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- W2491221427 abstract "The validity of different proposals for the origin of the catalytic power of enzymes can be explored by computer simulation approaches. In this work we use such approaches to explore the catalytic role of dynamical and non-equilibrium effects. In agreement with our previous studies it is found that dynamical effects are not so different in enzymes and solutions and therefore do not contribute significantly to catalysis. It is also found that non-equilibrium solvation effects in proteins are somewhat smaller but similar to the corresponding effects in solution. The difference is due to the fact that the reorganization free energy is smaller in proteins and this reduces both the overall barrier and the non-equilibrium barrier. This effect, however, is a part of the previously proposed catalytic role of the preorganized enzyme active site and not a new dynamical effect. It is further found that the solvent coordinate is neither frozen in the transition state of the enzyme, nor in the transition state of the corresponding solution reaction." @default.
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- W2491221427 date "1999-04-08" @default.
- W2491221427 modified "2023-10-13" @default.
- W2491221427 title "Energetics and Dynamics of Transition States of Reactions in Enzymes and Solutions" @default.
- W2491221427 doi "https://doi.org/10.1021/bk-1999-0721.ch038" @default.
- W2491221427 hasPublicationYear "1999" @default.
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