PMID: 7150247Aug 15, 1982Paper

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

The Biochemical Journal
G D Hitchens, D B Kell

Abstract

1. The principle of the double-inhibitor titration method for assessing competing models of electron transport phosphorylation is expounded. 2. This principle is applied to photophosphorylation by chromatophores from Rhodopseudomonas capsulata N22. 3. It is found that, in contrast to the predictions of the chemiosmotic coupling model, free energy transfer is confined to individual electron transport chain and ATP synthase complexes. 4. 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. 5. Photophosphorylation is completely inhibited by the uncoupler SF 6847 at a concentration corresponding to 0.31 molecules per electron transport chain. 6. 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 co-operative conformation transition in the chromatophore membrane, which leads to uncoupling and which is not present in the absence of uncoupler.

Citations

Nov 15, 1985·European Journal of Biochemistry·M G ElferinkW N Konings
Aug 3, 1987·European Journal of Biochemistry·E C Slater
Jan 1, 1987·Biochimica Et Biophysica Acta·S R Caplan, D Pietrobon
Oct 1, 1983·Archives of Biochemistry and Biophysics·I A SkulskiiV V Glasunov
Aug 28, 2013·BMB Reports·Donato PastoreDaniela Trono
Feb 13, 1984·FEBS Letters·I P KrasinskayaL S Yaguzhinsky
Jan 5, 2000·Bioelectrochemistry and Bioenergetics·A D de Grey

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