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Proton pump coupled to cytochrome c oxidase in Paracoccus denitrificans

Van Verseveld, H.W.; Krab, K.; Stouthamer, A.H.

Biochimica et Biophysica Acta 635(3): 525-534

1981

ISSN/ISBN: 0006-3002
PMID: 6263335
DOI: 10.1016/0005-2728(81)90111-0
Accession: 044080369

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Summary
The proton translocating properties of cytochrome c oxidase in whole cells of Paracoccus denitrificans have been studied with the oxidant pulse method. leads to H+/2e- quotients have been measured with endogenous substrates, added methanol and added ascorbate (+TMPD) as reductants, and oxygen and ferricyanide as oxidants. It was found that both the observed leads to H+/O with ascorbate (+TMPD) as reductant, and the differences in proton ejection between oxygen-and ferricyanide pulses, with endogenous substrates or added methanol as a substrate, indicate that the P. denitrificans cytochrome c oxidase translocates protons with a stoichiometry of 2H+/2e-. The results presented in this and previous papers are in good agreement with recent findings concerning the mitochondrial cytochrome c oxidase, and suggest unequal charge separation by different coupling segments of the respiratory chain of P. denitrificans.

References

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