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Thermodynamic Property Values for Enzyme-catalyzed Reactions

Published

Author(s)

Robert N. Goldberg

Abstract

This chapter deals with how one can obtain values of thermodynamic properties specifically the apparent equilibrium constant K, the standard molar transformed Gibbs energy change rG, and the standard molar transformed enthalpy change rH for biochemical reactions and, in particular, for enzyme-catalyzed reactions.  In addition to direct measurement, these property values can be obtained in a variety of ways:  from thermochemical cycle calculations; from tables of standard molar formation properties; by estimation from property values for a chemically similar reaction or substance; by means of estimation by using a group-contribution method; by combining a known value of the standard molar enthalpy change rH and an estimated value for the standard molar entropy change rS in order to obtain the standard molar Gibbs energy change rG for a given reaction; and by use of computational chemistry.  
Citation
Proceedings of the 3rd International Beilstein Workshop on Experimental Standard Conditions of Enzyme Characterizations

Keywords

Apparent equilibrium constant, enthalpy, enzyme-catalyzed reactions, heat capacity, thermodynamics

Citation

Goldberg, R. (2008), Thermodynamic Property Values for Enzyme-catalyzed Reactions, Proceedings of the 3rd International Beilstein Workshop on Experimental Standard Conditions of Enzyme Characterizations (Accessed March 1, 2024)
Created August 20, 2008, Updated February 17, 2017