Hydrogen tunneling and protein motion in enzyme reactions.
Theoretical perspectives on hydrogen transfer reactions in enzymes are presented. The proton-coupled electron transfer reaction catalyzed by soybean lipoxygenase and the hydride transfer reaction catalyzed by dihydrofolate reductase are discussed. The first reaction is nonadiabatic and involves two distinct electronic states, while the second reaction is predominantly adiabatic and occurs on the electronic ground state. Theoretical studies indicate that hydrogen tunneling and protein motion play significant roles in both reactions. In both cases, the proton donor-acceptor distance decreases relative to its equilibrium value to enable efficient hydrogen tunneling. Equilibrium thermal motions of the protein lead to conformational changes that facilitate hydrogen transfer, but the nonequilibrium dynamical aspects of these motions have negligible impact.
Department of Chemistry, 104 Chemistry Building, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Sharon
S
Hammes-Schiffer
D003903:Deuterium; D004579:Electron Transport; D006859:Hydrogen / Q000737:chemistry*; D007700:Kinetics; D008084:Lipoxygenase / Q000737:chemistry; D008958:Models, Molecular; D008962:Models, Theoretical; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D011522:Protons; D013025:Glycine max / Q000201:enzymology; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry; D013816:Thermodynamics
D011506:Proteins; D011522:Protons; D006859:Hydrogen; D003903:Deuterium; D008084:Lipoxygenase; D013762:Tetrahydrofolate Dehydrogenase