Cytochrome C-mediated Electron Transfer Between Ubiquinol-cytochrome C Reductase and Cytochrome C Oxidase. Kinetic Evidence for a Mobile Cytochrome C Pool

Overview

Journal Biochem J

Specialty Biochemistry

Date 1984 Jan 15

PMID 6320810

Citations 3

Authors

R J Froud

C I Ragan

Affiliations

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Abstract

Ubiquinol oxidase has been reconstituted from ubiquinol-cytochrome c reductase (Complex III), cytochrome c and cytochrome c oxidase (Complex IV). The steady-state level of reduction of cytochrome c by ubiquinol-2 varies with the molar ratios of the complexes and with the presence of antimycin in a way that can be quantitatively accounted for by a model in which cytochrome c acts as a freely diffusible pool on the membrane. This model was based on that of Kröger & Klingenberg [(1973) Eur. J. Biochem. 34, 358-368] for ubiquinone-pool behaviour. Further confirmation of the pool model was provided by analysis of ubiquinol oxidase activity as a function of the molar ratio of the complexes and prediction of the degree of inhibition by antimycin.

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