JR; Panizzi, P; Smith, F | 1 |
| Jarzęcki, AA; Kruft, BI; Magliozzo, RS | 1 |
| Colaço, HG; Giuffrè, A; Leandro, P; Sarti, P; Vicente, JB | 1 |
| Bowman, HE; Burstyn, JN; Dent, MR | 1 |
| Sharma, GS; Singh, LR | 1 |
| Battista, T; Cervelli, M; Ciaccio, C; Coletta, M; Fiorucci, L; Howes, BD; Mariottini, P; Santucci, R; Smulevich, G; Tognaccini, L | 1 |
| Hirota, S; Nagao, S; Wang, Z; Yamashiro, N | 1 |
| Fita, I; Rovira, C; Wang, B | 1 |
| Arbelo-López, HD; López-Garriga, J; Rodriguez-Mackenzie, AD; Roman-Morales, EM; Wymore, T | 1 |
| Pletneva, EV; Zhong, F | 1 |
| Jameson, GNL; Kleffmann, T; Ledgerwood, EC; Parakra, RD | 1 |
| Gray, HB; Winkler, JR | 1 |
| Gao, SQ; He, B; Li, L; Lin, YW; Liu, HX; Wen, GB | 1 |
| Nesterova, AM; Remenshchikov, VE; Vladimirov, GK; Vladimirov, YA; Volkov, VV | 1 |
| Deng, Y; Hoke, KR; Pletneva, EV; Weaver, ML | 1 |
| Alonso-Mori, R; Bergmann, U; Biasin, E; Chollet, M; Driel, TBV; Gaffney, KJ; Gee, LB; Glownia, JM; Hadt, RG; Hartsock, RW; Hedman, B; Hodgson, KO; Kjaer, KS; Kroll, T; Kunnus, K; Lim, H; Mara, MW; Nelson, S; Reinhard, ME; Sokaras, D; Solomon, EI; Weninger, C | 1 |
| Aarsand, AK; Aguilera, P; Brunet, M; Deulofeu, R; García-Villoria, J; Gómez-Gómez, À; Pozo, OJ; Sandberg, S; To-Figueras, J; Wijngaard, R | 1 |
| Adamczyk, K; Blumberger, J; Butt, JN; Clarke, TA; Edwards, MJ; Hall, CR; Jeuken, LJC; Jiang, X; Meech, SR; Piper, SEH; Sazanovich, IV; Towrie, M; van Wonderen, JH; Wu, X; Zhang, H | 1 |
| Balwani, M; Fanelli, MJ; Gouya, L; Longo, N; Petrides, PE; Phillips, J; Plutzky, J; Rhyee, S; Sardh, E; Sweetser, MT; Ventura, P | 1 |
| El Baze, A; Knizia, D; Lakhssassi, A; Lakhssassi, N; Meksem, J; Meksem, K | 1 |
| Ben Aoun, S; Ibrahim, SM | 1 |
3 review(s) available for methionine and heme
| Article | Year |
|---|---|
Amino acid sequence, haem-iron co-ordination geometry and functional properties of mitochondrial and bacterial c-type cytochromes.
Topics: Amino Acid Sequence; Animals; Bacteria; Cytochrome c Group; Heme; Histidine; Iron; Ligands; Methionine; Mitochondria; Phylogeny; Protein Binding; Protein Conformation | 1985 |
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 |
Catalase in peroxidase clothing: Interdependent cooperation of two cofactors in the catalytic versatility of KatG.
Topics: Antitubercular Agents; Archaea; Bacteria; Bacterial Proteins; Catalase; Coenzymes; Heme; Isoniazid; Methionine; Models, Molecular; Mycobacterium tuberculosis; Peroxidase; Prodrugs; Tryptophan; Tyrosine | 2014 |
192 other study(ies) available for methionine and heme
| Article | Year |
|---|---|
Defined and semi-defined media for the growth of amoebae of Physarum polycephalum.
Topics: Amino Acids; Biotin; Culture Media; Glucose; Heme; Hydrogen-Ion Concentration; Iron; Methionine; Myxomycetes; Physarum; Thiamine | 1976 |
Binding of messenger RNA in initiation of eukaryotic translation.
Topics: Guanosine Triphosphate; Heme; Iodine Radioisotopes; Isotope Labeling; Kinetics; Methionine; Methods; Penicillium chrysogenum; Peptide Chain Initiation, Translational; Protein Biosynthesis; Ribonucleases; RNA, Messenger; RNA, Transfer, Amino Acyl | 1979 |
Inhibition of peptide chain initiation in lysates from ATP-depleted cells. II. Studies on the mechanism of the lesion and its relation to similar alterations caused by oxidized glutathione and hemin deprivation.
Topics: Adenine; Adenosine Triphosphate; Aerobiosis; Anaerobiosis; Animals; Cyclic AMP; Female; Fructosephosphates; Glutathione; Heme; Hemin; Hexosediphosphates; Methionine; Peptide Chain Initiation, Translational; Protein Biosynthesis; Reticulocytes; Ribosomes; RNA, Transfer; Tissue Extracts | 1975 |
Location of Cr(III) in the Cr(III)--cytochrome c complex as observed by NMR spectroscopy.
Topics: Animals; Chromium; Cytochrome c Group; Heme; Horses; Magnetic Resonance Spectroscopy; Methionine; Myocardium; Protein Binding; Protein Conformation | 1979 |
Complexation of iron hexacyanides by cytochrome c. Evidence for electron exchange at the exposed heme edge.
Topics: Animals; Binding Sites; Cytochrome c Group; Electron Transport; Ferricyanides; Ferrocyanides; Heme; Horses; Hydrogen-Ion Concentration; Ligands; Lysine; Methionine; Myocardium; Osmolar Concentration; Protein Binding | 1975 |
Regulation of protein synthesis in rabbit reticulocyte lysates by the heme-regulated protein kinase: inhibition of interaction of Met-tRNAfMet binding factor with another initiation factor in formation of Met-tRNAfMet.40S ribosomal subunit complexes.
Topics: Adenosine Triphosphate; Animals; Heme; Magnesium; Methionine; Peptide Chain Initiation, Translational; Peptide Initiation Factors; Phosphates; Protein Biosynthesis; Protein Kinases; Rabbits; Reticulocytes; Ribosomes; RNA, Transfer | 1978 |
Regulation of protein synthesis in rabbit reticulocyte lysates: additional initiation factor required for formation of ternary complex (eIF-2.GTP.Met-tRNAf) and demonstration of inhibitory effect of heme-regulated protein kinase.
Topics: Animals; Blood Proteins; Guanosine Triphosphate; Heme; Kinetics; Magnesium; Methionine; Molecular Weight; Peptide Chain Initiation, Translational; Peptide Initiation Factors; Protein Biosynthesis; Protein Kinases; Rabbits; Reticulocytes; RNA, Transfer | 1979 |
Protein synthesis in rabbit reticulocytes: mechanism of protein synthesis inhibition by heme-regulated inhibitor.
Topics: Animals; Blood Proteins; Guanosine Triphosphate; Heme; Kinetics; Methionine; Peptide Chain Initiation, Translational; Peptide Initiation Factors; Phosphorylation; Protein Biosynthesis; Rabbits; Reticulocytes; RNA, Transfer | 1979 |
Protein synthesis in rabbit reticulocytes: characteristics of a postribosomal supernatant factor that reverses inhibition of protein synthesis in heme-deficient lysates and inhibition of ternary complex (Met-tRNAfMet.eIF-2.GTP) formation by heme-regulated
Topics: Animals; Cytosol; Guanosine Triphosphate; Heme; Methionine; Molecular Weight; Peptide Chain Initiation, Translational; Peptide Initiation Factors; Phosphorylation; Protein Binding; Rabbits; Reticulocytes; RNA, Transfer, Amino Acyl | 1979 |
Incorporation of methionine-derived methyl groups into sirohaem by Escherichia coli.
Topics: Chemical Phenomena; Chemistry; Escherichia coli; Glucose; Heme; Methionine; Oxidoreductases; Sulfites | 1977 |
Identification of the haem ligands of cytochrome b562 by X-ray and NMR methods.
Topics: Amino Acid Sequence; Cytochromes; Escherichia coli; Heme; Histidine; Ligands; Magnetic Resonance Spectroscopy; Methionine; Protein Conformation; X-Ray Diffraction | 1978 |
Control of protein synthesis by hemin. Evidence that the hemin-controlled translational repressor inhibits formation of 80 S initiation complexes from 48 S intermediate initiation complexes.
Topics: Animals; Escherichia coli; Heme; Hemin; Kinetics; Methionine; Peptide Chain Initiation, Translational; Protein Biosynthesis; Proteins; Rabbits; Reticulocytes; RNA, Transfer | 1979 |
Regulation of protein synthesis by hemin. Evidence that the hemin-controlled translational repressor inhibits the rate of formation of 40S.Met-tRNAf complexes directly.
Topics: Animals; Heme; Hemin; Kinetics; Methionine; Molecular Weight; Peptide Chain Initiation, Translational; Protein Biosynthesis; Rabbits; Repressor Proteins; Reticulocytes; Ribosomes; RNA, Transfer; Transcription Factors | 1979 |
The high-temperature inactivation of rabbit reticulocyte lysates by a haemin-independent mechanism.
Topics: Animals; Cell-Free System; Cytosol; Ethylmaleimide; Heme; Hemin; In Vitro Techniques; Leucine; Methionine; Peptide Chain Initiation, Translational; Protein Biosynthesis; Rabbits; Reticulocytes; Ribosomes; Temperature | 1978 |
Nutritional anemia induced by excess methionine in rat and the alleviative effects of glycine on it.
