Steady-state rate of F1-ATPase turnover during ATP hydrolysis by the single catalytic site
Milgrom YaM; Murataliev, M.B.
Febs Letters 212(1): 63-67
1987
ISSN/ISBN: 0014-5793 PMID: 2879744 DOI: 10.1016/0014-5793(87)81557-0
Accession: 041430963
Under the conditions of ATP regeneration and molar excess of nucleotide-depleted F1-ATPase the enzyme catalyses steady-state ATP hydrolysis by the single catalytic site. Values of Km = 10(-8) M and Vm = 0.05 s-1 for the single-site catalysis have been determined. ADP release limits single-site ATP hydrolysis under steady-state conditions. The equilibrium constant for ATP hydrolysis at the F1-ATPase catalytic site is less than or equal to 0.7.
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