title: A transient kinetic study of enthalpy changes during the reaction of myosin subfragment 1 with ATP.
abstract: 1. The enthalpy changes during individual reaction steps of the myosin subfragment 1 ATPase were studied with the use of a new stopped-flow calorimeter [Howarth, Millar & Gutfreund (1987) Biochem. J. 248, 677-682]. 2. At 5 degrees C and pH 7.0, the endothermic on-enzyme ATP-cleavage step was observed directly (delta H = +64 kJ.mol-1). 3. ADP binding is accompanied by a biphasic enthalpy change. 4. The release and uptake of protons was investigated by the use of two buffers with widely different heats of ionization. 5. Protons are involved in all four principal steps of the myosin subfragment 1 ATPase.
authors.affiliation: Marine Biological Association, Plymouth, U.K.
authors.forename: N C
authors.initials: NC
authors.lastname: Millar
authors.forename: J V
authors.initials: JV
authors.lastname: Howarth
authors.forename: H
authors.initials: H
authors.lastname: Gutfreund
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D002021:Buffers; D002101:Cacodylic Acid; D006868:Hydrolysis; D007093:Imidazoles; D007700:Kinetics; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011485:Protein Binding; D011522:Protons; D013816:Thermodynamics
chemical_list: D002021:Buffers; D007093:Imidazoles; D015879:Myosin Subfragments; D010446:Peptide Fragments; D011522:Protons; D000244:Adenosine Diphosphate; C029899:imidazole; D000255:Adenosine Triphosphate; D002101:Cacodylic Acid; D009218:Myosins