Topics: 5-Aminolevulinate Synthetase; Amino Acids; Anemia; Animals; Blood Cells; Bone Marrow; Glycine; Heme; Iron; Liver; Methionine; Mixed Function Oxygenases; Organ Size; Rats | 1978 |
Isolation of two initiation factors that can partially reverse the inhibition of protein synthesis due to hemin deficiency or the hemin-controlled translational represssor in rabbit reticulocyte lysates.
Topics: Animals; Cell-Free System; Codon; Heme; Hemin; Methionine; Peptide Chain Initiation, Translational; Peptide Initiation Factors; Protein Binding; Protein Biosynthesis; Rabbits; Reticulocytes; Ribosomes; RNA, Transfer; Suppression, Genetic | 1977 |
Functional relationships between a reticulocyte polypeptide-chain-initiation factor (IF-MP) and the translational inhibitor involved in regulation of protein synthesis by haemin.
Topics: Animals; Blood Proteins; Guanosine Triphosphate; Heme; Hemin; Kinetics; Macromolecular Substances; Methionine; Peptide Chain Initiation, Translational; Peptide Initiation Factors; Polyribosomes; Protein Binding; Protein Biosynthesis; Rabbits; Reticulocytes; RNA, Transfer | 1976 |
Partial reaction of peptide initiation inhibited by the reticulocyte hemin-controlled repressor.
Topics: Animals; Binding Sites; Blood Proteins; Guanosine Triphosphate; Heme; Methionine; Peptide Chain Initiation, Translational; Peptide Initiation Factors; Rabbits; Reticulocytes; Ribosomes; RNA, Transfer | 1976 |
Ability of formyl-methionyl-tRNA to initiate globin synthesis in the presence of double-stranded RNA or in the absence of hemin.
Topics: Animals; Escherichia coli; Globins; Heme; Hemin; Leucine; Leucine-tRNA Ligase; Liver; Methionine; Methionine-tRNA Ligase; N-Formylmethionine; Peptide Chain Initiation, Translational; Protein Biosynthesis; Rabbits; Reticulocytes; RNA; RNA, Transfer; Valine; Valine-tRNA Ligase | 1975 |
Neurochemical aspects of porphyria. Studies on the possible neurotoxicity of delta-aminolaevulinic acid.
Topics: Aminolevulinic Acid; Animals; Behavior, Animal; Brain; Carbon Radioisotopes; Cerebral Ventricles; Female; Heme; Injections; Levulinic Acids; Liver; Lysine; Methionine; Nephrectomy; Nerve Tissue Proteins; Rats; Sulfur Radioisotopes | 1975 |
Functional role of heme ligation in cytochrome c. Effects of replacement of methionine 80 with natural and non-natural residues by semisynthesis.
Topics: Amino Acids; Animals; Catalysis; Cations; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Cytochrome c Group; Heme; Horses; Iron; Methionine; Mutation; Myocardium; Oxidation-Reduction; Oxygen; Spectrophotometry, Ultraviolet | 1992 |
Mutagenesis of methionine-183 drastically affects the physicochemical properties of cytochrome c1 of the bc1 complex of Rhodobacter capsulatus.
Topics: Amino Acid Sequence; Base Sequence; Carbon Monoxide; Chemical Phenomena; Chemistry, Physical; Cytochrome b Group; Cytochromes c1; Electrophoresis, Polyacrylamide Gel; Heme; Iron; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Restriction Mapping; Rhodobacter capsulatus; Spectrophotometry | 1992 |
Stimulation by heme of steryl ester synthase and aerobic sterol exclusion in the yeast Saccharomyces cerevisiae.
Topics: Acyltransferases; Aerobiosis; Aminolevulinic Acid; Esterification; Fatty Acids, Unsaturated; Heme; Lovastatin; Methionine; Saccharomyces cerevisiae; Sterol O-Acyltransferase; Sterols | 1992 |
1H NMR study of the solution molecular and electronic structure of Escherichia coli ferricytochrome b562: evidence for S = 1/2 in equilibrium S = 5/2 spin equilibrium for intact His/Met ligation.
Topics: Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrogen; Kinetics; Magnetic Resonance Spectroscopy; Methionine; Thermodynamics; X-Ray Diffraction | 1991 |
Chloroquine inhibits heme-dependent protein synthesis in Plasmodium falciparum.
Topics: Animals; Cell-Free System; Chloroquine; Eukaryotic Initiation Factor-2; Heme; Kinetics; Methionine; Phosphorylation; Plasmodium falciparum; Protein Biosynthesis; Protozoan Proteins; Rabbits; Reticulocytes; Ribosomes | 1991 |
C-methylation occurs during the biosynthesis of heme d1.
Topics: Bacterial Proteins; Carbon Isotopes; Cytochrome c Group; Cytochromes; Heme; Isotope Labeling; Magnetic Resonance Spectroscopy; Methionine; Methylation; Molecular Structure; Nitrite Reductases; Pseudomonas aeruginosa | 1990 |
Bis-methionine axial ligation of haem in bacterioferritin from Pseudomonas aeruginosa.
Topics: Bacterial Proteins; Binding Sites; Circular Dichroism; Cytochrome b Group; Electron Spin Resonance Spectroscopy; Ferritins; Heme; Methionine; Protein Binding; Protein Conformation; Pseudomonas aeruginosa; Species Specificity | 1990 |
Dietary treatment eliminates succinylacetone from the urine of a patient with tyrosinaemia type 1.
Topics: Amino Acid Metabolism, Inborn Errors; Female; Heme; Heptanoates; Heptanoic Acids; Humans; Infant; Methionine; Phenylalanine; Tyrosine | 1990 |
Redox properties of the diheme cytochrome c4 from Azotobacter vinelandii and characterisation of the two hemes by NMR, MCD and EPR spectroscopy.
Topics: Azotobacter; Cytochrome c Group; Diethyl Pyrocarbonate; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Methionine; Oxidation-Reduction; Spectrophotometry; Spectrum Analysis | 1989 |
Haemoglobin and myoglobin as inhibitors of hydroxyl radical generation in a model system of "iron redox" cycle.
Topics: Animals; Edetic Acid; Ferric Compounds; Free Radicals; Heme; Hemoglobins; Hydrogen Peroxide; Hydroxides; Hydroxyl Radical; Kinetics; Methionine; Models, Biological; Myoglobin; Oxidation-Reduction | 1989 |
Axial ligand replacement in horse heart cytochrome c by semisynthesis.
Topics: Animals; Chemical Phenomena; Chemistry; Cytochrome c Group; Heme; Histidine; Horses; Methionine; Myocardium; Protein Conformation; Spectrophotometry, Ultraviolet | 1989 |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c.
Topics: Animals; Cytochrome c Group; Deuterium; Deuterium Oxide; Heme; Histidine; Horses; Magnetic Resonance Spectroscopy; Methionine; Protein Conformation; Species Specificity; Tuna; Water | 1987 |
Biosynthesis of heme in immature erythroid cells. The regulatory step for heme formation in the human erythron.
Topics: Adolescent; Adult; Aminolevulinic Acid; Anemia, Sickle Cell; Animals; Bone Marrow; Child; Cycloheximide; Feedback; Female; Globins; Glycine; Heme; Humans; Iron Radioisotopes; Kinetics; Male; Methionine; Middle Aged; Protein Biosynthesis; Rabbits; Reticulocytes; Transferrin | 1988 |
Role of erythrocyte destruction products in the mechanism of erythropoiesis autoregulation.
Topics: Anemia; Animals; Blood Proteins; Blood Volume; Bone Marrow; Bone Marrow Examination; Cell Membrane; Cytoplasm; Erythrocytes; Erythropoiesis; Globins; Hematocrit; Heme; Hemoglobinometry; Hemolysis; Immune Sera; Iron Isotopes; Methionine; Oxygen Consumption; Rabbits; Reticulocytes; RNA; Sulfur Isotopes | 1970 |
Electron paramagnetic resonance of nitric oxide cytochrome C.
Topics: Animals; Chemical Phenomena; Chemistry; Cytochromes; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Methionine; Myocardium; Nitric Oxide; Powders; Radioisotopes | 1969 |
Further studies on the translation of globin mRNA and encephalomyocarditis virus RNA in a cell-free system from Krebs II ascites cells.
Topics: Amino Acids; Animals; Autoradiography; Carbon Isotopes; Carcinoma, Krebs 2; Centrifugation, Density Gradient; Encephalomyocarditis virus; Globins; Heme; Kinetics; Macromolecular Substances; Magnesium; Methionine; Mice; Peptide Chain Initiation, Translational; Peptides; Potassium Chloride; Rabbits; RNA, Messenger; RNA, Viral; Subcellular Fractions; Sulfur Isotopes; Trypsin; Viral Proteins | 1972 |
A reversal of heme crevice strengths of ferri- and ferrocytochrome c on carboxymethylation.
Topics: 1-Propanol; Animals; Chemical Phenomena; Chemistry; Cytochrome c Group; Electron Transport; Heme; Horses; Iron Chelating Agents; Methionine; Methylation; Myocardium; Protein Conformation; Spectrophotometry | 1972 |
Photo-oxidative modification of the heme ligands in horse heart ferricytochrome c: conformational and functional studies.
