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PMID: 144916 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Oligomycin-dependent ionophoric protein subunit of mitochondrial adenosinetriphosphatase.

Criddle RS, Packer L, Shieh P

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.

MeSH Terms
Adenosine Triphosphatases Bacteriorhodopsins Chemical Phenomena Chemistry Drug Resistance, Microbial Filtration Fungal Proteins/analysis Ionophores/analysis Lipids Membranes, Artificial Mitochondria/enzymology Oligomycins/pharmacology Saccharomyces cerevisiae/enzymology Time Factors
Chemicals
Fungal Proteins Ionophores Lipids Membranes, Artificial Oligomycins Bacteriorhodopsins Adenosine Triphosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Criddle R S
Packer L
Shieh P
References (25)
25 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1977-10-00
Pages
4306-10
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431929
Subset
IM
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