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  • Title: Binding and oxidation of mutant cytochromes c by cytochrome-c oxidase.
    Author: Michel B, Mauk AG, Bosshard HR.
    Journal: FEBS Lett; 1989 Jan 30; 243(2):149-52. PubMed ID: 2537228.
    Abstract:
    Mutation of conserved Phe-82 of yeast iso-1 cytochrome c to Tyr, Gly, Ser, Leu, or Ile affects binding to and reaction with cytochrome-c oxidase from beef heart. The observed changes of binding and kinetic constants reflect mutation-induced rearrangements in the heme vicinity brought about by the replacement of Phe-82. Such conformational rearrangements are also revealed by altered circular dichroism spectra of the oxidase-bound mutant cytochromes c. Variations in Km for cytochrome c oxidation do not parallel variations in Kd, the dissociation constant for binding of cytochrome c to the oxidase. This observation does not support an enzymatic mechanism in which the rate of cytochrome c oxidation is governed by product dissociation.
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