Steady-state rate of F1-ATPase turnover during ATP hydrolysis by the single catalytic site |
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Authors: | A Robinson B Austen |
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Institution: | A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, 119899 Moscow, USSR |
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Abstract: | 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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