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. 1990 Nov;87(21):8408–8412. doi: 10.1073/pnas.87.21.8408

Cytochrome c oxidase: decay of the primary oxygen intermediate involves direct electron transfer from cytochrome a.

S H Han 1, Y C Ching 1, D L Rousseau 1
PMCID: PMC54965  PMID: 2172987

Abstract

The decay of the primary intermediate generated in the reaction of oxygen with cytochrome c oxidase is nearly one order of magnitude faster in the fully reduced form of the enzyme than it is in the mixed valence form. To account for this observation, we propose a model describing the early molecular events in the reaction. In this model the decay of the primary Fe-O2 intermediate in the fully reduced enzyme is a consequence of direct electron transfer from cytochrome a. To test the model we measured the time dependence of the oxidation of cytochrome a by monitoring the resonance Raman scattering intensity of its vibrational modes. A rapid oxidation of cytochrome a was detected that quantitatively agrees with the model. These results indicate that the mechanism of oxygen reduction and proposed frameworks for proton translocation must be reexamined.

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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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