F0F1-ATPase from Vibrio alginolyticus. Subunit composition and proton pumping activity.
An F0F1-ATPase was isolated from the membranes of the marine bacterium Vibrio alginolyticus. Homology between the subunits of the F0-complexes from E. coli and V. alginolyticus was found using antibodies against subunits a, b and c of the E. coli F0F1-ATPase. The F0F1-complex from V. alginolyticus was reconstituted into proteoliposomes, which were competent in ATP-dependent proton uptake. This process was inhibited by triphenyltin, DCCD, and venturicidin. Na+ did not affect proton translocation.
Dmitriev OYu
A.N. Belozersky Laboratory for Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Krasnoselskaya
I A
IA
Papa
S
S
Skulachev
V P
VP
D000255:Adenosine Triphosphate / Q000494:pharmacology; D001693:Biological Transport, Active; D015153:Blotting, Western; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone / Q000494:pharmacology; D008081:Liposomes / Q000378:metabolism; D046911:Macromolecular Substances; D008970:Molecular Weight; D011188:Potassium / Q000494:pharmacology; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D011522:Protons; D012964:Sodium / Q000494:pharmacology; D014733:Vibrio / Q000201:enzymology*
D008081:Liposomes; D046911:Macromolecular Substances; D011522:Protons; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; D000255:Adenosine Triphosphate; D012964:Sodium; D006180:Proton-Translocating ATPases; D011188:Potassium