PMID: 6093868Oct 9, 1984

Effect of membrane potential and pH gradient on electron transfer in cytochrome oxidase

Biochemistry
P M MoroneyP C Hinkle

Abstract

Steady-state spectra of cytochrome oxidase in phospholipid vesicles were obtained by using hexaammineruthenium(II) and ascorbate as reductants. Cytochrome a was up to 80% reduced in the steady state in coupled vesicles. Upon addition of nigericin or acetate, which decrease delta pH, resulting in an increase in delta psi, cytochrome a became more oxidized in the steady state with no change in the rate of respiration. On the other hand, uncouplers or valinomycin plus nigericin, which lower both delta psi and delta pH, stimulated respiration 2-8-fold and also lowered the steady-state level of reduction of cytochrome a. These experiments indicate that electron transfer between cytochromes a and a 3 is sensitive primarily to the pH gradient. Studies with the reconstituted and the soluble enzyme at various pH values indicated that the pH on the matrix side of the membrane, rather than delta pH, controlled the steady-state level of reduced cytochrome a. Hexaammineruthenium(II) substituted for cytochrome c in measurements of proton pumping by cytochrome oxidase. Dicyclohexylcarbodiimide, which eliminated proton pumping by cytochrome oxidase, decreased the effect of ionophores on the steady-state level of reduced cytochrome a.

References

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Citations

Apr 1, 1987·Journal of Bioenergetics and Biomembranes·L J Prochaska, P S Fink
Jan 1, 1988·The International Journal of Biochemistry·T D Madden
Apr 17, 1985·Biochimica Et Biophysica Acta·A Chakrabartty, R A Stinson
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Aug 3, 1987·European Journal of Biochemistry·W de Vrij, W N Konings
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Oct 15, 2013·The Journal of Chemical Physics·Shahin Sowlati-Hashjin, Chérif F Matta
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Related Concepts

hexammineruthenium(II)
Cytochrome c Oxidase Subunit VIa
Cytochromes
Dicyclohexylcarbodiimide
Respiratory Chain
Hydrogen-Ion Concentration
Niosomes
Resting Potentials
Oxidation-Reduction
Oxygen Consumption

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