The dynamic energy landscape of dihydrofolate reductase catalysis.

  title={The dynamic energy landscape of dihydrofolate reductase catalysis.},
  author={David D. Boehr and Dan McElheny and H Jane Dyson and Peter E. Wright},
  volume={313 5793},
We used nuclear magnetic resonance relaxation dispersion to characterize higher energy conformational substates of Escherichia coli dihydrofolate reductase. Each intermediate in the catalytic cycle samples low-lying excited states whose conformations resemble the ground-state structures of preceding and following intermediates. Substrate and cofactor exchange occurs through these excited substates. The maximum hydride transfer and steady-state turnover rates are governed by the dynamics of… CONTINUE READING
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