Topics: Amino Acids; Animals; Circular Dichroism; Cytochrome c Group; Electron Transport; Heme; Histidine; Horses; Kinetics; Membranes; Methionine; Mitochondria, Liver; Myocardium; Oxidation-Reduction; Oxygen Consumption; Photochemistry; Protein Binding; Protein Conformation; Rats; Spectrophotometry; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Sulfoxides | 1972 |
Specificity of the control of protein synthesis by haemin.
Topics: Animals; Blood Proteins; Cell-Free System; Electrophoresis, Polyacrylamide Gel; Encephalomyocarditis virus; Globins; Heme; Methionine; Protein Biosynthesis; Proteins; Rabbits; Reticulocytes; RNA, Messenger; RNA, Viral; Sulfur Isotopes; Viral Proteins | 1973 |
Initiation of globin synthesis in rabbit reticulocyte cell-free systems: inhibition by double-stranded RNA.
Topics: Animals; Bacteriophages; Cell-Free System; Coliphages; DNA; DNA, Viral; Globins; Heme; Hemolysis; Methionine; Peptide Chain Initiation, Translational; Phosphorus Radioisotopes; Poliovirus; Poly I-C; Protein Hydrolysates; Rabbits; Reoviridae; Reticulocytes; RNA, Transfer; RNA, Viral; Thymus Gland | 1972 |
The structure of the heme crevice of ferric cytochrome c alkylated at methionine-80.
Topics: Alkylation; Chemical Phenomena; Chemistry; Cytochrome c Group; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Ligands; Mathematics; Methionine; Protein Binding; Protein Conformation; Spectrophotometry, Ultraviolet | 1974 |
Fine structure of the magnetooptical rotatory dispersion curves and the surroundings of heme in ferrocytochrome c and its model compounds.
Topics: Acetates; Amides; Amino Acid Sequence; Animals; Bromine; Cyanides; Cytochrome c Group; Heme; Horses; Imidazoles; Iodoacetates; Iron; Magnetics; Methionine; Myoglobin; Optical Rotatory Dispersion; Protein Conformation; Pyridines; Spectrophotometry | 1974 |
The effect of cyclic AMP and related compounds on the control of protein synthesis in reticulocyte lysates.
Topics: Animals; Blood Proteins; Carbon Radioisotopes; Cell-Free System; Cyclic AMP; Glutathione; Heme; Kinetics; Leucine; Methionine; Oxidation-Reduction; Penicillium chrysogenum; Peptide Chain Initiation, Translational; Protein Biosynthesis; Purine Nucleotides; Purines; Rabbits; Reticulocytes; RNA; Stimulation, Chemical; Sulfur Radioisotopes | 1974 |
Alkaline isomerization of ferricytochrome c: identification of the lysine ligand.
Topics: Animals; Cytochrome c Group; Guanidines; Heme; Horses; Hydrogen-Ion Concentration; In Vitro Techniques; Iron; Ligands; Lysine; Methionine; Myocardium; Spectrophotometry, Ultraviolet | 1974 |
Haem ligands of the ferricytochrome c of Ustilago sphaerogena.
Topics: Acetates; Alkylation; Amino Acid Sequence; Basidiomycota; Bromine; Carboxylic Acids; Cytochrome c Group; Cytochrome Reductases; Electron Transport Complex IV; Heme; Histidine; Imidazoles; Iron; Kinetics; Ligands; Methionine; Methylation; Molecular Conformation; Spectrophotometry | 1974 |
Kinetics of carbon monoxide binding and electron transfer by cytochrome c polymers.
Topics: Animals; Binding Sites; Carbon Monoxide; Chromatography, Gel; Cytochrome c Group; Electron Transport; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Methionine; Methylation; Models, Biological; Myocardium; Photochemistry; Photolysis; Spectrophotometry; Sulfites | 1974 |
Control of protein synthesis in reticulocyte lysates by haemin.
Topics: Animals; Blood Proteins; Cell-Free System; Heme; Methionine; Peptide Chain Initiation, Translational; Protein Binding; Protein Biosynthesis; Rabbits; Reticulocytes; RNA, Ribosomal; RNA, Transfer; Sulfur Isotopes | 1973 |
Biosynthesis of reticulocyte membrane proteins by membrane-free polyribosomes.
Topics: Acetates; Anemia; Animals; Autoradiography; Blood Proteins; Cell Membrane; Cell-Free System; Electrophoresis, Polyacrylamide Gel; Heme; Hydrogen-Ion Concentration; Iontophoresis; Methionine; Methods; Molecular Weight; Peptides; Polyribosomes; Rabbits; Reticulocytes; Sodium Dodecyl Sulfate; Sulfur Isotopes; Trypsin | 1973 |
Met-tRNAfMet binding to 40S ribosomal subunits: a site for the regulation of initiation of protein synthesis by hemin.
Topics: Animals; Blood Proteins; Carbon Radioisotopes; Centrifugation, Density Gradient; Chromatography, DEAE-Cellulose; Chromatography, Ion Exchange; Globins; Heme; Hemin; Leucine; Methionine; Molecular Weight; Peptide Chain Initiation, Translational; Protein Binding; Protein Biosynthesis; Rabbits; Rats; Reticulocytes; Ribosomes; RNA, Transfer; Sulfur Radioisotopes | 1974 |
Translational repression in the control of globin chain initiation by hemin.
Topics: Animals; Carbon Radioisotopes; Centrifugation, Density Gradient; Codon; Cycloheximide; Globins; Heme; Hemin; Kinetics; Leucine; Methionine; Peptide Chain Initiation, Translational; Protein Biosynthesis; Rabbits; Reticulocytes; Ribose; Ribosomes; RNA, Messenger; RNA, Transfer; Spectrophotometry, Ultraviolet; Sulfur Radioisotopes; Temperature; Time Factors | 1974 |
Iron ligands in different forms of ferricytochrome c: the 620-nm band as a probe.
Topics: 1-Propanol; Animals; Chromatography, Gel; Cytochromes; Ethanol; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Mathematics; Methionine; Myocardium; Osmolar Concentration; Pepsin A; Peptides; Protein Binding; Protein Conformation; Protein Denaturation; Spectrophotometry; Temperature; Thermodynamics; Trypsin; Urea; Water | 1972 |
Regulation of synthesis of non-globin proteins in cell-free extracts of rabbit reticulocytes.
Topics: Animals; Anti-Bacterial Agents; Autoradiography; Blood Proteins; Carbon Isotopes; Cell-Free System; Electrophoresis, Polyacrylamide Gel; Genetic Code; Globins; Heme; Hemolysis; Leucine; Methionine; Molecular Weight; Peptide Chain Elongation, Translational; Protein Biosynthesis; Rabbits; Reoviridae; Reticulocytes; RNA; RNA, Messenger; RNA, Viral; Sulfur Isotopes | 1973 |
Inhibition of globin chain initiation in reticulocyte lysates by pactamycin: accumulation of methionyl-valine.
Topics: Animals; Antibiotics, Antineoplastic; Carbon Radioisotopes; Centrifugation, Density Gradient; Electrophoresis; Globins; Heme; In Vitro Techniques; Liver; Methionine; Peptide Chain Elongation, Translational; Peptide Chain Initiation, Translational; Polyribosomes; Protein Binding; Puromycin; Rabbits; Reticulocytes; Ribosomes; RNA, Transfer; Sucrose; Sulfur Radioisotopes; Valine | 1973 |
Hemin control of globin synthesis: effect of a translational repressor on Met-tRNAf binding to the small ribosomal subunit and its relation to the activity and alailability of an initiation factor.
Topics: Animals; Cell Fractionation; Centrifugation, Zonal; Chromatography, Ion Exchange; Cycloheximide; Formates; Globins; Heme; Methionine; Peptide Initiation Factors; Potassium Chloride; Protein Biosynthesis; Rabbits; Reticulocytes; Ribosomes; RNA, Transfer; Subcellular Fractions; Sulfur Radioisotopes; Suppression, Genetic | 1973 |
Inhibition of an initiation codon function by hemin deficiency and the hemin-controlled translational repressor in the reticulocyte cell-free system.
Topics: Animals; Anti-Bacterial Agents; Cell-Free System; Centrifugation, Density Gradient; Chromatography, DEAE-Cellulose; Chromatography, Gel; Chromatography, Ion Exchange; Cycloheximide; Genes, Regulator; Heme; Methionine; Oligonucleotides; Oligopeptides; Peptide Chain Initiation, Translational; Peptide Initiation Factors; Peptides; Polyamines; Protein Biosynthesis; Rabbits; Reticulocytes; RNA, Messenger; RNA, Transfer; Spectrophotometry, Ultraviolet; Sulfur Radioisotopes | 1973 |
Structure-function relation in hemoglobin Köln (beta 98 Val leads to Met).
Topics: Carboxyhemoglobin; Diphosphoglyceric Acids; Heme; Hemoglobinometry; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Kinetics; Ligands; Methionine; Molecular Weight; Oxygen; Oxyhemoglobins; Spectrum Analysis; Ultracentrifugation; Valine | 1974 |
Heme-linked properties of Euglena cytochrome f.
Topics: Alkylation; Carbon Monoxide; Cyanides; Cytochromes; Euglena; Heme; Hydrogen-Ion Concentration; Iron; Kinetics; Metalloproteins; Methionine; Molecular Conformation; Osmolar Concentration; Oxidation-Reduction; Spectrophotometry; Temperature; Thermodynamics | 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 |
Probing the topography of proteins in solution by photosensitized oxidation. The heme environment in horse heart ferrocytochrome c.
