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Cytochrome oxidase as a proton pump.

M T Wilson¹, D Bickar

¹Department of Chemistry and Biological Chemistry, University of Essex, Colchester, U.K.

Journal of Bioenergetics and Biomembranes

|October 1, 1991

Summary

Cytochrome oxidase functions as a proton pump, but only the final two electrons are coupled to proton translocation. This finding restricts potential mechanisms for proton pumping by this crucial enzyme.

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Area of Science:

Biochemistry
Molecular Biology
Bioenergetics

Background:

Cytochrome oxidase is a key enzyme in cellular respiration.
It is known to function as a proton pump, contributing to the proton gradient across membranes.
The precise mechanism and stoichiometry of proton pumping remain areas of active research.

Purpose of the Study:

To review the structure of cytochrome oxidase.
To outline evidence for its function as a redox-linked proton pump.
To discuss proposed mechanisms of proton translocation.

Main Methods:

Review of existing literature and experimental data.
Analysis of the H+/e- stoichiometry of the proton pump.
Consideration of specific experimental results suggesting a limited coupling of electrons to proton translocation.

Main Results:

Evidence suggests cytochrome oxidase acts as a redox-linked proton pump.
The overall H+/e- stoichiometry is discussed, with findings indicating only the final two electrons are coupled to proton translocation.
This limited coupling places restrictions on proposed pump mechanisms.

Conclusions:

The study reviews cytochrome oxidase structure and its proton pump activity.
It highlights that only the final two electrons are coupled to proton translocation, impacting mechanistic models.
Direct and indirect proton translocation mechanisms are discussed in light of enzyme conformational changes, subunit III, and the CuA site.

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