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. 1987 Nov 15;248(1):161–165. doi: 10.1042/bj2480161

Modulation of cytochrome oxidase activity by inorganic and organic phosphate.

F Malatesta 1, G Antonini 1, P Sarti 1, M Brunori 1
PMCID: PMC1148513  PMID: 2829818

Abstract

The activity of cytochrome oxidase reconstituted into phospholipid vesicles has been studied as a function of orthophosphate, ATP and inositol hexakisphosphate concentrations. The respiratory-control ratio was found to be quite sensitive to these compounds and was inversely related to the anion concentration. This effect is related to a phosphate-dependent decrease in the rate constant for ferrocytochrome c oxidation observed in the presence of ionophores. The data cannot be interpreted simply on the basis of ionic strength, which is known to limit cytochrome c binding to cytochrome oxidase, since cytochrome oxidase-containing vesicles responded differently to phosphate depending on the energization state of the phospholipid membrane.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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