The analysis of enzymic free energy relationships using kinetic and computational models.
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).
Greig
Ian R
IR
Department of Chemistry, University of Bath, Bath BA2 6AS, UK. i.greig@bath.ac.uk
D055162:Biocatalysis; D004798:Enzymes / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D013816:Thermodynamics
D004798:Enzymes