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Tunneling and coupled motion in the Escherichia coli dihydrofolate reductase catalysis
R Steven Sikorski1, Lin Wang, Kelli A Markham
1Department of Chemistry, University of Iowa, Iowa City, Iowa 52242, USA.
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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