Topics: Amino Acids; Animals; Chromatography, Gel; Cyanides; Cytochromes; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Light; Methionine; Myocardium; Oxidation-Reduction; Peptides; Photochemistry; Radiation Effects; Tryptophan; Tyrosine | 1971 |
Some aspects of pH and temperature dependence of the NMR spectra of cytochrome C.
Topics: Animals; Chemical Phenomena; Chemistry; Cytochromes; Electron Transport; Heme; Horses; Hydrogen-Ion Concentration; Iron; Lysine; Magnetic Resonance Spectroscopy; Methionine; Oxidation-Reduction; Protons; Temperature; Threonine; Water | 1971 |
Iodine, hemin and heminester as oxidants in a synthesis of ATP from ADP and P i mediated by thiols and disulfides.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Aerobiosis; Animals; Catalysis; Cattle; Chemical Phenomena; Chemistry; Disulfides; Electron Transport; Esters; Heme; Iodine; Methionine; Models, Biological; Oxidation-Reduction; Oxidative Phosphorylation; Oxygen; Phosphates; Quaternary Ammonium Compounds; Sulfhydryl Compounds; Thioglycolates | 1971 |
Reconstitution of horse heart cytochrome c: interaction of the components obtained upon cleavage of the peptide bond following methionine residue 65.
Topics: Animals; Circular Dichroism; Cyanogen Bromide; Cytochromes; Fluorescence; Heme; Horses; Liver; Methionine; Myocardium; Oxidation-Reduction; Oxygen Consumption; Peptides; Rats; Spectrum Analysis; Succinate Dehydrogenase; Ultraviolet Rays | 1971 |
Immunochemistry of sperm whale myoglobin. V. Specific modification of the methionine residues with beta-propiolactone.
Topics: Animals; Antigen-Antibody Reactions; Antigens; Binding Sites; Cetacea; Goats; Heme; Heterocyclic Compounds; Immunochemistry; Lactones; Methionine; Myoglobin; Rabbits; Sulfonic Acids | 1969 |
Heme sulfuric anhydrides. I. Synthesis and reactions of mesoheme sulfuric anhydride.
Topics: Amino Acids; Anhydrides; Chemical Phenomena; Chemistry; Chromatography, Thin Layer; Heme; Histidine; Methionine; Models, Structural; Spectrophotometry; Sulfuric Acids | 1970 |
Heme sulfuric anhydrides. II. Properties of heme models prepared from mesoheme sulfuric anhydrides.
Topics: Anhydrides; Chemical Phenomena; Chemistry; Cytochromes; Dioxins; Heme; Histidine; Imidazoles; Methionine; Models, Chemical; Oxidation-Reduction; Spectrophotometry; Sulfuric Acids | 1970 |
The ability of exogenous heme to restore globin synthesis in reticulocytes with impaired heme formation.
Topics: Amino Acids; Animals; Blood Proteins; Bloodletting; Carbon Isotopes; Cycloheximide; Depression, Chemical; Globins; Glycine; Heme; Hemoglobins; Hydrazines; Isonicotinic Acids; Methionine; Peptide Biosynthesis; Rabbits; Radioisotopes; Reticulocytes; Selenium; Stimulation, Chemical; Time Factors | 1970 |
Polyamino acid derivatives of mammalian cytochrome c undecapeptide.
Topics: Anhydrides; Animals; Chemical Phenomena; Chemistry; Cytochromes; Glycine; Heme; Horses; Hydrogen-Ion Concentration; Iron; Methionine; Myocardium; Oxidation-Reduction; Peptides; Spectrophotometry; Spectrum Analysis; Valine | 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 |
Type c ferri- and ferrohemochrome formation between hemin c, amino acids, and peptides.
Topics: Amino Acids; Ammonia; Arginine; Cytochromes; Detergents; Glycine; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Indoles; Iron; Lysine; Methionine; Peptides; Pigments, Biological; Porphyrins; Protein Binding; Spectrophotometry; Sulfur; Tryptophan | 1968 |
The reversible unfolding of horse heart ferricytochrome c.
Topics: Alkylation; Animals; Chemical Phenomena; Chemistry; Cytochromes; Dialysis; Glycols; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Iron; Methionine; Myocardium; Spectrum Analysis; Tyrosine; Ultracentrifugation; Urea; Viscosity | 1968 |
Modification of methionine in the haem environment of cytochrome c.
Topics: Cytochromes; Heme; Methionine; Spectrum Analysis | 1969 |
Photodynamic action of porphyrins on amino acids and proteins. I. Selective photooxidation of methionine in Aqueous solution.
Topics: Amino Acids; Chemical Phenomena; Chemistry; Chlorophyll; Hematoporphyrins; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Light; Magnesium; Methionine; Micrococcus; Muramidase; Oxidation-Reduction; Porphyrins; Radiation Effects; Spectrophotometry; Time Factors; Tryptophan; Tyrosine; Water | 1969 |
The structural environment of the tryptophanyl residue of horse heart ferricytochrome c.
Topics: Amino Acids; Animals; Cytochromes; Heme; Horses; Hydrogen-Ion Concentration; Methionine; Myocardium; Oxidation-Reduction; Spectrophotometry; Tryptophan; Tyrosine; Viscosity | 1967 |
The spatial structure of the axially bound methionine in solution conformations of horse ferrocytochrome c and Pseudomonas aeruginosa ferrocytochrome c551 by 1H NMR.
Topics: Animals; Bacterial Proteins; Cytochrome c Group; Heme; Horses; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Protein Conformation; Pseudomonas aeruginosa | 1984 |
Different chirality of the axial methionine in homologous cytochromes c determined by 1H NMR and CD sectroscopy.
Topics: Animals; Chemistry, Organic; Circular Dichroism; Computers; Cytochrome c Group; Heme; Horses; Magnetic Resonance Spectroscopy; Methionine; Organic Chemistry Phenomena; Oxidation-Reduction; Protein Conformation; Pseudomonas aeruginosa; Rabbits; Species Specificity | 1980 |
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 |
Kinetic intermediates in the formation of ordered complexes from cytochrome c fragments. Evidence that methionine ligation is a late event in the folding process.
Topics: Animals; Binding Sites; Cytochrome c Group; Heme; Horses; Kinetics; Methionine; Myocardium; Oscillometry; Protein Binding; Protein Conformation | 1980 |
Alkaline isomerization of ferricytochrome c: lysine is not replacing methionine at the sixth co-ordination site of the haem iron.
Topics: Acetylation; Amino Acids; Animals; Binding, Competitive; Cytochrome c Group; Heme; Hydrogen-Ion Concentration; Isomerism; Kinetics; Lysine; Methionine; Phenylalanine; Protein Conformation | 1981 |
Structure and heme environment of ferrocytochrome c553 from 1H NMR studies.
Topics: Cyanobacteria; Cytochrome c Group; Heme; Histidine; Magnetic Resonance Spectroscopy; Methionine; Phenylalanine; Protein Conformation; Tryptophan; Tyrosine | 1982 |
A new spatial structure for the axial methionine observed in cytochrome c5 from Pseudomonas mendocina. Correlations with the electronic structure of heme c.
Topics: Circular Dichroism; Cytochrome c Group; Heme; Iron; Ligands; Magnetic Resonance Spectroscopy; Methionine; Oxidation-Reduction; Protein Conformation; Pseudomonas | 1983 |
Coordination of the heme iron in the low-potential cytochromes c-553 from Desulfovibrio vulgaris and Desulfovibrio desulfuricans. Different chirality of the axially bound methionine in the oxidized and reduced states.
Topics: Binding Sites; Cytochrome c Group; Desulfovibrio; Heme; Iron; Magnetic Resonance Spectroscopy; Methionine; Oxidation-Reduction; Protein Binding; Protein Conformation; Species Specificity | 1983 |
Synthesis of the apoprotein of cytochrome b in heme-deficient yeast cells.
Topics: 5-Aminolevulinate Synthetase; Apoproteins; Cycloheximide; Cytochromes; Heme; Methionine; Mitochondria; Mutation; Peptide Fragments; Saccharomyces cerevisiae; Submitochondrial Particles | 1980 |
Partial purification and characterization of a 90,000-dalton peptide involved in activation of the eIF-2 alpha protein kinase of the hemin-controlled translational repressor.
Topics: Animals; Blood Proteins; Cross Reactions; Eukaryotic Initiation Factor-2; Heme; Humans; Immunoassay; Immunoglobulin G; Kinetics; Methionine; Molecular Weight; Peptide Initiation Factors; Protein Biosynthesis; Protein Kinases; Proteins; Rabbits; Reticulocytes; Ribosomes; RNA, Transfer | 1980 |
Three-dimensional solution structure of the cyanide adduct of a Met80Ala variant of Saccharomyces cerevisiae iso-1-cytochrome c. Identification of ligand-residue interactions in the distal heme cavity.
Topics: Alanine; Amino Acid Sequence; Animals; Crystallography, X-Ray; Cyanides; Cytochrome c Group; Cytochromes c; Heme; Horses; Ligands; Magnetic Resonance Spectroscopy; Methionine; Molecular Sequence Data; Myocardium; Protein Conformation; Protein Structure, Secondary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Solutions | 1995 |
Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli.
Topics: Amino Acid Sequence; Base Sequence; Cytochrome b Group; Cytochromes; Dithionite; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Genotype; Heme; Histidine; Leucine; Ligands; Macromolecular Substances; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; NADPH Oxidases; Oligodeoxyribonucleotides; Oxidation-Reduction; Oxidoreductases; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Restriction Mapping; Spectrophotometry | 1995 |
The haem b558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation.
