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
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25 references, click to expand
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