Quantum-classical simulation methods for hydrogen transfer in enzymes: a case study of dihydrofolate reductase.
A variety of theoretical approaches have been used to investigate hydrogen transfer in enzymatic reactions. The free energy barriers for hydrogen transfer in enzymes have been calculated using classical molecular dynamics simulations in conjunction with quantum mechanical/molecular mechanical and empirical valence bond potentials. Nuclear quantum effects have been included with several different approaches. Applications of these approaches to hydride transfer in dihydrofolate reductase are consistent with experimental measurements and provide significant insight into the protein conformational changes that facilitate the hydride transfer reaction.
Hammes-Schiffer
Sharon
S
Department of Chemistry, 152 Davey Laboratory, Pennsylvania State University, University Park, Pennsylvania 16802, USA. shs@chem.psu.edu
D003198:Computer Simulation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D015394:Molecular Structure; D011522:Protons; D011789:Quantum Theory; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry*
D011522:Protons; D013762:Tetrahydrofolate Dehydrogenase