Topics: Bacterial Proteins; Circular Dichroism; Cytochrome b Group; Cytochromes; Electron Spin Resonance Spectroscopy; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Methionine; NADPH Oxidases; Oxidoreductases; Spectrophotometry, Ultraviolet | 1995 |
An unusual conformation of the methionine haem ligand in cytochrome cL established by two-dimensional 1H-NMR.
Topics: Computer Simulation; Cytochrome c Group; Gram-Negative Aerobic Bacteria; Heme; Ligands; Magnetic Resonance Spectroscopy; Methionine; Methylococcaceae; Models, Molecular; Molecular Conformation | 1994 |
Characterization of mutant Met100Lys of cytochrome c-550 from Thiobacillus versutus with lysine-histidine heme ligation.
Topics: Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Lysine; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Mutation; Spectrophotometry; Structure-Activity Relationship; Thiobacillus | 1994 |
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 |
Spectroscopic characterization of flavocytochrome c-552 from the photosynthetic purple sulfur bacterium Chromatium vinosum.
Topics: Chromatium; Circular Dichroism; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Ethylene Glycol; Ethylene Glycols; Heme; Histidine; Methionine; Spectrophotometry, Infrared; Spectrum Analysis | 1994 |
Structurally engineered cytochromes with unusual ligand-binding properties: expression of Saccharomyces cerevisiae Met-80-->Ala iso-1-cytochrome c.
Topics: Alanine; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cloning, Molecular; Cytochrome c Group; Cytochromes; Cytochromes c; Escherichia coli; Heme; Horses; Methionine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Conformation; Protein Engineering; Recombinant Proteins; Restriction Mapping; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Transcription, Genetic | 1993 |
Fast events in protein folding initiated by nanosecond laser photolysis.
Topics: Amino Acid Sequence; Animals; Binding Sites; Carbon Monoxide; Cytochrome c Group; Guanidine; Guanidines; Heme; Horses; Kinetics; Lasers; Methionine; Photolysis; Protein Conformation; Protein Folding; Protein Structure, Secondary; Spectrophotometry; Time Factors | 1993 |
Pitfalls in assigning heme axial coordination by EPR. c-Type cytochromes with atypical Met-His ligation.
Topics: Bacterial Proteins; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Histidine; Magnetic Resonance Spectroscopy; Methionine; Spectrum Analysis | 1993 |
Cytochrome c6 from Monoraphidium braunii. A cytochrome with an unusual heme axial coordination.
Topics: Amino Acid Sequence; Chlorophyta; Cytochromes; Cytochromes f; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen-Ion Concentration; Isoelectric Point; Methionine; Molecular Sequence Data; Molecular Weight; Oxidation-Reduction; Sequence Alignment; Spectrophotometry, Ultraviolet; Spectroscopy, Mossbauer; Surface-Active Agents | 1993 |
Substitution of a haem-iron axial ligand in flavocytochrome b2.
Topics: Base Sequence; Cytochromes b5; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Histidine; Iron; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Methionine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Spectrum Analysis | 1993 |
Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding.
Topics: Cytochrome c Group; Diffusion; Guanidine; Guanidines; Heme; Kinetics; Ligands; Methionine; Models, Structural; Peroxidases; Protein Conformation; Protein Denaturation; Protein Folding; Spectrophotometry; Time Factors | 1996 |
Bis-methionine ligation to heme iron in mutants of cytochrome b562. 1. Spectroscopic and electrochemical characterization of the electronic properties.
Topics: Bacterial Proteins; Circular Dichroism; Cloning, Molecular; Cytochrome b Group; Electrochemistry; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli; Escherichia coli Proteins; Ferritins; Heme; Hydrogen-Ion Concentration; Iron; Ligands; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Recombinant Proteins; Spectrophotometry | 1996 |
Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions.
Topics: Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Ferric Compounds; Ferrous Compounds; Heme; Hydrogen-Ion Concentration; Iron; Ligands; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Mutation; Oxidation-Reduction; Protein Conformation; Temperature | 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 |
Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles.
Topics: Animals; Binding Sites; Circular Dichroism; Cytochrome c Group; Heme; Horses; Kinetics; Liposomes; Methionine; Microscopy, Fluorescence; Models, Chemical; Phosphatidylserines; Protein Conformation; Protein Denaturation; Spectrophotometry | 1997 |
The Soret circular dichroism spectrum as a probe for the heme Fe(III)-Met(80) axial bond in horse cytochrome c.
Topics: Animals; Circular Dichroism; Cytochrome c Group; Ferric Compounds; Heme; Horses; Methionine; Protein Conformation; Protein Denaturation | 1997 |
Evidence for an unfolding and refolding pathway in cytochrome c.
Topics: Animals; Binding Sites; Cytochrome c Group; Heme; Horses; Hydrogen; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Protein Folding; Thermodynamics | 1998 |
Conversion of mitochondrial cytochrome b5 into a species capable of performing the efficient coupled oxidation of heme.
Topics: Cytochromes b5; Electrochemistry; Electron Spin Resonance Spectroscopy; Heme; Heme Oxygenase (Decyclizing); Histidine; Magnetic Resonance Spectroscopy; Mass Spectrometry; Methionine; Mitochondria; Mutagenesis, Site-Directed; NADP; Oxidation-Reduction | 1998 |
Single electron reduction of cytochrome c oxidase compound F: resolution of partial steps by transient spectroscopy.
Topics: 2,2'-Dipyridyl; Animals; Cattle; Coordination Complexes; Electron Transport; Electron Transport Complex IV; Heme; Indicators and Reagents; Kinetics; Lysine; Methionine; Oxidation-Reduction; Photolysis; Proton Pumps; Rhodobacter sphaeroides; Spectrophotometry | 1998 |
Yeast iso-1-cytochrome c met80X mutants: the pKa of the spin state transition as a probe for haem pocket flexibility.
Topics: Cytochrome c Group; Cytochromes c; Heme; Hydrogen-Ion Concentration; Methionine; Molecular Probes; Mutation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins | 1998 |
Substitution of the sixth axial ligand of Rhodobacter capsulatus cytochrome c1 heme yields novel cytochrome c1 variants with unusual properties.
Topics: Amino Acid Substitution; Binding Sites; Cytochromes c1; Electron Transport Complex III; Heme; Histidine; Ligands; Lysine; Methionine; Mutagenesis, Site-Directed; NADH Dehydrogenase; Oxidation-Reduction; Rhodobacter capsulatus; Spectrophotometry | 1999 |
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 |
Cytochrome cM from synechocystis 6803. Detection in cells, expression in Escherichia coli, purification and physical characterization.
Topics: Amino Acid Sequence; Bacterial Proteins; Blotting, Western; Cyanobacteria; Cytochrome c Group; Escherichia coli; Heme; Histidine; Isoelectric Point; Methionine; Molecular Weight; Oxidation-Reduction; Recombinant Fusion Proteins; Sequence Deletion; Solubility; Spectrum Analysis; Titrimetry | 2000 |
Cytochrome cd(1) from Paracoccus pantotrophus exhibits kinetically gated, conformationally dependent, highly cooperative two-electron redox behavior.
Topics: Allosteric Regulation; Allosteric Site; Apoenzymes; Cytochrome c Group; Cytochromes; Dimerization; Electrons; Heme; Histidine; Holoenzymes; Kinetics; Ligands; Methionine; Nitrite Reductases; Oxidation-Reduction; Paracoccus; Protein Conformation; Spectrum Analysis; Temperature; Titrimetry | 2000 |
Obtaining ligand geometries from paramagnetic shifts in low-spin haem proteins.
Topics: Cyanides; Heme; Hemeproteins; Histidine; Ligands; Methionine; Models, Theoretical; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation | 2000 |
Haem-linked interactions in horseradish peroxidase revealed by spectroscopic analysis of the Phe-221-->Met mutant.
Topics: Arabidopsis; Catalysis; Heme; Horseradish Peroxidase; Hydrogen-Ion Concentration; Hydroxamic Acids; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Phenylalanine; Plasmids; Spectrum Analysis, Raman | 2001 |
Rate of intrachain contact formation in an unfolded protein: temperature and denaturant effects.
Topics: Animals; Binding Sites; Cytochrome c Group; Diffusion; Dose-Response Relationship, Drug; Guanidine; Heme; Horses; Kinetics; Ligands; Methionine; Protein Conformation; Protein Denaturation; Protein Folding; Solvents; Temperature; Thermodynamics | 2001 |
Electron and proton transfer in the arginine-54-methionine mutant of cytochrome c oxidase from Paracoccus denitrificans.
Topics: Arginine; Biological Transport; Copper; Electron Transport; Electron Transport Complex IV; Heme; Kinetics; Membrane Potentials; Methionine; Mutagenesis, Site-Directed; Oxygen; Paracoccus denitrificans; Phospholipids; Photolysis; Protons; Spectrophotometry | 2001 |
Site-directed mutagenesis of the heme axial ligands in the hemoflavoenzyme cellobiose dehydrogenase.
Topics: Amino Acid Substitution; Carbohydrate Dehydrogenases; Catalysis; Cellulose; Heme; Histidine; Ligands; Methionine; Molecular Weight; Mutagenesis, Site-Directed; Phanerochaete | 2001 |
Controlling the functionality of cytochrome c(1) redox potentials in the Rhodobacter capsulatus bc(1) complex through disulfide anchoring of a loop and a beta-branched amino acid near the heme-ligating methionine.
