Enzyme catalysis electrostatic basis

Warshel A, Sharma PK, Kato M, Xiang Y, Liu HB, Olsson MHM (2006) Electrostatic basis for enzyme catalysis. Chem Rev 106 3210-3235... 

N4ray-Szab6, G., Fuxreiter, M., Warshel, A. (1997). Electrostatic basis of enzyme catalysis. In G. N4ray-Szab6 A. Warshel (Eds.), Computational approaches to biochemical reactivity. Dordrecht Kluwer. 

The available data support a mechanism involving catalysis by distortion in which the enzyme binds and stabilizes a transition state that is characterized by partial rotation about the C-N amide bond. The energy that is required to distort this bond out of planarity with the C=0 bond, thereby destroying the resonance stabilization of the amide linkage, is supplied by favorable transition state binding interactions between enzyme and substrate. As Lumry states (1986), mechanical distortion as a source of small-molecule reactivity is attractive as a basis for enzymatic catalysis. It is quite realistic to assume that a distorted substrate will have enhanced reactivity, either because its ground state or the activated complex for its chemical reaction or both are altered by strain and stress in the protein conformation. However, as mentioned previously, this distortion need not be the result of mechanical deformation but could also be the result of desolvation or electrostatic destabilization. In fact, the current data support contributions from all three mechanisms for distortion. 

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