PMID: 40970Nov 10, 1979

The charge stoichiometry of cytochrome c oxidase in the reconstituted system

The Journal of Biological Chemistry
E Sigel, E Carafoli

Abstract

Purified cytochrome c oxidase was reconstituted into phospholipid vesicles having high internal pH buffering capacity. In the presence of valinomycin, 2 K+ ions were taken up by the vesicles per electron transferred from cytochrome c to oxygen. The charge stoichiometry of 2 was obtained from simultaneous measurement of changes of K+, H+, and oxygen in the medium after addition of the reductant ascorbate/TMPD (N,N,N',N'-tetramethyl-p-phenylenediamine). The changes in oxygen concentration were measured with a fast responding oxygen electrode (90% response time, 0.4 s). The existence of a proton pump in cytochrome c oxidase could thus be confirmed, and its charge stoichiometry measured, in a reconstituted system uncomplicated by other respiratory chain components.

Related Concepts

CYCS
COX1
Cytochrome C Oxidase
Cytochrome c Oxidase Subunit VIa
Valinomycin
Potassium
Myocardium
ATP12A gene
Ascorbate
Vesicle

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