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. 1977 Oct;74(10):4306–4310. doi: 10.1073/pnas.74.10.4306

Oligomycin-dependent ionophoric protein subunit of mitochondrial adenosinetriphosphatase.

R S Criddle, L Packer, P Shieh
PMCID: PMC431929  PMID: 144916

Abstract

A proteolipid isolated from yeast mitochondrial adenosinetriphosphatase (subunit 9) (ATP phosphohydrolase; EC 3.6.1.3) by chloroform/methanol extraction has been shown to discharge photo-induced potentials across a planar phospholipid membrane containing bacteriorhodopsin. Oligomycin, a specific inhibitor of oxidative phosphorylation which binds to this protein, allows the potential gradient to be reestablished. When proteolipid was isolated from an oligomycin-resistant strain, ionophoric activity was still obtained but the effect was not reversed by oligomycin. These studies suggest that the hydrophobic subunit-9 polypeptide is the ionophoric component linking ATP synthesis (hydrolysis) with proton translocation.

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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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