Binding of MOA-stilbene to the mitochondrial cytochrome bc1 complex is affected by the protonation state of a redox-Bohr group of the 'Rieske' iron-sulfur protein

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1321, Issue 3, 1997, Pages 238-242

  Brandt, Ulrich ^a   Djafarzadeh Andabili, Roghieh ^a  

^a UNIVERSITY HOSPITAL FRANKFURT   (Germany)

Author keywords

Cytochrome bc1 complex; E methoxyacrylate; Inhibitor; Iron sulfur protein; MOA stilbene; Q cycle

Indexed keywords

3 METHOXYACRYLIC ACID; ENZYME INHIBITOR; IRON SULFUR PROTEIN; UBIQUINOL CYTOCHROME C REDUCTASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATTLE; DISSOCIATION CONSTANT; ENZYME ACTIVE SITE; ENZYME BINDING; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTON TRANSPORT;

ANIMALS; BINDING SITES; CATTLE; ELECTRON TRANSPORT COMPLEX III; HYDROGEN-ION CONCENTRATION; IRON-SULFUR PROTEINS; KINETICS; OXIDATION-REDUCTION; STILBENES;

BOS TAURUS; BOVINAE;

EID: 0030730497     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(97)00060-1     Document Type: Article

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