Topics: Amino Acid Sequence; Binding Sites; Cytochromes c1; Disulfides; Electron Transport; Electron Transport Complex III; Electrophoresis, Polyacrylamide Gel; Factor Xa; Heme; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Plasmids; Protein Folding; Rhodobacter capsulatus; Sequence Homology, Amino Acid | 2001 |
Replacement of the methionine axial ligand in cytochrome c(550) by a lysine: effects on the haem electronic structure.
Topics: Amino Acid Substitution; Cyanides; Cytochrome c Group; Heme; Ligands; Lysine; Methionine; Mutation; Nuclear Magnetic Resonance, Biomolecular; Paracoccus | 2002 |
Mutants of the CuA site in cytochrome c oxidase of Rhodobacter sphaeroides: I. Spectral and functional properties.
Topics: Amino Acid Substitution; Asparagine; Cell Membrane; Copper; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Glycine; Heme; Histidine; Iron; Kinetics; Leucine; Manganese; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Structure, Secondary; Proton Pumps; Rhodobacter sphaeroides; Spectrometry, Fluorescence; Spectrophotometry; Spectroscopy, Fourier Transform Infrared | 2002 |
Chemical shift-based constraints for solution structure determination of paramagnetic low-spin heme proteins with bis-His and His-CN axial ligands: the cases of oxidized cytochrome b(5) and Met80Ala cyano-cytochrome c.
Topics: Alanine; Cyanides; Cytochrome c Group; Cytochromes b5; Heme; Histidine; Ligands; Methionine; Models, Molecular; Molecular Structure; Mutation; Oxidation-Reduction; Yeasts | 2002 |
Probing electrostatic interactions in cytochrome c using site-directed chemical modification.
Topics: Alkylation; Animals; Binding Sites; Chromatography, High Pressure Liquid; Cytochrome c Group; Electron Transport Complex IV; Heme; Hydrogen-Ion Concentration; Methionine; Models, Molecular; Oxidation-Reduction; Oxidoreductases; Protein Binding; Protein Conformation; Rats; Saccharomyces cerevisiae; Static Electricity; Sulfonium Compounds; Thermodynamics | 2002 |
Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli.
Topics: Carbon Monoxide; Carrier Proteins; Cloning, Molecular; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Methionine; Mutation; Oxygen; Phosphoric Diester Hydrolases; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Spectrum Analysis, Raman; Time Factors | 2002 |
The unfolding of oxidized c-type cytochromes: the instructive case of Bacillus pasteurii.
Topics: Bacillus; Cytochrome c Group; Guanidine; Heme; Hydrogen-Ion Concentration; Iron; Ligands; Magnetic Resonance Spectroscopy; Methionine; Mitochondria; Models, Molecular; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Protein Folding; Spectrum Analysis; Thermodynamics | 2002 |
Influence of amino acid side chain packing on Fe-methionine coordination in thermostable cytochrome C.
Topics: Bacterial Proteins; Binding Sites; Cytochrome c Group; Gram-Negative Chemolithotrophic Bacteria; Heme; Hot Temperature; Iron; Methionine; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Pseudomonas aeruginosa | 2002 |
Unusual cyanide bindings to a heme-regulated phosphodiesterase from Escherichia coli: effect of Met95 mutations.
Topics: Azides; Cyanides; Escherichia coli; Fluorides; Heme; Imidazoles; Iron; Kinetics; Methionine; Mutagenesis, Site-Directed; Mutation; Phosphoric Diester Hydrolases; Protein Binding; Protein Structure, Tertiary; Spectrophotometry | 2002 |
NMR study of the conformational transition of cytochrome c upon the displacement of Met80 by exogenous ligand: structural and magnetic characterization of azidoferricytochrome c.
Topics: Animals; Azides; Cytochrome c Group; Heme; Horses; Ligands; Magnetic Resonance Spectroscopy; Methionine; Models, Chemical; Models, Molecular; Myocardium; Protein Folding; Protein Structure, Secondary | 2003 |
ORGANIC REQUIREMENTS AND SYNTHETIC MEDIA FOR GROWTH OF THE MYXOMYCETE PHYSARUM POLYCEPHALUM.
Topics: Biotin; Culture Media; Glycine; Heme; Methionine; Myxomycetes; Physarum polycephalum; Research; Thiamine | 1963 |
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 |
Radiation-induced enhancement of nitrite reducing activity of cytochrome c.
Topics: Circular Dichroism; Cytochromes c; Drug Stability; Gamma Rays; Heme; Methionine; Nitrite Reductases; Nitrites; Oxidation-Reduction; Protein Folding | 2003 |
Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina.
Topics: Alanine; Crystallization; Crystallography, X-Ray; Cytochrome c Group; Deuterium Oxide; Electron Transport; Flavin-Adenine Dinucleotide; Heme; Histidine; Kinetics; Ligands; Methionine; Molecular Weight; Mutagenesis, Site-Directed; Potentiometry; Shewanella; Solubility; Solvents; Succinate Dehydrogenase | 2003 |
Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli. Kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met-95 mutants.
Topics: Carbon Monoxide; Carrier Proteins; Catalysis; Cloning, Molecular; Escherichia coli; Escherichia coli Proteins; Heme; Kinetics; Light; Methionine; Mutation; Oxidation-Reduction; Oxygen; Phosphoric Diester Hydrolases; Protein Structure, Tertiary; Spectrophotometry; Spectroscopy, Fourier Transform Infrared; Time Factors | 2004 |
Characterization of Met95 mutants of a heme-regulated phosphodiesterase from Escherichia coli. Optical absorption, magnetic circular dichroism, circular dichroism, and redox potentials.
Topics: 3',5'-Cyclic-AMP Phosphodiesterases; Catalysis; Circular Dichroism; Escherichia coli; Heme; Methionine; Oxidation-Reduction; Phosphoric Diester Hydrolases; Point Mutation; Spectrum Analysis | 2003 |
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 |
A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide.
Topics: Animals; Binding Sites; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Stability; Ferric Compounds; Glycine; Heme; Hemeproteins; Histidine; Horses; Imidazoles; Iron; Ligands; Mercaptoethanol; Methionine; Peptide Fragments; Peptides; Protein Structure, Secondary; Spectrum Analysis, Raman; Structure-Activity Relationship | 2004 |
A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor.
Topics: Amino Acid Sequence; Carrier Proteins; Catalysis; Crystallography, X-Ray; Cyclic AMP; Dimerization; Escherichia coli; Escherichia coli Proteins; Heme; Hydrogen Bonding; Iron; Ligands; Methionine; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Phosphoric Diester Hydrolases; Protein Folding; Protein Structure, Tertiary; Sequence Homology, Amino Acid | 2004 |
Proton uptake upon anaerobic reduction of the Paracoccus denitrificans cytochrome c oxidase: a kinetic investigation of the K354M and D124N mutants.
Topics: Amino Acid Substitution; Anaerobiosis; Asparagine; Aspartic Acid; Calibration; Electron Transport Complex IV; Heme; Lysine; Methionine; Oxidation-Reduction; Paracoccus denitrificans; Phenolsulfonphthalein; Protein Subunits; Protons; Spectrophotometry | 2004 |
Heme axial methionine fluxionality in Hydrogenobacter thermophilus cytochrome c552.
Topics: Bacteria; Bacterial Proteins; Biophysical Phenomena; Biophysics; Cytochrome c Group; Heme; Ligands; Magnetics; Methionine; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular | 2004 |
Design and synthesis of de novo cytochromes c.
Topics: Amino Acid Sequence; Animals; Cattle; Cytochromes b; Cytochromes c; Genes, Synthetic; Helix-Loop-Helix Motifs; Heme; Histidine; Methionine; Molecular Sequence Data; Oxidation-Reduction; Peptides; Protein Binding; Protein Engineering; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Sulfides | 2004 |
Human heme oxygenase oxidation of 5- and 15-phenylhemes.
Topics: Animals; Ascorbic Acid; Benzoic Acid; Biliverdine; Carbon Monoxide; Chromatography, High Pressure Liquid; Chromatography, Liquid; Crystallography, X-Ray; Electrons; Esters; Heme; Heme Oxygenase (Decyclizing); Horses; Humans; Ions; Lysine; Mass Spectrometry; Methionine; Models, Chemical; Models, Molecular; Myoglobin; NADPH-Ferrihemoprotein Reductase; Oxidoreductases Acting on CH-CH Group Donors; Oxygen; Spectrophotometry; Stereoisomerism; Time Factors; Ultraviolet Rays | 2004 |
Cytochrome c550 in the cyanobacterium Thermosynechococcus elongatus: study of redox mutants.
Topics: Calcium; Chlorine; Cloning, Molecular; Cyanobacteria; Cysteine; Cytochrome c Group; DNA; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hot Temperature; Ligands; Methionine; Models, Genetic; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Oxygen; Plasmids; Point Mutation; Polymerase Chain Reaction; Synechocystis; Temperature; Thylakoids; Time Factors | 2004 |
Hydroxyl radical oxidation of cytochrome c by aerobic radiolysis.
Topics: Aerobiosis; Amino Acid Sequence; Animals; Cytochromes c; Dose-Response Relationship, Radiation; Electrons; Heme; Horses; Hydroxyl Radical; Hydroxylation; Intracellular Membranes; Methionine; Mitochondria, Heart; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Peptide Fragments; Phenylalanine; Protein Conformation; Pulse Radiolysis; Rats; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrophotometry, Ultraviolet; Tyrosine | 2004 |
The 40s Omega-loop plays a critical role in the stability and the alkaline conformational transition of cytochrome c.
