Transient state kinetic studies of proton liberation by myosin and subfragment 1.
Myosin and subfragment 1 give a maximum burst size of 0.25 to 0.30 protons per active site at pH 8 with ATP, alpha,beta-methylene-ATP, ADP, and adenylyl imidodiphosphate as substrates. The proton is derived from a change in conformation of the enzyme-substrate complex since it is produced by substrates which are not hydrolyzed. The rate constants for the binding of ATP and the proton release step in 0.1 M, 0.5 M, and 1.0 M KCl have been determined by analysis of the concentration dependence of the apparent rate. (see article)
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000266:Adenylyl Imidodiphosphate; D000818:Animals; D001665:Binding Sites; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009132:Muscles / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism; D009218:Myosins / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits; D013552:Swine
D000266:Adenylyl Imidodiphosphate; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D009218:Myosins