[Theory of charge transfer enzymatic reactions]

The influence on the elementary act energy of the change in the energies of reactants solvation and their coulombic interaction due to the transfer of reaction from the aqueous to nonaqueous medium of low dielectric permittivity, particularly the enzyme globule, has been considered. A quantitative calculation of the energies has been carried out for the isotropic dielectric model taking into account the distance of reacting particles from the aqueous/nonaqueous interface. It has been shown that the transfer of the reaction into protein globule leads to a large energy gain and hence accelerates the reaction considerably. This is true in the case when the absolute charge of reactants decreases in the course of the reaction for both particles or for one of them situated further from the interface.