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F 0 F 1 ‐ATPase from Vibrio alginolyticus Subunit composition and proton pumping activity
Author(s) -
Dmitriev O.Yu.,
Krasnoselskaya I.A.,
Papa S.,
Skulachev V.P.
Publication year - 1991
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(91)80702-5
Subject(s) - vibrio alginolyticus , protein subunit , atpase , chemistry , membrane , ammonium , proton , vibrio , biochemistry , stereochemistry , biology , bacteria , enzyme , physics , organic chemistry , genetics , gene , quantum mechanics
An F 0 F 1 ‐ATPase was isolated from the membranes of the marine bacterium Vibrio alginolyticus . Homology between the subunits of the F 0 ‐complexes from E. coli and V. alginolyticus was found using antibodies against subunits a , b and c of the E. coli F 0 F 1 ‐ATPase. The F 0 F 1 ‐complex from V. alginolyticus was reconstituted into proteoliposomes, which were competent in ATP‐dependent proton uptake. This process was inhibited by triphenyltin, DCCD, and venturicidin. Na + did not affect proton translocation.