The rate acceleration of ATP hydrolysis by F(1)F(o)-ATP synthase is of the order of 10(11)-fold. We present a cyclic enzyme mechanism for the reaction, relate it to known F(1) X-ray structure and speculate on the linkage between enzyme reaction intermediates and subunit rotation. Next, we describe five factors known to be important in the Escherichia coli enzyme for the rate acceleration. First, the provision of substrate binding energy by residues lining the catalytic site is substantial; beta-Lys155 and beta-Arg182 are specific examples, both of which differentially support substrate MgATP versus product MgADP binding. Second, octahedral coordination of the Mg(2+) in MgATP is crucial for both catalysis and catalytic site asymmetry. The residues involved are beta-Thr156, beta-Glu185 and beta-Asp242. Third, there is stabilization of a pentacoordinate phosphorus catalytic transition state by residues beta-Lys155, beta-Arg182 and alpha-Arg376. Fourth, residue beta-Glu181 binds the substrate water and stabilizes the catalytic transition state. Fifth, there is strong positive catalytic cooperativity, with binding of MgATP at all three sites yielding the maximum rate (V(max)); the molecular basis of this factor remains to be elucidated.
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JOURNAL ARTICLE| 01 January 2000
Rate acceleration of ATP hydrolysis by F(1)F(o)-ATP synthase
A.E. Senior ,
S. Nadanaciva ,
Online Issn: 1477-9145
Print Issn: 0022-0949
© 2000 by Company of Biologists
J Exp Biol (2000) 203 (1): 35–40.
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A.E. Senior, S. Nadanaciva, J. Weber; Rate acceleration of ATP hydrolysis by F(1)F(o)-ATP synthase. J Exp Biol 1 January 2000; 203 (1): 35–40. doi: https://doi.org/10.1242/jeb.203.1.35
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