title: Protein's electronic polarization contributes significantly to its catalytic function.
abstract: Ab initio quantum mechanical/molecular mechanical method is combined with the polarized protein-specific charge to study the chemical reactions catalyzed by protein enzymes. Significant improvement in the accuracy and efficiency of free-energy simulation is demonstrated by calculating the free-energy profile of the primary proton transfer reaction in triosephosphate isomerase. Quantitative agreement with experimental results is achieved. Our simulation results indicate that electronic polarization makes important contribution to enzyme catalysis by lowering the energy barrier by as much as 3 kcal/mol.
authors.affiliation: State Key Laboratory of Precision Spectroscopy and Department of Physics, Institute of Theoretical and Computational Science, East China Normal University, Shanghai 200062, China. yxiang@phy.ecnu.edu.cn
authors.forename: Yun
authors.initials: Y
authors.lastname: Xiang
authors.forename: Lili
authors.initials: L
authors.lastname: Duan
authors.forename: John Z H
authors.initials: JZ
authors.lastname: Zhang
mesh_terms: D055162:Biocatalysis; D004583:Electrons; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D011789:Quantum Theory
chemical_list: D004798:Enzymes