Localized energy coupling during photophosphorylation by chromatophores of Rhodopseudomonas capsulata N22.
The principle of the dual inhibitor titration method for testing models of electron-transport phosphorylation is outlined, and the method is applied to the study of photophosphorylation in bacterial chromatophores. It is concluded that energy coupling is strictly localized in nature in this system, in the sense that free energy released by a particular electron-transport chain may be used only by a particular H+-ATP synthase. Dual inhibitor titrations using the uncoupler SF 6847 and the H+-ATP synthase inhibitor oligomycin indicate that uncouplers act by shuttling rapidly between the localized energy-coupling sites.
D025181:ATP Synthetase Complexes; D000968:Antimycin A / Q000494:pharmacology; D020130:Bacterial Chromatophores / Q000378:metabolism*; D004579:Electron Transport; D007700:Kinetics; D009097:Multienzyme Complexes / Q000378:metabolism; D009570:Nitriles / Q000494:pharmacology; D009840:Oligomycins / Q000494:pharmacology; D010770:Phosphotransferases / Q000378:metabolism; D010785:Photophosphorylation / Q000187:drug effects; D012241:Rhodopseudomonas / Q000378:metabolism*; D014475:Uncoupling Agents / Q000494:pharmacology
D009097:Multienzyme Complexes; D009570:Nitriles; D009840:Oligomycins; D014475:Uncoupling Agents; C001784:SF 6847; D000968:Antimycin A; D010770:Phosphotransferases; D025181:ATP Synthetase Complexes