Proceedings of the National Academy of Sciences · 1978 · 491 citations · 14 references
Life SciencesBiochemistryChemistryCatalysisEnzymologyProtein BiochemistryElectrostatic Interactions In BiomoleculesElectrostatics In BiomoleculesEnzymatic CatalysisEnzyme CatalysisEnzyme StabilityTransition State StabilizationActive SitesAqueous SolvationElectrostatic Contributions To StabilityElectrostatic Effects On Protein StabilityEnzyme ElectrostaticsEnzyme Stabilization MechanismsStabilizationThermodynamics Of Enzyme Catalysis
Quantitative studies of the energetics of enzymatic reactions and the corresponding reactions in aqueous solutions indicate that charge stabilization is the most important energy contribution in enzyme catalysis. Low electrostatic stabilization in aqueous solutions is shown to be consistent with surprisingly large electrostatic stabilization effects in active sites of enzymes. This is established quantitatively by comparing the relative stabilization of the transition states of the reaction of lysozyme and the corresponding reaction is aqueous solution.
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Subtilisin. Stereochemical mechanism involving transition-state stabilization
Jon D. Robertus, Joseph Kraut, Richard A. Alden et al. · Biochemistry · 1972 · 377 citations