Topics: Catalysis; Circular Dichroism; Cytochrome c Group; Electrochemistry; Enzyme Stability; Heme; Hydrogen-Ion Concentration; Iron; Lysine; Methionine; Oxidation-Reduction; Peptide Fragments; Protein Conformation; Protein Denaturation; Protein Folding; Spectrum Analysis, Raman | 2004 |
Photodissociation of heme distal methionine in ferrous cytochrome C revealed by subpicosecond time-resolved resonance Raman spectroscopy.
Topics: Cytochromes c; Heme; Kinetics; Methionine; Photochemistry; Spectrum Analysis, Raman | 2004 |
In situ effects of mutations of the extrinsic cytochrome c550 of photosystem II in Synechocystis sp. PCC6803.
Topics: Amino Acid Substitution; Calcium; Cytochrome c Group; Fluorometry; Heme; Histidine; Ligands; Methionine; Mutagenesis, Site-Directed; Oxygen; Photolysis; Photosystem II Protein Complex; Polarography; Synechocystis; Thylakoids | 2004 |
A proteomic analysis of thioacetamide-induced hepatotoxicity and cirrhosis in rat livers.
Topics: Animals; Down-Regulation; Fatty Acids; Ferritins; Fibrosis; Glutathione; Heme; Humans; Image Processing, Computer-Assisted; Iron; Lipid Peroxidation; Liver; Liver Cirrhosis; Methionine; Oxidative Stress; Oxygenases; Proteomics; Rats; Rats, Wistar; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Thioacetamide; Time Factors; Trypsin; Up-Regulation | 2004 |
Autocatalytic formation of green heme: evidence for H2O2-dependent formation of a covalent methionine-heme linkage in ascorbate peroxidase.
Topics: Amino Acid Sequence; Ascorbate Peroxidases; Catalysis; Heme; Hydrogen Peroxide; Kinetics; Methionine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Peroxidases; Pisum sativum; Plant Proteins; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrophotometry, Ultraviolet | 2004 |
Suppression of axial methionine fluxion in Hydrogenobacter thermophilus Gln64Asn cytochrome c552.
Topics: Amino Acid Substitution; Bacteria; Base Sequence; Cytochrome c Group; DNA, Bacterial; Electrochemistry; Genes, Bacterial; Heme; Methionine; Models, Molecular; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Recombinant Proteins | 2005 |
The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalase; Catalysis; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Crystallography, X-Ray; Heme; Hydrogen Peroxide; Kinetics; Mass Spectrometry; Methionine; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mycobacterium tuberculosis; Peptides; Peracetic Acid; Plasmids; Protein Binding; Recombinant Proteins; Spectrophotometry; Time Factors; Trypsin; Tryptophan; Tyrosine; Ultraviolet Rays | 2005 |
Role of the covalent glutamic acid 242-heme linkage in the formation and reactivity of redox intermediates of human myeloperoxidase.
Topics: Animals; Aspartic Acid; Binding Sites; Bromides; Chlorides; CHO Cells; Circular Dichroism; Cricetinae; Cyanides; Enzyme Stability; Eosinophil Peroxidase; Ferric Compounds; Glutamic Acid; Glutamine; Heme; Humans; Methionine; Oxidation-Reduction; Peroxidase; Recombinant Proteins | 2005 |
The effect of replacing the axial methionine ligand with a lysine residue in cytochrome c-550 from Paracoccus versutus assessed by X-ray crystallography and unfolding.
Topics: Bacterial Proteins; Crystallography, X-Ray; Cytochrome c Group; Enzyme Stability; Heme; Ligands; Lysine; Methionine; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Paracoccus; Peroxidases; Protein Denaturation; Protein Structure, Tertiary; Temperature | 2005 |
Heme axial methionine fluxion in Pseudomonas aeruginosa Asn64Gln cytochrome c551.
Topics: Bacterial Proteins; Cytochrome c Group; Heme; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Molecular Conformation; Mutagenesis, Site-Directed; Pseudomonas aeruginosa; Spectrophotometry, Ultraviolet | 2005 |
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 |
Redox interaction of cytochrome c3 with [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F.
Topics: Binding Sites; Cytochrome c Group; Desulfovibrio vulgaris; Heme; Hydrogenase; Kinetics; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Oxidation-Reduction | 2006 |
Probing the unusual oxidation/reduction behavior of Paracoccus pantotrophus cytochrome cd1 nitrite reductase by replacing a switchable methionine heme iron ligand with histidine.
Topics: Amino Acid Sequence; Cytochromes; Heme; Histidine; Iron; Ligands; Methionine; Nitrite Reductases; Oxidation-Reduction; Paracoccus pantotrophus | 2006 |
Cardiolipin activates cytochrome c peroxidase activity since it facilitates H(2)O(2) access to heme.
Topics: Animals; Binding Sites; Cardiolipins; Cytochrome-c Peroxidase; Enzyme Activation; Ferrous Compounds; Heme; Hydrogen Peroxide; Iron; Liposomes; Methionine; Oxidation-Reduction | 2006 |
Heme biosynthesis in Methanosarcina barkeri via a pathway involving two methylation reactions.
Topics: Archaeal Proteins; Culture Media; Heme; Methanosarcina barkeri; Methionine; Methylation; Uroporphyrinogens; Uroporphyrins | 2006 |
Heme crevice disorder after sixth ligand displacement in the cytochrome c-551 family.
Topics: Bacterial Proteins; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Hydrogen-Ion Concentration; Ligands; Methionine; Nitrosomonas; Nuclear Magnetic Resonance, Biomolecular; Potassium Cyanide; Protein Conformation; Protein Isoforms; Pseudomonas | 2007 |
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 |
Critical role of the heme axial ligand, Met95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward Cyclic diGMP.
Topics: 3',5'-Cyclic-AMP Phosphodiesterases; Carbon Monoxide; Catalysis; Cyclic GMP; Escherichia coli; Heme; Iron; Ligands; Methionine; Models, Molecular; Nitric Oxide; Oxygen; Phosphoric Diester Hydrolases; Protein Binding; Protein Conformation | 2007 |
Modulation of heme redox potential in the cytochrome c6 family.
Topics: Amino Acid Sequence; Crystallography, X-Ray; Cyanobacteria; Cytochromes c6; Electrochemistry; Electron Transport; Glutamine; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Ligands; Methionine; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Valine | 2007 |
Bis-methionine ligation to heme iron in the streptococcal cell surface protein Shp facilitates rapid hemin transfer to HtsA of the HtsABC transporter.
Topics: Alanine; Amino Acid Substitution; ATP-Binding Cassette Transporters; Binding Sites; Electron Spin Resonance Spectroscopy; Heme; Hemin; Hydrogen-Ion Concentration; Kinetics; Membrane Proteins; Methionine; Models, Biological; Models, Molecular; Protein Binding; Protein Structure, Tertiary; Streptococcus pyogenes | 2007 |
Novel haem co-ordination variants of flavocytochrome P450BM3.
Topics: Bacterial Proteins; Circular Dichroism; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Fatty Acids; Glutamine; Heme; Kinetics; Methionine; Mutagenesis, Site-Directed; Mutation; NADPH-Ferrihemoprotein Reductase; Protein Binding; Thermodynamics | 2009 |
Ligand binding to the Fe(III)-protoporphyrin IX complex of phosphodiesterase from Escherichia coli (Ec DOS) markedly enhances catalysis of cyclic di-GMP: roles of Met95, Arg97, and Phe113 of the putative heme distal side in catalytic regulation and ligand
Topics: Animals; Arginine; Catalysis; Cattle; Cyclic GMP; Escherichia coli Proteins; Ferric Compounds; Heme; Ligands; Methionine; Mutagenesis, Site-Directed; Phenylalanine; Phosphoric Diester Hydrolases; Protein Binding; Protein Structure, Tertiary; Protoporphyrins | 2008 |
Probing the heme-binding site of the cytochrome c maturation protein CcmE.
Topics: Amino Acid Substitution; Apoproteins; Bacterial Outer Membrane Proteins; Binding Sites; Cytochromes c; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Heme; Hemeproteins; Ligands; Magnetic Resonance Spectroscopy; Methionine; Mutant Proteins; Mutation; Oxidation-Reduction; Potentiometry; Protein Structure, Secondary; Tyrosine | 2009 |
NirJ, a radical SAM family member of the d1 heme biogenesis cluster.
Topics: Heme; Methionine | 2010 |
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 |
Cytochrome c-554 from Methylosinus trichosporium OB3b; a protein that belongs to the cytochrome c2 family and exhibits a HALS-Type EPR signal.
Topics: Absorption; Amino Acid Sequence; Animals; Anisotropy; Bacterial Proteins; Circular Dichroism; Cytochrome b Group; Cytochrome c Group; Cytochromes c2; Electron Spin Resonance Spectroscopy; Heme; Horses; Mass Spectrometry; Methionine; Methylococcus capsulatus; Methylosinus trichosporium; Molecular Sequence Data; Molecular Weight; Spin Labels; Structural Homology, Protein | 2011 |
Perturbation of the redox site structure of cytochrome c variants upon tyrosine nitration.
