| Literature DB >> 144916 |
R S Criddle, L Packer, P Shieh.
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.Entities:
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Year: 1977 PMID: 144916 PMCID: PMC431929 DOI: 10.1073/pnas.74.10.4306
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205