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Change in heat capacity accurately predicts vibrational coupling in enzyme catalyzed reactions
Author(s) -
Arcus Vickery L.,
Pudney Christopher R.
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.06.042
Subject(s) - kinetic isotope effect , chemistry , rotational–vibrational coupling , catalysis , heat capacity , thermodynamics , coupling (piping) , enzyme catalysis , reaction coordinate , substrate (aquarium) , reaction rate , reaction rate constant , kinetic energy , chemical physics , computational chemistry , kinetics , deuterium , molecule , physics , materials science , organic chemistry , atomic physics , quantum mechanics , oceanography , metallurgy , geology
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.