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lüll Environmentally coupled hydrogen tunneling Linking catalysis to dynamics Knapp MJ; Klinman JPEur J Biochem 2002[Jul]; 269 (13): 3113-21Many biological C-H activation reactions exhibit nonclassical kinetic isotope effects (KIEs). These nonclassical KIEs are too large (kH/kD > 7) and/or exhibit unusual temperature dependence such that the Arrhenius prefactor KIEs (AH/AD) fall outside of the semiclassical range near unity. The focus of this minireview is to discuss such KIEs within the context of the environmentally coupled hydrogen tunneling model. Full tunneling models of hydrogen transfer assume that protein or solvent fluctuations generate a reactive configuration along the classical, heavy-atom coordinate, from which the hydrogen transfers via nuclear tunneling. Environmentally coupled tunneling also invokes an environmental vibration (gating) that modulates the tunneling barrier, leading to a temperature-dependent KIE. These properties directly link enzyme fluctuations to the reaction coordinate for hydrogen transfer, making a quantum view of hydrogen transfer necessarily a dynamic view of catalysis. The environmentally coupled hydrogen tunneling model leads to a range of magnitudes of KIEs, which reflect the tunneling barrier, and a range of AH/AD values, which reflect the extent to which gating modulates hydrogen transfer. Gating is the primary determinant of the temperature dependence of the KIE within this model, providing insight into the importance of this motion in modulating the reaction coordinate. The potential use of variable temperature KIEs as a direct probe of coupling between environmental dynamics and the reaction coordinate is described. The evolution from application of a tunneling correction to a full tunneling model in enzymatic H transfer reactions is discussed in the context of a thermophilic alcohol dehydrogenase and soybean lipoxygenase-1.|*Catalysis[MESH]|*Hydrogen[MESH]|Alcohol Dehydrogenase/chemistry/metabolism[MESH]|Chemistry, Physical/methods[MESH]|Enzymes/*chemistry/metabolism[MESH]|Glycine max/enzymology[MESH]|Isotopes[MESH]|Kinetics[MESH]|Lipoxygenase/chemistry/metabolism[MESH]|Proteins/*chemistry/metabolism[MESH]|Temperature[MESH] |