How Important Are Quantum Mechanical Nuclear Motions in Enzyme Catalysis?
- 1 January 1996
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 118 (47) , 11745-11751
- https://doi.org/10.1021/ja962007f
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Linear Free Energy Relationships with Quantum Mechanical Corrections: Classical and Quantum Mechanical Rate Constants for Hydride Transfer between NAD+ Analogs in SolutionsJournal of the American Chemical Society, 1995
- Simulation of enzyme reactions using valence bond force fields and other hybrid quantum/classical approachesChemical Reviews, 1993
- Free energy calculations: Applications to chemical and biochemical phenomenaChemical Reviews, 1993
- Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase IIIBiochemistry, 1993
- A quantized classical path approach for calculations of quantum mechanical rate constantsThe Journal of Physical Chemistry, 1993
- Computer simulation of the initial proton transfer step in human carbonic anhydrase IJournal of Molecular Biology, 1992
- Simulations of quantum mechanical corrections for rate constants of hydride-transfer reactions in enzymes and solutionsThe Journal of Physical Chemistry, 1991
- Quantum corrections for rate constants of diabatic and adiabatic reactions in solutionsThe Journal of Chemical Physics, 1990
- Rigorous formulation of quantum transition state theory and its dynamical correctionsThe Journal of Chemical Physics, 1989
- Imaginary time path integral Monte Carlo route to rate coefficients for nonadiabatic barrier crossingThe Journal of Chemical Physics, 1987