Differential effects of triphenyltin and 8-azido-ATP on the ATP synthesis, ATP-Pi exchange, and ATP hydrolysis in liposomes containing ATP synthase and bacteriorhodopsin.
The ATP hydrolysis activity of purified ATP synthase reconstituted in liposomes was inhibited by triphenyltin in a manner different from that of other thiol-specific reagents. In liposomes containing ATP synthase and bacteriorhodopsin, ATP hydrolysis and ATP-Pi exchange were inhibited by triphenyltin to a greater extent than the ATP synthesis, in contrast to what was found with an F1-specific inhibitor, 8-azido-ATP. The possibility is discussed that ATP hydrolysis and ATP synthesis are differently coupled to proton conduction through F0.
Van der Bend
R L
RL
Duetz
W
W
Colen
A M
AM
Van Dam
K
K
Berden
J A
JA
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism* / Q000494:pharmacology; D000609:Aminoacridines; D001386:Azides / Q000494:pharmacology*; D001436:Bacteriorhodopsins / Q000502:physiology*; D002338:Carotenoids / Q000502:physiology*; D005453:Fluorescence; D006868:Hydrolysis; D008027:Light; D008081:Liposomes / Q000378:metabolism*; D009947:Organotin Compounds / Q000494:pharmacology*; D010710:Phosphates / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000502:physiology*; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D000609:Aminoacridines; D001386:Azides; D008081:Liposomes; D009947:Organotin Compounds; D010710:Phosphates; D013439:Sulfhydryl Reagents; C010847:9-amino-6-chloro-2-methoxyacridine; D002338:Carotenoids; D001436:Bacteriorhodopsins; C017040:8-azidoadenosine 5'-triphosphate; D000255:Adenosine Triphosphate; C030665:triphenyltin; D006180:Proton-Translocating ATPases