Tunneling and Coupled Motion in the Escherichia coli Dihydrofolate Reductase Catalysis
Journal of the American Chemical Society2004Vol. 126(15), pp. 4778–4779
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Renatus Sikorski, Lin Wang, Kelli A Markham, P. T. Ravi Rajagopalan, Stephen J. Benkovic, Amnon Kohen
Abstract
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 1 degrees to 2 degrees coupled motion. The data also suggested environmentally coupled tunneling and commitment to catalysis on pre-steady-state isotope effects.
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