Molecular Dynamics and Complexity in Catalysis and Biocatalysis by Marco Piumetti

Author:Marco Piumetti
Language: eng
Format: epub, pdf
ISBN: 9783030885007
Publisher: Springer International Publishing

The activated complex to which the structure [AB]‡ is assigned for the reaction

has a higher energy (enthalpy) than the reactants. If the products are more stable than the reactants, the reaction is exothermic (ƩHproducts – ƩHreactants < 0). In contrast, if the products are less stable than the reactants, the process is endothermic (ƩHproducts – ƩHreactants > 0).

The transition states of chemical reactions seem to have lifetimes near 10−13 s, which is on the order of magnitude of the time of a single bond vibration. It appears that enzymes act to stabilize transition states that lie between reactants and products and, thus, are expected to bind any inhibitor closely resembling such a transition state. Substrates and products often engage in several enzyme reactions, while the transition state has a tendency to be a characteristic of one specific enzyme.

The analysis of a unimolecular reaction is presented here. Suppose that ΔG‡ is the difference in Gibbs free energy between the transition state X‡ and the ground state X (namely, the Gibbs free energy of activation). The relationship between the Gibbs free energy change and the equilibrium constant is

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