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High‐Accuracy Computation of Reaction Barriers in Enzymes
Author(s) -
Claeyssens Frederik,
Harvey Jeremy N.,
Manby Frederick R.,
Mata Ricardo A.,
Mulholland Adrian J.,
Ranaghan Kara E.,
Schütz Martin,
Thiel Stephan,
Thiel Walter,
Werner HansJoachim
Publication year - 2006
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200602711
Subject(s) - chorismate mutase , yield (engineering) , computational chemistry , computation , reactivity (psychology) , enzyme , chemistry , ab initio , catalysis , enzyme catalysis , materials science , thermodynamics , organic chemistry , physics , computer science , biosynthesis , medicine , alternative medicine , algorithm , pathology
Modeling enzyme catalysis: High‐level ab initio QM/MM calculations yield activation enthalpies and free energies for chorismate mutase and para ‐hydroxybenzoate hydroxylase that are in excellent agreement with experimental results. Enzyme reactivity is described quantitatively by transition‐state theory.