Energy-linked reactions catalyzed by the purified ATPase complex (F0F1) from Rhodospirillum rubrum chromatophores.
1. The isolation of F0F1-ATPase complex from Rhodospirillum rubrum chromatophores by the use of taurodeoxycholate is described. 2. The enzyme preparation contains about 12 polypeptides; five are subunits of the F1 moiety. 3. The ATPase activity of the purified enzyme is dependent on the addition of phospholipids. 4. Km-vales for Mg2+-ATP and Ca2+-ATP are similar to the values obtained for the membrane-bound enzyme. 5. The F0F1-ATPase complex is more than 70% inhibited by oligomycin and N,N'-dicyclohexylcarbodiimide. 6. The F0F1-ATPase complex was integrated into liposomes. The reconstituted proteoliposomes catalyzed energy transduction as shown by ATP-dependent quenching of acridine dye fluorescence and ATP-32Pi exchange.
D000251:Adenosine Triphosphatases / Q000302:isolation & purification / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D020130:Bacterial Chromatophores / Q000201:enzymology; D002474:Cell-Free System; D005453:Fluorescence; D008081:Liposomes; D046911:Macromolecular Substances; D008563:Membrane Lipids / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008970:Molecular Weight; D012247:Rhodospirillum rubrum / Q000201:enzymology*; D012995:Solubility; D014475:Uncoupling Agents / Q000494:pharmacology
D008081:Liposomes; D046911:Macromolecular Substances; D008563:Membrane Lipids; D008565:Membrane Proteins; D014475:Uncoupling Agents; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases