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Tunneling and Coupled Motion in the Escherichia coli Dihydrofolate Reductase Catalysis
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文摘
H-transfer was studied in the complex kinetic cascade of dihydrofolate reductase. Intrinsic kinetic isotope effects, their temperature dependence, and other temperature-dependent parameters indicated H-tunneling, but no 1tities/deg.gif"> to 2tities/deg.gif"> coupled motion. The data also suggested environmentally coupled tunneling and commitment to catalysis on pre-steady-state isotope effects.

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