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Title: Reaction of thionitrobenzoate-modified yeast cytochrome c with monomeric and dimeric forms of beef heart cytochrome c oxidase. Author: Darley-Usmar VM, Georgevich G, Capaldi RA. Journal: FEBS Lett; 1984 Jan 23; 166(1):131-5. PubMed ID: 6319188. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]