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The dynamic energy landscape of dihydrofolate reductase catalysis

Academic Article
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Overview

authors

  • Boehr, D. D.
  • McElheny, D.
  • Dyson, Jane
  • Wright, Peter

publication date

  • 2006

journal

  • Science  Journal

abstract

  • 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 transitions between ground and excited states of the intermediates. Thus, the modulation of the energy landscape by the bound ligands funnels the enzyme through its reaction cycle along a preferred kinetic path.

subject areas

  • Binding Sites
  • Catalysis
  • Escherichia coli
  • Kinetics
  • Ligands
  • Models, Molecular
  • NADP
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Binding
  • Protein Conformation
  • Tetrahydrofolate Dehydrogenase
  • Tetrahydrofolates
  • Thermodynamics
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1130258

PubMed ID

  • 16973882
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Additional Document Info

start page

  • 1638

end page

  • 1642

volume

  • 313

issue

  • 5793

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