A critical appraisal of evidence for localized energy coupling. Kinetic studies on liposomes containing bacteriorhodopsin and ATP synthase.
In intact systems (chloroplasts, mitochondria and bacteria) many experiments have been reported which are indicative of localized coupling between ATP synthase and electron transfer complexes. We have carried out similar experiments with a system in which we may assume that specific interactions between the proton pumps are absent: reconstituted vesicles containing bacteriorhodopsin and yeast mitochondrial ATP synthase. The only experiment that gives results which differ from those previously published for intact systems concerns the effect of uncouplers on the rate of ATP synthesis at different levels of inhibition of the ATP synthase. We propose that this type of experiment may discriminate between localized and delocalized coupling.
D025181:ATP Synthetase Complexes; D000255:Adenosine Triphosphate / Q000096:biosynthesis; D001436:Bacteriorhodopsins / Q000378:metabolism*; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone / Q000494:pharmacology; D002338:Carotenoids / Q000378:metabolism*; D004579:Electron Transport; D004735:Energy Transfer; D007700:Kinetics; D008027:Light; D008081:Liposomes / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010770:Phosphotransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011522:Protons
D008081:Liposomes; D009097:Multienzyme Complexes; D011522:Protons; D002338:Carotenoids; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; D001436:Bacteriorhodopsins; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; D025181:ATP Synthetase Complexes