Amount and turnover rate of the F0F1-ATPase and the stoichiometry of its inhibition by oligomycin in Rhodospirillum rubrum chromatophores.
The amount of F1-ATPase in chromatophores from Rhodospirillum rubrum was determined by Western blotting using anti-RrF1 rabbit antibodies. 9.1 mmol F1 (mol bacteriochlorophyll)-1 was obtained or 14% of the total protein content of the chromatophores. The turnover rate of the F0F1-ATPase was 17 molecules ATP s-1 during synthesis, 2 molecules ATP s-1 during hydrolysis under coupled conditions with Mg2+ as the divalent cation, and 7 molecules ATP s-1 during hydrolysis in the presence of carbonyl cyanide p-trifluoromethoxyphenylhydrazone. Binding of 1 mol oligomycin/mol F0F1-ATPase was found to inhibit the activities of the enzyme completely. A single binding site was found with a Kd of approximately 2 microM.
Norling
B
B
Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, University of Stockholm, Sweden.
Strid
A
A
Tourikas
C
C
Nyrén
P
P
D000255:Adenosine Triphosphate / Q000378:metabolism; D020130:Bacterial Chromatophores / Q000201:enzymology / Q000378:metabolism*; D001429:Bacteriochlorophylls / Q000378:metabolism; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D009840:Oligomycins / Q000494:pharmacology; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D012247:Rhodospirillum rubrum
D001429:Bacteriochlorophylls; D009840:Oligomycins; D000255:Adenosine Triphosphate; D017301:Ca(2+) Mg(2+)-ATPase; D006180:Proton-Translocating ATPases