Studies of the chemical steps of enzyme catalysis increasingly implicate active site compaction in the achievement of very high rate accelerations. A general model has emerged in which sampling of a protein's conformational landscape produces a subset of conformers that have become transiently optimized with regard to inter-nuclear distances and electrostatic interactions. The study of enzymatic C-H activation has been especially fruitful in this regard, given the widespread evidence for room temperature hydrogen tunneling. This talk will discuss our recent ability to link the physical parameters defining an enzyme catalyzed H-tunneling process to biophysical probes of protein motions distal to the active site. (Supported by the National Institutes of Health, GM025765)

Changing paradigms in enzyme catalysis

251st National Meeting (2016)

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