The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Use of Isotope Effects to Elucidate Enzyme Mechanism
Abstract
The chemical bond breaking steps are normally not rate limiting for enzymatic reactions. However, comparison of deuterium and tritium isotope effects on the same reaction, especially when coupled with 13C isotope effects for the same step measured with deuterated as well as unlabeled substrates, allows calculation of the intrinsic isotope effects on the bond breaking steps and thus a determination of the commitments to catalysis for the reactants. The variation in observed isotope effects as a function of reactant concentration can be used to determine kinetic mechanisms, while the pH variation of isotope effects can determine the stickiness of the reactants and which portions of the reactant mechanism are pH dependent. Finally the size of primary and secondary intrinsic isotope effects can be used to determine transition state structure.
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Cites
The Expression of Isotope Effects on Enzyme-Catalyzed Reactions
Northrop, D. B. (1981) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.50.070181.000535 · Cited by 279
Cited by
Carbon Isotopes in Photosynthesis
O'Leary, M. H. (1988) · BioScience · doi:10.2307/1310735 · Cited by 2,475
Carbon isotope effects on enzyme-catalyzed carboxylation of ribulose bisphosphate
Roeske, C. A., & O'Leary, M. H. (1984) · Biochemistry · doi:10.1021/bi00320a058 · Cited by 332
Mode of Action of Bi- and Trinuclear Zinc Hydrolases and Their Synthetic Analogues
Weston, J. (2005) · Chemical Reviews · doi:10.1021/cr020057z · Cited by 311
Metadata
- Authors
- Wallace Cleland, W.
- Venue
- Critical Reviews in Biochemistry
- Publisher
- Informa UK Limited
- Published
- 1982-01
- Volume
- 13
- Issue
- 4
- Pages
- 385-428
- ISSN
- 0045-6411 (ISSN-L)
- 1040-8355
- OpenAlex
- W1979034187
- Cited by
- 175
- References
- 1
- FWCI
- 3.82
- Type
- journal article
- Language
- en
- Open access
- closed
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