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Fluctuating Enzymes: Lessons from Single-Molecule Studies
Abstract
Recent single-molecule enzymology measurements with improved statistics have demonstrated that a single enzyme molecule exhibits large temporal fluctuations of the turnover rate constant at a broad range of time scales (from 1 ms to 100 s). The rate constant fluctuations, termed as dynamic disorder, are associated with fluctuations of the protein conformations observed on the same time scales. We discuss the unique information extractable from these experiments and the reconciliation of these observations with ensemble-averaged Michaelis-Menten equation. A theoretical model based on the generalized Langevin equation (GLE) treatment of Kramers' barrier crossing problem for chemical reactions accounts naturally for the observation of dynamic disorder and highly dispersed kinetics.
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Citations
Cites
Reaction-rate theory: fifty years after Kramers
Hänggi, P., Talkner, P., & Borkovec, M. (1990) · Reviews of Modern Physics · doi:10.1103/revmodphys.62.251 · Cited by 6,154
Cited by
Local force and geometry sensing regulate cell functions
Vogel, V., & Sheetz, M. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1890 · Cited by 2,328
The Moderately Efficient Enzyme: Evolutionary and Physicochemical Trends Shaping Enzyme Parameters
Bar-Even, A., Noor, E., Savir, Y., Liebermeister, W., Davidi, D., Tawfik, D. S., & Milo, R. (2011) · Biochemistry · doi:10.1021/bi2002289 · Cited by 1,050
Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
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
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
Metadata
- Authors
- Min, W., English, B. P., Luo, G., Cherayil, B. J., Kou, S. C., & Xie, X. S.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-12-01
- Volume
- 38
- Issue
- 12
- Pages
- 923-931
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2148362226
- Cited by
- 361
- References
- 1
- FWCI
- 8.41
- Type
- journal article
- Language
- en
- Open access
- closed
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