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. 1976 Jan;73(1):113–117. doi: 10.1073/pnas.73.1.113

Oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.

B Errede, G P Haight Jr, M D Kamen
PMCID: PMC335850  PMID: 174095

Abstract

Attempts to rationalize the kinetics of cytochrome c oxidation catalyzed by solubilized mitochondrial cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) have been based on assumptions of productive complex formation (Michaelis-Menten approach). However, the range of substrate concentrations used has not, in general, been sufficient to establish a general rate equation. Data adequate to derive such a rate expression are presented, as well as a method for estimation of constants which appear in the rate law deduced and reported herein. It is shown that either of two types of mechanisms, one assuming productive complex formation, as opposed to the other postulating dead-end complex formation, accurately predict the rate equation as deduced from experiment.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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