Binding and oxidation of mutant cytochromescby cytochrome-coxidase
- 30 January 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 243 (2) , 149-152
- https://doi.org/10.1016/0014-5793(89)80118-8
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 dissociationKeywords
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