Reaction of thionitrobenzoate-modified yeast cytochrome c with monomeric and dimeric forms of beef heart cytochrome c oxidase

Academic Article

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. © 1984.
  • Digital Object Identifier (doi)

    Author List

  • Darley-Usmar VM; Georgevich G; Capaldi RA
  • Start Page

  • 131
  • End Page

  • 135
  • Volume

  • 166
  • Issue

  • 1