Localization and possible role of an adenosine triphosphatase in Chlorobium thiosulfatophilum.
1. Evidence is presented that the ATPase activity detected in cell extracts of Chlorobium thiosulfatophilum is bound to the cytoplasmic membrane rather than to the chlorobium vesicles. 2. The activity of this ATPase is inhibited in vitro by various carbodiimides, phloridzin and sodium azide. 3. The apparent Km for ATP is approximately 0.2 mM and the enzyme shows product inhibition by ADP. 4. Photophosphorylation, characterized in vivo, is inhibited by many of the compounds that inhibit the ATPase.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D001419:Bacteria / Q000187:drug effects / Q000201:enzymology*; D002234:Carbodiimides / Q000494:pharmacology; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology; D004140:Dinitrophenols / Q000494:pharmacology; D004579:Electron Transport; D007700:Kinetics; D008027:Light; D010785:Photophosphorylation / Q000187:drug effects; D011804:Quinolines / Q000494:pharmacology; D013347:Subcellular Fractions / Q000201:enzymology
D002234:Carbodiimides; D004140:Dinitrophenols; D011804:Quinolines; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases