Energy‐Linked Reactions Catalyzed by the Purified ATPase Complex (F0F1) from Rhodospirillum rubrum Chromatophores

Abstract
1. The isolation of the 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′‐dicyclohexyl‐carbodiimide. 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.