Mechanism of adenosine 5'-triphosphate cleavage by myosin: studies with oxygen-18-labeled adenosine 5'-triphosphate

Abstract
During the hydrolysis of MgATP catalyzed by myosin [rabbit skeletal muscle], ATP bound to the protein undergoes a reaction such that the .beta.-nonbridge O atoms exchange position with the .beta..gamma.-bridge O atom. The extent of this exchange was variable but averaged 45% for ATP that had been bound for 2 s at the myosin subfragment 1 active site at ionic strength 0.08 M, pH 8.0 and 22.degree. C. ATP cleavage in the myosin active site is readily reversible. The .beta.-phosphate of ADP that must be formed in this cleavage step is apparently highly constrained in the protein.

This publication has 12 references indexed in Scilit: