On the extent of localization of the energized membrane state in chromatophores from Rhodopseudomonas capsulata N22

Abstract

The principle of the double-inhibitor titration method for assessing competing models of electron transport phosphorylation is expounded. This principle is applied to photophosphorylation by chromatophores from R. capsulata N22. In contrast to the predictions of the chemiosmotic coupling model, free energy transfer is confined to individual electron transport chain and ATP synthase complexes. This conclusion is not weakened by arguments concerning the degree of uncoupling in the native chromatophore preparation or the relative number of electron transport chain and ATP synthase complexes present. Photophosphorylation is completely inhibited by the uncoupler SF 6847 [3,5-di-tert-butyl-4-hydroxybenzylidene malononitrile] at a concentration corresponding to 0.31 molecules per electron transport chain. The apparent paradox is solved by the proposal, consistent with the available evidence on the mode of action of uncouplers, that uncoupler binding causes a cooperative conformational transition in the chromatophore membrane, which leads to uncoupling and which is not present in the absence of uncoupler.