Toward accurate barriers for enzymatic reactions: QM/MM case study on p-hydroxybenzoate hydroxylase
2008 | journal article
Jump to: Cite & Linked | Documents & Media | Details | Version history
Documents & Media
Details
- Authors
- Mata, Ricardo A. ; Werner, Hans-Joachirn; Thiel, Stefan; Thiel, Walter
- Abstract
- The hydroxylation reaction catalyzed by p-hydroxybenzoate hydroxylase has been investigated by quantum mechanical/molecular mechanical (QM/MM) calculations at different levels of QM theory. The solvated enzyme was modeled (∼23000 atoms in total, 49 QM atoms). The geometries of reactant and transition state were optimized for ten representative pathways using semiempirical (AM1) and density functional (B3LYP) methods as QM components. Single-point calculations at B3LYP/MM optimized geometries were performed with local correlation methods [LMP2, LCCSD(T0)] and augmented triple-zeta basis sets. A careful validation of the latter approach with regard to all computational parameters indicates convergence of the QM contribution to the computed barriers to within ∼1kcalmol−1. Comparison with the available experimental data supports this assessment.
- Issue Date
- 2008
- Journal
- The Journal of Chemical Physics
- ISSN
- 0021-9606
- eISSN
- 1089-7690
- Language
- English