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Tunneling and Coupled Motion in the Escherichia coli Dihydrofolate Reductase Catalysis
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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Citations
Cited by
An NMR Perspective on Enzyme Dynamics
Boehr, D. D., Dyson, H. J., & Wright, P. E. (2006) · Chemical Reviews · doi:10.1021/cr050312q · Cited by 458
Mechanisms and Free Energies of Enzymatic Reactions
Gao, J., Ma, S., Major, D. T., Nam, K., Pu, J., & Truhlar, D. G. (2006) · Chemical Reviews · doi:10.1021/cr050293k · Cited by 401
Taking Ockham's razor to enzyme dynamics and catalysis
Glowacki, D. R., Harvey, J. N., & Mulholland, A. J. (2012) · Nature Chemistry · doi:10.1038/nchem.1244 · Cited by 232
Nuclear quantum tunnelling in enzymatic reactions – an enzymologist's perspective
Johannissen, L. O., Hay, S., & Scrutton, N. S. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp00614g · Cited by 22
What are the signatures of tunnelling in enzyme-catalysed reactions?
Johannissen, L. O., Iorgu, A. I., Scrutton, N. S., & Hay, S. (2020) · Faraday Discussions · doi:10.1039/c9fd00044e · Cited by 12
Metadata
- Authors
- Sikorski, R. S., Wang, L., Markham, K. A., Rajagopalan, P. T. R., Benkovic, S. J., & Kohen, A.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2004-03-26
- Volume
- 126
- Issue
- 15
- Pages
- 4778-4779
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2064187591
- Cited by
- 191
- References
- 0
- FWCI
- 9.96
- Type
- journal article
- Language
- en
- Open access
- closed
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- Sikorski, R. S., Wang, L., Markham, K. A., Rajagopalan, P. T. R., Benkovic, S. J., & Kohen, A. (2004). Tunneling and Coupled Motion in the Escherichia coli Dihydrofolate Reductase Catalysis. Journal of the American Chemical Society. https://doi.org/10.1021/ja031683w
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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