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. 1989 May 15;160(3):1132-9.
doi: 10.1016/s0006-291x(89)80121-4.

Valinomycin binds stoichiometrically to cytochrome c oxidase and changes its structure and function

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Valinomycin binds stoichiometrically to cytochrome c oxidase and changes its structure and function

D Steverding et al. Biochem Biophys Res Commun. .

Abstract

Valinomycin binds to soluble and reconstituted cytochrome c oxidase (COX) in a stoichiometric manner, as shown by a spectral shift of the oxidized gamma-band. No spectral change is found with nigericin or 18-crown-6 and in the absence of potassium ions. Titration of the proton pumping activity of reconstituted COX with valinomycin reached a maximum of H+/e- - 0.73 after addition of 1 mole of valinomycin per mole of reconstituted COX. It is concluded that K+-translocation in proton-pumping COX vesicles occurs via enzyme-bound valinomycin.

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