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Cited by 957

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis

Boehr, David D., McElheny, Dan, Dyson, H. Jane, Wright, Peter E.·2006·Science

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.

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Metadata

Authors
Boehr, D. D., McElheny, D., Dyson, H. J., & Wright, P. E.
Venue
Science
Published
2006-09-15
Volume
313
Issue
5793
Pages
1638-1642
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2083144176
Cited by
957
References
1
FWCI
22.72
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis. https://app.cochat.ai/papers/10.1126/science.1130258
The paper
Boehr, D. D., McElheny, D., Dyson, H. J., & Wright, P. E. (2006). The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis. Science. https://doi.org/10.1126/science.1130258

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.