title: Free energy change in the elementary steps of actomyosin ATPase reaction.
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.
authors.affiliation: Department of Biology, Faculty of Science, Osaka University, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Inoue
authors.forename: T
authors.initials: T
authors.lastname: Arata
authors.forename: M
authors.initials: M
authors.lastname: Yasui
mesh_terms: 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
chemical_list: D000199:Actins; D010446:Peptide Fragments; C033025:actin subfragments; D000255:Adenosine Triphosphate; D009218:Myosins