Topics: Cytochromes c; Fatty Acids; Heme; Humans; Iron; Kinetics; Lysine; Methionine; Mutation; Nitro Compounds; Oxidation-Reduction; Phenylalanine; Protein Stability; Protein Structure, Quaternary; Recombinant Proteins; Silver Compounds; Static Electricity; Sulfhydryl Compounds; Tyrosine; Water | 2012 |
Role of Met(58) in the regulation of electron/proton transfer in trihaem cytochrome PpcA from Geobacter sulfurreducens.
Topics: Bacterial Proteins; Cytochromes c; Electron Transport; Escherichia coli; Geobacter; Heme; Hydrogen-Ion Concentration; Lysine; Magnetic Resonance Spectroscopy; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Solutions; Thermodynamics | 2012 |
Oxidative damage in MauG: implications for the control of high-valent iron species and radical propagation pathways.
Topics: Amino Acid Motifs; Bacterial Proteins; Heme; Iron; Kinetics; Methionine; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans | 2013 |
Post-translational transformation of methionine to aspartate is catalyzed by heme iron and driven by peroxide: a novel subunit-specific mechanism in hemoglobin.
Topics: Adult; Amino Acid Sequence; Amino Acid Substitution; Aspartic Acid; Crystallography, X-Ray; Fetal Hemoglobin; Heme; Hemoglobin A; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen Peroxide; Iron; Methionine; Models, Molecular; Molecular Sequence Data; Mutation, Missense; Oxidation-Reduction; Protein Processing, Post-Translational; Protein Subunits; Proteomics; Static Electricity | 2014 |
Self-oxidation of cytochrome c at methionine80 with molecular oxygen induced by cleavage of the Met-heme iron bond.
Topics: Cytochromes c; Dithiothreitol; Heme; Humans; Iron; Liposomes; Methionine; Oxidation-Reduction; Oxygen; Protein Conformation; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | 2014 |
Methionine ligand lability of homologous monoheme cytochromes c.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins; Cytochromes c; Electrochemical Techniques; Electrodes; Escherichia coli; Gene Expression; Heme; Histidine; Kinetics; Ligands; Methionine; Molecular Sequence Data; Nitrosomonas europaea; Oxidation-Reduction; Protein Folding; Pseudomonas aeruginosa; Recombinant Proteins; Sequence Alignment; Shewanella; Temperature; Thermodynamics | 2015 |
Inactivation of myeloperoxidase by benzoic acid hydrazide.
Topics: Amino Acid Sequence; Aniline Compounds; Animals; Benzoic Acid; Carbocyanines; Catalytic Domain; Cattle; Electrons; Enzyme Inhibitors; Fluorescent Dyes; Free Radicals; Glutamic Acid; Heme; Humans; Hydrogen Peroxide; Inflammation; Lysine; Mass Spectrometry; Methionine; Molecular Conformation; Molecular Sequence Data; Neutrophils; Oxygen; Peroxidase; Spectrometry, Fluorescence | 2015 |
Density Functional Theory Insights into the Role of the Methionine-Tyrosine-Tryptophan Adduct Radical in the KatG Catalase Reaction: O2 Release from the Oxyheme Intermediate.
Topics: Bacterial Proteins; Carbon; Catalase; Catalysis; Electrons; Heme; Hydrogen; Hydrogen Bonding; Methionine; Models, Chemical; Mycobacterium tuberculosis; Nitrogen; Oxygen; Quantum Theory; Tryptophan; Tyrosine | 2015 |
S-Adenosyl-l-methionine Modulates CO and NO• Binding to the Human H2S-generating Enzyme Cystathionine β-Synthase.
Topics: Carbon Monoxide; Cystathionine beta-Synthase; Heme; Humans; Kinetics; Methionine; Nitric Oxide; Oxidation-Reduction; S-Adenosylmethionine | 2016 |
Met(104) is the CO-replaceable ligand at Fe(II) heme in the CO-sensing transcription factor BxRcoM-1.
Topics: Burkholderia; Carbon Monoxide; Ferrous Compounds; Heme; Ligands; Methionine; Transcription Factors | 2016 |
Conformational status of cytochrome c upon N-homocysteinylation: Implications to cytochrome c release.
Topics: Animals; Apoptosis; Cardiolipins; Cattle; Circular Dichroism; Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Homocysteine; Iron; Ligands; Methionine; Myocardium; Oxygen; Peroxidase; Peroxidases; Protein Conformation; Protein Processing, Post-Translational; Spectrophotometry, Ultraviolet | 2017 |
The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket.
Topics: Alanine; Circular Dichroism; Cytochromes c; Heme; Histamine; Humans; Kinetics; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Binding; Recombinant Proteins; Structure-Activity Relationship; Tyrosine | 2017 |
Effect of methionine80 heme coordination on domain swapping of cytochrome c.
Topics: Calorimetry; Cytochromes c; Heme; Humans; Kinetics; Methionine | 2017 |
Theory Uncovers the Role of the Methionine-Tyrosine-Tryptophan Radical Adduct in the Catalase Reaction of KatGs: O
Topics: Catalase; Catalytic Domain; Electron Transport; Free Radicals; Heme; Histidine; Methionine; Molecular Dynamics Simulation; Oxidation-Reduction; Oxygen; Peroxidases; Protein Conformation; Protons; Tryptophan; Tyrosine | 2018 |
Charge Transfer and π to π* Transitions in the Visible Spectra of Sulfheme Met Isomeric Structures.
Topics: Heme; Hemoglobins; Isomerism; Methionine; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Quantum Theory; Spectrophotometry | 2018 |
Ligation and Reactivity of Methionine-Oxidized Cytochrome c.
Topics: Amino Acid Sequence; Binding Sites; Cytochromes c; Electron Spin Resonance Spectroscopy; Heme; Imidazoles; Iron; Ligands; Methionine; Models, Biological; Oxidation-Reduction; Spectrum Analysis, Raman; Sulfoxides; Yeasts | 2018 |
The proportion of Met80-sulfoxide dictates peroxidase activity of human cytochrome c.
Topics: Apoptosis; Cardiolipins; Cytochrome-c Peroxidase; Enzyme Activation; Glycine; Heme; Humans; Hydrogen Peroxide; Hydrogen-Ion Concentration; Iron; Kinetics; Methionine; Mutation; Safrole; Sulfones | 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 |
Neuroglobin is capable of self-oxidation of methionine64 introduced at the heme axial position.
Topics: Coordination Complexes; Escherichia coli; Heme; Humans; Iron; Ligands; Methionine; Molecular Conformation; Mutation; Neuroglobin; Oxidation-Reduction; Oxygen; Protein Binding; Sulfones | 2018 |
Comparison of the Size and Properties of the Cytochrome c/Cardiolipin Nanospheres in a Sediment and Non-polar Medium.
Topics: Animals; Apoptosis; Cardiolipins; Crystallization; Cytochromes c; Dynamic Light Scattering; Fluorescence Resonance Energy Transfer; Heme; Horses; Hydrogen Bonding; Hydrogen-Ion Concentration; Lipid Bilayers; Lipid Peroxidation; Methanol; Methionine; Mitochondria, Heart; Mitochondrial Membranes; Nanospheres; Protein Conformation; Protein Unfolding | 2019 |
A Heme Propionate Staples the Structure of Cytochrome
Topics: Coordination Complexes; Cytochromes c; Heme; Humans; Hydrogen-Ion Concentration; Iron; Kinetics; Ligands; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Propionates | 2019 |
Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c.
Topics: Cytochromes c; Electron Transport; Ferrous Compounds; Heme; Iron; Metals; Methionine; Molecular Dynamics Simulation; Photolysis; Spectrometry, X-Ray Emission | 2021 |
Dysregulation of homocysteine homeostasis in acute intermittent porphyria patients receiving heme arginate or givosiran.
Topics: Acetylgalactosamine; Adult; Arginine; Cystathionine beta-Synthase; Female; Folic Acid; Heme; Homeostasis; Homocysteine; Homocystinuria; Humans; Hydroxymethylbilane Synthase; Hyperhomocysteinemia; Male; Methionine; Middle Aged; Porphyria, Acute Intermittent; Pyridoxal Phosphate; Pyrrolidines; Young Adult | 2021 |
Nanosecond heme-to-heme electron transfer rates in a multiheme cytochrome nanowire reported by a spectrally unique His/Met-ligated heme.
Topics: Cytochrome c Group; Cytochromes; Electron Transport; Electrons; Heme; Histidine; Methionine; Molecular Dynamics Simulation; Nanowires; Oxidation-Reduction; Shewanella | 2021 |
Hyperhomocysteinemia in acute hepatic porphyria (AHP) and implications for treatment with givosiran.
Topics: Clinical Trials as Topic; Cystathionine beta-Synthase; Folic Acid; Heme; Homocysteine; Humans; Hyperhomocysteinemia; Methionine; Porphyrias, Hepatic; Pyridoxine; RNA, Small Interfering; Sulfur; Vitamin B 6 | 2022 |
Proteomic, Transcriptomic, Mutational, and Functional Assays Reveal the Involvement of Both THF and PLP Sites at the GmSHMT08 in Resistance to Soybean Cyst Nematode.
Topics: Animals; Carbon; Cysts; Glycine; Glycine Hydroxymethyltransferase; Glycine max; Glyoxylates; Heme; Methionine; Nematoda; Plant Diseases; Proteomics; Purines; Pyridoxal Phosphate; Serine; Tetrahydrofolates; Transcriptome | 2022 |
An engineered thermally tolerant apo-cytochrome scaffold for metal-less incorporation of heme derivative.
Topics: Alanine; Cytochromes c; Heme; Ligands; Methionine; Molecular Docking Simulation; Oxidation-Reduction | 2023 |