Change in heat capacity accurately predicts vibrational coupling in enzyme catalyzed reactions

Vickery L Arcus, Christopher R Pudney

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The temperature dependence of kinetic isotope effects (KIEs) have been used to infer the vibrational coupling of the protein and or substrate to the reaction coordinate, particularly in enzyme-catalyzed hydrogen transfer reactions. We find that a new model for the temperature dependence of experimentally determined observed rate constants (macromolecular rate theory, MMRT) is able to accurately predict the occurrence of vibrational coupling, even where the temperature dependence of the KIE fails. This model, that incorporates the change in heat capacity for enzyme catalysis, demonstrates remarkable consistency with both experiment and theory and in many respects is more robust than models used at present.

Original languageEnglish
Pages (from-to)2200-2206
Number of pages7
JournalFEBS Letters
Volume589
Issue number17
Early online date11 Jul 2015
DOIs
Publication statusPublished - 4 Aug 2015

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Specific heat
Hot Temperature
Isotopes
Temperature
Enzymes
Kinetics
Catalysis
Hydrogen
Rate constants
Substrates
Proteins
Experiments

Cite this

Change in heat capacity accurately predicts vibrational coupling in enzyme catalyzed reactions. / Arcus, Vickery L; Pudney, Christopher R.

In: FEBS Letters, Vol. 589, No. 17, 04.08.2015, p. 2200-2206.

Research output: Contribution to journalArticle

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