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  • Title: The effect of depletion of nucleotide and of delta and epsilon subunits on ATP synthesis in dimethyl sulfoxide by F1-ATPase of Escherichia coli.
    Author: Beharry S, Bragg PD.
    Journal: Biochem Biophys Res Commun; 1993 Jul 15; 194(1):483-9. PubMed ID: 8333861.
    Abstract:
    The F1-ATPase of Escherichia coli contains 3 mol bound adenine nucleotide/mol F1. It is of the F1[2,1] type based on the ability of GTP to displace 1 mol adenine nucleotide/mol F1 (Kironde, F.A.S. and Cross, R.L. (1986) J. Biol. Chem. 261, 12544-12549). A portion of the adenine nucleotide (2 mol/mol F1) is not displaceable by GTP. F1[2,1] was converted to F1[1,0]. This form of the enzyme synthesized ATP from endogenous ADP and inorganic phosphate in a medium containing 30% (v/v) dimethyl sulfoxide (Me2SO). A delta,epsilon subunit-depleted form of the F1-ATPase was shown to be predominantly in the F1[0,1] form. ATP was not synthesized from endogenous ADP by the subunit-depleted enzyme in Me2SO unless additional molecules of ADP were bound. It is concluded that ATP synthesis from endogenous ADP in Me2SO occurs at GTP-nondisplaceable adenine nucleotide binding sites.
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