Evaluating substrate specificity of glutathione peroxidase mimic by molecular dynamics simulations and kinetics |
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| Authors: | Shao-Wu Lv Qing-Chuan Zheng Ying Mu Xiao-Guang Wang Yue-Tong Ji Gui-Min Luo Jun-Qiu Liu Jia-Cong Shen |
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| Affiliation: | (1) Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, 2519 Jiefang Road, Changchun, 130021, P.R. China;(2) State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun, 130023, P.R. China;(3) Key Laboratory for Supramolecular Structure and Materials of the Ministry of Education, Jilin University, Changchun, 130012, P.R. China |
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| Abstract: | The substrate specificities of glutathione peroxidase (GPX) mimic, 6,6′-ditellurobis(6-deoxy-β-cyclodextrin) (6-TeCD), for three hydroperoxides (ROOH), H2O2, tert-butyl hydroperoxide (t-BuOOH) and cumene hydroperoxide (CuOOH), are investigated through molecular dynamics (MD) simulations. The most stable conformations and the total interaction energies of complex of 6-TeCD with ROOH are used to evaluate the substrate specificity of 6-TeCD. The steady-state kinetics of 6-TeCD is studied and the Michaelis-Menten constant (K m) and second-order rate constant k max/K ROOH show that 6-TeCD displays different affinity and specificity to ROOH. These results of experiments are well consistent with ones obtained by MD simulations, indicating that MD simulations could be applied to evaluation substrate specificity of small-molecule enzyme mimics. |
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| Keywords: | Glutathione peroxidase Enzyme mimic Substrate specificity Molecular dynamics simulations Kinetics |
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