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PMID: 2859888 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Inhibition of Escherichia coli H+-ATPase by venturicidin, oligomycin and ossamycin.

Biochimica et biophysica acta ·Vol. 807 ·No. 3 ·1985-05-31 ·Pages 238-44

Perlin DS, Latchney LR, Senior AE

Abstract

The antibiotics venturicidin, oligomycin and ossamycin were investigated as potential inhibitors of the Escherichia coli H+-ATPase. It was found that venturicidin strongly inhibited ATP-driven proton transport and ATP hydrolysis, while oligomycin weakly inhibited these functions. Inhibition of the H+-ATPase by venturicidin and oligomycin was correlated with inhibition of F0-mediate proton transport. Both inhibitors were found to interfere with the covalent reaction between dicyclohexyl[14C]carbodiimide and the F0 subunit c (uncE protein). Ossamycin had no direct inhibitory effect on E. coli F0 or F1; rather, it was found to uncouple ATP hydrolysis from proton transport.

MeSH Terms
Adenosine Triphosphate/metabolism Aminoglycosides/pharmacology Anti-Bacterial Agents/pharmacology Biological Transport, Active/drug effects Escherichia coli/enzymology Hydrogen-Ion Concentration Lactones/pharmacology Macrolides Oligomycins/pharmacology Proton-Translocating ATPases/antagonists & inhibitors Uncoupling Agents Venturicidins/pharmacology
Chemicals
Aminoglycosides Anti-Bacterial Agents Lactones Macrolides Oligomycins Uncoupling Agents Venturicidins ossamycin Adenosine Triphosphate Proton-Translocating ATPases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Perlin D S
Latchney L R
Senior A E
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1985-05-31
Pages
238-44
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
Grants
NIGMS NIH HHS · GM25349 · United States
NIGMS NIH HHS · GM29805 · United States
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