Mode of inhibition of sodium azide on H+-ATPase of Escherichia coli.
Sodium azide inhibited multi-site (steady-state) ATPase activity of E. coli F1 more than 90%, but did not affect uni-site (single-site) ATPase activity. Thus azide inhibited multi-site ATPase activity by lowering catalytic cooperativity. Consistent with this observation, azide changed the ligand-induced fluorescence response of aurovertin bound to F1.
D000244:Adenosine Diphosphate / Q000378:metabolism / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000378:metabolism; D001313:Aurovertins / Q000378:metabolism; D001386:Azides / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D011487:Protein Conformation / Q000187:drug effects; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D019810:Sodium Azide; D013050:Spectrometry, Fluorescence
D001313:Aurovertins; D001386:Azides; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D019810:Sodium Azide; D006180:Proton-Translocating ATPases; D008274:Magnesium