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Free energy change in the elementary steps of actomyosin ATPase reaction
Progress in Clinical and Biological Research
|January 1, 1989
Abstract:
We determined the rate constants of the elementary steps of actomyosin ATPase reaction, and calculated the effective free energy change in the elementary steps of ATPase reaction. It was shown that most of the free energy obtained by ATP hydrolysis is liberated in the step from the actomyosin-phosphate-ADP complex to actomyosin-ADP complex.