The oligomycin axis of mitochondrial ATP synthase: OSCP and the proton channel

Oligomycin has long been known as an inhibitor of mitochondrial ATP synthase, putatively binding the F(o) subunits 9 and 6 that contribute to proton channel function of the complex. As its name implies, OSCP is the oligomycin sensitivity-conferring protein necessary for the intact enzyme complex to...

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Bibliographic Details
Published in:Journal of bioenergetics and biomembranes 2000-10, Vol.32 (5), p.507-515
Main Authors: Devenish, R J, Prescott, M, Boyle, G M, Nagley, P
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
Animals
ATP
Binding Sites
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - metabolism
Enzymes
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Mitochondrial Proton-Translocating ATPases - antagonists & inhibitors
Mitochondrial Proton-Translocating ATPases - chemistry
Mitochondrial Proton-Translocating ATPases - metabolism
Models, Molecular
Multiprotein Complexes
Oligomycins - pharmacology
Protein Subunits
Proteins
Rats
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Saccharomyces cerevisiae - enzymology
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Summary:Oligomycin has long been known as an inhibitor of mitochondrial ATP synthase, putatively binding the F(o) subunits 9 and 6 that contribute to proton channel function of the complex. As its name implies, OSCP is the oligomycin sensitivity-conferring protein necessary for the intact enzyme complex to display sensitivity to oligomycin. Recent advances concerning the structure and mechanism of mitochondrial ATP synthase have led to OSCP now being considered a component of the peripheral stator stalk rather than a central stalk component. How OSCP confers oligomycin sensitivity on the enzyme is unknown, but probably reflects important protein-protein interactions made within the assembled complex and transmitted down the stator stalk, thereby influencing proton channel function. We review here our studies directed toward establishing the stoichiometry, assembly, and function of OSCP in the context of knowledge of the organization of the stator stalk and the proton channel.
ISSN:0145-479X
1573-6881
DOI:10.1023/A:1005621125812