[Energy conversion of the phosphate bond in the actomyosin-ATP system, accompanied by acceleration of myosin adenosine triphospatase].

A possible mechanism of the active motion ("tilt") of the actin-bound myosin head in ATP hydrolysis reaction is considered. This motion is considered. This motion can be goverened by actinmyosin affinity changes at two sites located on the head. Such an affinity change is assumed to take place already in the macroergic myosin (M) -products (P) complex MP. Then at a contact with actin a tilting force is generated, and the M energy liberation, coupled with the head ratation, goes on with a concomitant potential barrier lowering and corresponding acceleration of the MP destruction. In this way a destruction. In this way a decrease of free energy with a change of the head orientation is equivalent to the energy liberated, which amounts to 9 kcal.mol-1.