The analysis of enzymic free energy relationships using kinetic and computational models


Greig, I., 2010. The analysis of enzymic free energy relationships using kinetic and computational models. Chemical Society Reviews, 39 (6), pp. 2272-2301.

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Free energy relationships are a ubiquitous means of characterizing trends in rates of reaction with changing molecular structure. They may be used to quantify the extent of progress along a reaction coordinate at a reaction's transition state or alternatively the extent of similarity between a reaction's transition state and some reference transformation. This critical review outlines correlative procedures for the treatment of experimentally-determined free energy relationships with a particular focus on enzyme-catalyzed group transfers. The reasons for observed non-linearities in free energy relationships are considered. Attention is paid to the influences of changes in kinetic mechanism (e. g. general-acid catalyzed versus uncatalyzed reactions, and the competition between associative, dissociative and concerted modes of group transfer), changes in rate-determining step and the choice of an appropriate reference reaction. The relationship between experimental data and physical/theoretical models of reactivity is discussed (191 references).


Item Type Articles
CreatorsGreig, I.
DepartmentsFaculty of Science > Chemistry
ID Code19183


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