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

David S. Perlin; Lisa R. Latchney; Alan E. Senior

doi:10.1016/0005-2728(85)90254-3

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

David S. Perlin
, Lisa R. Latchney
, Alan E. Senior

Center for Discovery and Innovation

Hackensack Meridian School of Medicine

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	238-244
Number of pages	7
Journal	BBA - Bioenergetics
Volume	807
Issue number	3
DOIs	https://doi.org/10.1016/0005-2728(85)90254-3
State	Published - May 31 1985

ASJC Scopus subject areas

Biophysics
Biochemistry
Cell Biology

Keywords

(E. coli)
H-ATPase
Oligomycin
Ossamycin
Proton translocation
Venturicidin

Access to Document

10.1016/0005-2728(85)90254-3

Cite this

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title = "Inhibition of Escherichia coli H+-ATPase by venturicidin, oligomycin and ossamycin",

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.",

keywords = "(E. coli), H-ATPase, Oligomycin, Ossamycin, Proton translocation, Venturicidin",

author = "Perlin, \{David S.\} and Latchney, \{Lisa R.\} and Senior, \{Alan E.\}",

year = "1985",

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doi = "10.1016/0005-2728(85)90254-3",

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T1 - Inhibition of Escherichia coli H+-ATPase by venturicidin, oligomycin and ossamycin

AU - Perlin, David S.

AU - Latchney, Lisa R.

AU - Senior, Alan E.

PY - 1985/5/31

Y1 - 1985/5/31

N2 - 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.

AB - 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.

KW - (E. coli)

KW - H-ATPase

KW - Oligomycin

KW - Ossamycin

KW - Proton translocation

KW - Venturicidin

UR - https://www.scopus.com/pages/publications/0021875477

U2 - 10.1016/0005-2728(85)90254-3

DO - 10.1016/0005-2728(85)90254-3

M3 - Article

C2 - 2859888

SN - 0005-2728

VL - 807

SP - 238

EP - 244

JO - BBA - Bioenergetics

JF - BBA - Bioenergetics

IS - 3

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