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• W2012024256 abstract "Everted membrane vesicles of the Gram-positive eubacterium Streptomyces lividans were prepared and the ATP synthase (F 1 F o ) was characterized in its membrane-bound form. In addition, the F 1 F o complex was solubilized, purified, and functionally reconstituted into phospholipid vesicles. The enzyme complex is similar with respect to subunit composition to those of other eubacterial ATP synthases. Whereas the F 1 part only exhibits ATPase activity in the presence of CaCl 2 (Hensel, M., Deckers-Hebestreit, G. and Altendorf, K. (1991) Eur. J. Biochem. 202, 1313–1319), the membrane-bound ATPase is also moderately stimulated by high concentrations of Mg 2+ ions (20 mM). In contrast, the physiological functions of the ATP synthase, i.e., ATP-driven H + translocation and ATP synthesis are strictly dependent on Mg 2+ ions. The biochemical properties of the ATP synthase of S. lividans show distinct similarity to the enzyme complex of rhodobacteria and bacilli. The ATPase activity is inhibited by N , N ′-dicyclohexylcarbodiimide, venturicidin, and tributyltin, typical inhibitors of F 1 F o -ATPases, which react with the membrane-bound F o complex. In addition, the ATPase activity is highly sensitive towards oligomycin, a feature which is only shared by the ATP synthase of rhodobacteria and mitochondria." @default.
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• W2012024256 date "1996-06-01" @default.
• W2012024256 modified "2023-09-29" @default.
• W2012024256 title "The ATP synthase of Streptomyces lividans: characterization and purification of the F1Fo complex" @default.
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• W2012024256 doi "https://doi.org/10.1016/0005-2728(96)00003-5" @default.
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