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Volumn 532, Issue 3, 2002, Pages 333-337
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A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis
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Author keywords
Cooperativity; Heme architecture; NMR; Polarography; Redox potential; Tetraheme cytochrome
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Indexed keywords
CYTOCHROME C;
FUMARIC ACID;
HEME;
HEME DERIVATIVE;
OXIDOREDUCTASE;
QUERCETIN;
SMALL TETRAHEME CYTOCHROME C;
UNCLASSIFIED DRUG;
AMINO TERMINAL SEQUENCE;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
CONTROLLED STUDY;
ELECTRON TRANSPORT;
MICROSCOPY;
NONHUMAN;
OXIDATION REDUCTION REACTION;
POLARIZATION;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN DOMAIN;
REDUCTION;
SHEWANELLA;
NON-PROGRAMMATIC;
BINDING SITES;
CYTOCHROME C GROUP;
ELECTRONS;
HEME;
HYDROGEN-ION CONCENTRATION;
MAGNETIC RESONANCE SPECTROSCOPY;
MODELS, CHEMICAL;
OXIDATION-REDUCTION;
OXIDOREDUCTASES;
POTASSIUM CHLORIDE;
PROTEIN BINDING;
PROTEIN STRUCTURE, TERTIARY;
SHEWANELLA;
SUCCINATE DEHYDROGENASE;
SHEWANELLA;
SHEWANELLA ONEIDENSIS;
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EID: 0037132498
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(02)03696-7 Document Type: Article |
Times cited : (39)
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References (20)
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