Inhibition of Escherichia coli H+-ATPase by venturicidin, oligomycin and ossamycin.
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.
Perlin
D S
DS
Latchney
L R
LR
Senior
A E
AE
D000255:Adenosine Triphosphate / Q000378:metabolism; D000617:Aminoglycosides / Q000494:pharmacology; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001693:Biological Transport, Active / Q000187:drug effects; D004926:Escherichia coli / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007783:Lactones / Q000494:pharmacology*; D018942:Macrolides; D009840:Oligomycins / Q000494:pharmacology*; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors*; D014475:Uncoupling Agents; D014698:Venturicidins / Q000494:pharmacology*
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D007783:Lactones; D018942:Macrolides; D009840:Oligomycins; D014475:Uncoupling Agents; D014698:Venturicidins; C008717:ossamycin; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases