Uncouplers can shuttle between localized energy-coupling sites during photophosphorylation by chromatophores of Rhodopseudomonas capsulata N22

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

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 tran...

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Role of photophosphorylation coupling factor in energy conversion by depleted chromatophores of Rhodospirillum rubrum.

Rhodospirillum rubrum chromatophores depleted of photophosphorylation coupling factor lost more than 95% of their phosphorylation activity in every tested phosphorylating system including the endogenous as well as the N-methylphenazonium methosulfate-supported systems. Full restoration of photophosphorylation in all tested systems was obtained by preincubating depleted chromatophores in the pre...

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Genetic recombination in Rhodopseudomonas capsulata.

A system for genetic exchange in Rhodopseudomonas capsulata has been discovered. Each genetic marker thus far examined can be transferred, and many strains of Rps. capsulata can participate in genetic exchange. The mechanism of gene transfer seems unlike that of any previously described bacterial system, since genes can be transferred by cell-free filtrates, but the vector is resistant to deoxy...

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Regulation o f nitrogenase activity in Rhodopseudomonas capsulata AD 2 differs in several respects from other Rhodospirillaceae: 1) Nitrogenase activity in this strain grown under severe N-starvation was fully derepressed, but in contrast to other Rhodospirillaceae, it was inhibited by am m onia in vivo. 2) Nitrogenase in extracts o f glutamate grown cells was fully active and not further stimu...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1983

ISSN: 0264-6021

DOI: 10.1042/bj2120025