Polarographic Reduction of the Heme Iron in Native Horse-Heart Cytochrome c

Betso, Stephen R.; Klapper, Michael H.; Anderson, Larry B.

doi:10.1007/978-3-0348-5848-9_9

Cited by 4 publications

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“…The electrochemical methods have been applied in studying the electron transfer reactions of model systems for the prosthetic group in the heme proteins (16). The electrochemical reduction of ferricytochrome c on platinum (17) and mercury electrodes (18) has been studied. The mechanism of Charge transfer was proposed to be a superposition of electron transport through adsorbed molecules and exchange of already reduced molecules (19).…”

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confidence: 99%

Electrode Reaction of Cytochrome c 3 of Desulfovibrio vulgaris, Miyazaki

Niki

Yagi

Inokuchi

et al. 1977

J. Electrochem. Soc.

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Cytochrome c3 is an electron carrier present in the redox system of sulfate-reducing bacteria, desulJovibrio (1). it has been isolated from d. vulgaris, Hildenborough (2, 3). d. vulgaris, Miyazaki (4-U), d. de-su~furicans (7), d. saIexigens (8), and d. gigas (9). The physicochemical properties of cytochrome c~ extracted from d. vu~garis, 1Vliyazaki, have been studied extensively in our laboratory (~). Its molecular weight is nearly 14,000. The heme content of cytochrome c~ has been believed to be two or more (3, 7, 10-12), and we confirmed that it contains four homes by chemical analysis (6). Later Meyer et al. also reported four heroes in the molecule (13). Cytochrome c3 is a natural electron acceptor for desulfovibrio hydrogenase (hydrogen: ferricytochrome c~ oxidoreductase, EC 1.12.2.1), and is reversibly reduced by molecular hydrogen in the presence of hydrogenase ( 14). It has been demonstrated by Yagi et al. (15) that cytochrome c3 is elec-* Electrochemical Society Active Member.

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confidence: 99%