[Estimation of the amount of energy transformed in the actomyosin--ATP system according to kinetics findings].

A kinetic scheme for actomyosin ATPase reaction, including two different states of the energy-rich actomyosin intermediate and different ways of its formation and decomposition, is considered. The energy, liberated in this reaction, amounts to 9 kcal. mol-1. Energy liberation is coupled with myosin head rotation. The energy-rich intermediate is stabilized by hindrances to head motion. By this mechanism the energy transduction in a filamentous actomyosin system can occur only after a dissociation act, and an ordered cyclical reaction can take place.