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Volumn 285, Issue 1, 2010, Pages 502-510
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Direct demonstration of half-of-the-sites reactivity in the dimeric cytochrome bc1 complex: Enzyme with one inactive monomer is fully active but unable to activate the second ubiquinol oxidation site in response to ligand binding at the ubiquinone reduction site
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Author keywords
[No Author keywords available]
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Indexed keywords
ANTIMYCIN;
CYTOCHROME B;
DIMERIC ENZYME;
ELECTRON TRANSFER;
LIGAND BINDING;
LOW CONCENTRATIONS;
PARACOCCUS DENITRIFICANS;
STEADY STATE RATES;
STEADY-STATE CONDITION;
UBIQUINOL;
UBIQUINONE;
WILD TYPES;
BINDING SITES;
ELECTRON TRANSITIONS;
ENZYMES;
MONOMERS;
OXIDATION;
ENZYME ACTIVITY;
CITRININ;
CYTOCHROME B;
UBIQUINOL CYTOCHROME C REDUCTASE;
UBIQUINONE;
ARTICLE;
CATALYSIS;
CONTROLLED STUDY;
DIMERIZATION;
ELECTRON TRANSPORT;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
GENE MUTATION;
LIGAND BINDING;
NONHUMAN;
OXIDATION;
PARACOCCUS DENITRIFICANS;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN DEGRADATION;
STEADY STATE;
WILD TYPE;
ANIMALS;
ANTIMYCIN A;
BINDING SITES;
CHROMATOGRAPHY, AFFINITY;
ELECTRON TRANSPORT COMPLEX III;
ENZYME ACTIVATION;
HORSES;
KINETICS;
LIGANDS;
MUTAGENESIS;
MUTANT PROTEINS;
OPERON;
OXIDATION-REDUCTION;
PARACOCCUS DENITRIFICANS;
PROTEIN MULTIMERIZATION;
TITRIMETRY;
UBIQUINONE;
PARACOCCUS DENITRIFICANS;
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EID: 73649089642
PISSN: 00219258
EISSN: 1083351X
Source Type: Journal
DOI: 10.1074/jbc.M109.072959 Document Type: Article |
Times cited : (56)
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References (33)
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