ABSTRACT
Keywords .............................................................................................. 144 References ............................................................................................. 145
8.1 QUANTUM-CHEMICAL MODELING OF THE KINETICS AND CHEMICAL MECHANISM OF THE METHYL ACETATE HYDROLYSIS IN REATIONS OF THE ENZYMATIC AND HOMOGENEOUS CATALYSIS BY CHEMO-TRYPSIN AND SERINE
8.1.1 INTRODUCTION
It has been done the quantum−chemical modeling of the methyl acetate hydrolysis reaction in the processes of enzymatic and homogeneous catalysis by chemotrypsin and serine respectively, it was shown that the structure of an active center of the chemotyrpsin taken in references is proved by our calculations. The kinetic parameters for the reactions of acyl compounds formation and also of their hydrolysis for both types of the catalysis were estimated. It was shown that the formation of acylchemotrypsin proceeds via a series of the intermediate complexes, caused by the conformation transition, which, in a great measure, caused by the hydrogen bonds of the chemotyrpsin and depend on the journey of serine active group hydrogen atom. It was established, that the stabilization of the activated complexes of the acidulating and deacidulating reactions in enzymatic and homogeneous catalysis in a great measure depends on a value of the charges of the reactive center that is indicated on the values of the kinetic parameters of such reactions. It has been calculated the thermodynamics of the elementary stages for the acidulating and deacidulating reactions.
