Chemical origins of enzymic catalysis

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I have developed a general approach to predicting rate constants for chemical reactions from the corresponding equilibrium constants. This requires no kinetic information and generally requires only relatively low levels of MO theory to calculate distortion energies. The key assumption in my approach is that if only one thing happens to a molecule (geometry change with no change in bonding or bonding change with no change in geometry) then the energy is a quadratic function of a suitable reaction coordinate. The kinetic barrier (intrinsic barrier) for a real reaction arises from the need for more than one thing to happen for a real chemical transformation. This approach has been very successful in tests to date, both published and still in progress.     The goal of my research program is to test this approach over the widest possible range of reactions, inorganic as well as organic, and to develop and make available software which will make it easy for others to apply the method. Not only does the method allow prediction of rates of reaction, it also provides a general mechanistic criterion by allowing a clear test of whether or not a proposed mechanism is compatible with the observed rate constant. Furthermore the approach has value as a qualitative way of thinking about reactions as well as for quantitative predictions. Important near term goals are to extend this approach to intramolecular reactions and to test it in a range of solvents. Ultimately it is hoped that the method can be applied to explaining the rate enhancements in enzyme catalyzed reactions, which continue to represent the largest unsolved set of problems facing physical organic chemistry.