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ERIC Number: EJ829112
Record Type: Journal
Publication Date: 2008-Aug
Pages: 6
Abstractor: As Provided
Reference Count: 8
ISBN: N/A
ISSN: ISSN-0021-9584
Rapid-Equilibrium Enzyme Kinetics
Alberty, Robert A.
Journal of Chemical Education, v85 n8 p1136-1141 Aug 2008
Rapid-equilibrium rate equations for enzyme-catalyzed reactions are especially useful because if experimental data can be fit by these simpler rate equations, the Michaelis constants can be interpreted as equilibrium constants. However, for some reactions it is necessary to use the more complicated steady-state rate equations. Thermodynamics is used in rapid-equilibrium derivations to calculate the equilibrium concentrations of reactants up to the rate-determining reaction, and that means that the reactions in the mechanism have to be independent. This is quite different from steady-state treatments of mechanisms where reactions do not have to be independent. The innovation in this article is the use of half-reactions to construct complete rapid-equilibrium rate equations. Five half-reactions are described. Any forward half-reaction can be combined with any reverse half-reaction. Rapid-equilibrium rate equations are given for fifteen mechanisms of enzyme-catalyzed reactions, but more rate equations can be constructed from these five half-reactions. (Contains 2 tables.)
Division of Chemical Education of the American Chemical Society. Subscription Department, P.O. Box 1267, Bellmawr, NJ 08099-1267. Tel: 800-691-9846; Tel: 856-931-5825; Fax: 856-931-4115; e-mail: jchemed@egpp.com; Web site: http://www.jce.divched.org
Publication Type: Journal Articles; Reports - Descriptive
Education Level: N/A
Audience: N/A
Language: English
Sponsor: N/A
Authoring Institution: N/A