Free energy change in the elementary steps of actomyosin ATPase reaction.
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.
Inoue
A
A
Department of Biology, Faculty of Science, Osaka University, Japan.
Arata
T
T
Yasui
M
M
D000199:Actins / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D066298:In Vitro Techniques; D007700:Kinetics; D008956:Models, Chemical; D009119:Muscle Contraction / Q000502:physiology; D009132:Muscles / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D013816:Thermodynamics
D000199:Actins; D010446:Peptide Fragments; C033025:actin subfragments; D000255:Adenosine Triphosphate; D009218:Myosins