Reaction of thionitrobenzoate-modified yeast cytochrome c with monomeric and dimeric forms of beef heart cytochrome c oxidase.
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.
D000345:Affinity Labels; D000818:Animals; D002417:Cattle; D003574:Cytochrome c Group / Q000378:metabolism*; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000378:metabolism*; D046911:Macromolecular Substances; D008929:Mitochondria, Heart / Q000201:enzymology*; D013329:Structure-Activity Relationship
D000345:Affinity Labels; D003574:Cytochrome c Group; D046911:Macromolecular Substances; D003576:Electron Transport Complex IV