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The dependence of the rate of transhydrogenase on the value of the protonmotive force in chromatophores from photosynthetic bacteria
Author(s) -
Cotton N.P.J.,
Myatt J.F.,
Jackson J.B.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81196-1
Subject(s) - rhodobacter , chemistry , chromatophore , membrane potential , biophysics , photosynthesis , membrane , antimycin a , rhodospirillales , photochemistry , biochemistry , electron transport chain , biology , fishery , mutant , gene
In conditions where the pH gradient is negligible, the rate of the pyridine nucleotide transhydrogenase in chromatophores of Rhodobacter capsulatus has a threshold dependence on membrane potential. The relationship is similar when either antimycin or myxothiazal or carbonyl cyanide p ‐trifluoromethoxyphenylhydrazone is used to depress the membrane potential. The relationship is distorted when membrane potential is reduced by lowering the photosynthetic light intensity.