期刊论文

Zhang, Xinhao;Chen, Kai

英文

Journal of Organometallic Chemistry

0022-328X

2018

864

58-67

10.1016/j.jorganchem.2018.01.018

We thank Prof. R. Hille of Ohio State University, Prof. W. Thiel of Max-Planck-Institut für Kohlenforschung and Prof. O. Wiest of University of Notre Dame for helpful comments and discussions. We are grateful for the financial support from the National Natural Science Foundation of China ( 21232001 , 81501847 ), the Youth Scientific Research Foundation of Central South University of Forestry and Technology ( QJ2017005B ), and the Shenzhen STIC ( JCYJ20170412150507046 ). We thank Prof. R. Hille of Ohio State University, Prof. W. Thiel of Max-Planck-Institut f?r Kohlenforschung and Prof. O. Wiest of University of Notre Dame for helpful comments and discussions. We are grateful for the financial support from the National Natural Science Foundation of China (21232001, 81501847), the Youth Scientific Research Foundation of Central South University of Forestry and Technology (QJ2017005B), and the Shenzhen STIC (JCYJ20170412150507046).

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The xanthine oxidase (XO) family is a group of molybdenum-containing enzymes that catalyze the transfer of an oxygen atom from water to a substrate, such as xanthine or aldehyde. The proposed mechanism for the reductive half-reaction of xanthine oxidase involves nucleophilic addition of Mo-bound hydroxide to the substrate and hydride transfer from the substrate to sulfido group (Mo=S) at the molybdenum cofactor (Moco) reaction center. A DFT study of a mechanism involving the near-by glutamic acid (Glu) residue for the oxidation of several model...