Enzymatic Catalysis and the Transition State Theory of Reaction Rates: Transition State Analogs

Abstract

In 1948 Pauling gave the following qualitative description of enzymatic catalysis in terms of the activated complex or transition state theory of reaction rates: "... I believe that ... the surface configuration of the enzyme is ... complementary to an unstable molecule with only transient existence—namely, the 'activated complex' for the reaction that is catalyzed by the enzyme. The mode of action of an enzyme would then be the following: the enzyme would show a small power of attraction for the substrate molecule or molecules, which would become attached to it in its active surface region. This substrate molecule, or these molecules, would then be strained by the forces of attraction to the enzyme, which would tend to deform it into the configuration of the activated complex, for which the power of attraction by the enzyme is the greatest. The activated complex would then, under the influence of ordinary thermal...