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Steady‐state rate of F 1 ‐ATPase turnover during ATP hydrolysis by the single catalytic site
Author(s) -
Milgrom Ya.M.,
Murataliev M.B.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81557-0
Subject(s) - atp hydrolysis , hydrolysis , steady state (chemistry) , atpase , chemistry , catalysis , nucleotide , turnover number , enzyme , kinetics , stereochemistry , biochemistry , gene , physics , quantum mechanics
Under the conditions of ATP regeneration and molar excess of nucleotide‐depleted F 1 ‐ATPase the enzyme catalyses steady‐state ATP hydrolysis by the single catalytic site. Values of K m = 10 −8 M and V m = 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 F 1 ‐ATPase catalytic site is ⩽ 0.7.