Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8291933 | Archives of Biochemistry and Biophysics | 2008 | 9 Pages |
Abstract
The application of kinetic isotope effects and molecular modeling to characterize three enzyme-catalyzed reactions is presented; the mechanism of the chloroacid dehalogenase catalyzed reaction is approached using chlorine kinetic isotope effects and solvent kinetic isotope effects. The pre-steady-state phase of the reaction catalyzed by methylmalonyl-CoA mutase is approached by different QM/MM schemes and the results are validated by comparison with the experimental value of the deuterium kinetic isotope effect. Finally, a procedure for improving QM/MM calculations is illustrated by analysis of the trihydroxynaphthalene reductase-catalyzed reaction.
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Authors
Agnieszka Dybala-Defratyka, Michal Rostkowski, Piotr Paneth,