Oligomycin-dependent ionophoric protein subunit of mitochondrial adenosinetriphosphatase.
- 1 October 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (10) , 4306-4310
- https://doi.org/10.1073/pnas.74.10.4306
Abstract
A proteolipid isolated from yeast [Saccharomyces cerevisiae] mitochondrial adenosinetriphosphatase (subunit 9) (ATP phosphohydrolase; EC 3.6.1.3) by chloroform/methanol extraction was 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.This publication has 25 references indexed in Scilit:
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