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Reaction of thionitrobenzoate‐modified yeast cytochrome c with monomeric and dimeric forms of beef heart cytochrome c oxidase
Author(s) -
Darley-Usmar Victor M.,
Georgevich Gradimir,
Capaldi Roderick A.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80058-7
Subject(s) - cytochrome c oxidase , coenzyme q – cytochrome c reductase , cytochrome c peroxidase , cytochrome c1 , chemistry , dimer , cytochrome p450 reductase , cytochrome b , cytochrome c , cytochrome , yeast , protein subunit , biochemistry , monomer , stereochemistry , enzyme , organic chemistry , mitochondrion , mitochondrial dna , polymer , gene
Thionitrobenzoate‐modified yeast cytochrome c was shown to react with both monomeric and dimeric forms of beef heart cytochrome c oxidase through subunit III. This cytochrome c derivative was found to inhibit electron transfer in the dimer but not in the monomer. These results are interpreted to show that the high affinity binding site for cytochrome c is a cleft at the interface between monomers in the cytochrome c oxidase dimer.