名师讲座
报告题目：Second-Coordination Sphere Effects Determine the Selectivity and Kinetics of Nonheme Iron Enzymes
报告时间：2024-11-01 10:00
报告人：Prof. S. P. de Visser
曼彻斯特大学
报告地点：曾呈奎楼B311
报告摘要：
Nonheme iron enzymes are versatile enzymes that catalyze vital functions for human health and are involved in the biosynthesis of natural products and the metabolism of toxic metabolites. Many natural products catalyzed reactions start from a free amino acid that is subsequently either hydroxylated or desaturated and built in into a scaffold. These reactions are often stereo- and regiospecific, but the enzymes have been designed to perform the reaction with high selectivity and yield. To find applications in biotechnology of these reactions and understand the high selectivity and specificity a series of computational studies were performed in my group using either the QM/MM or QM cluster approach. In general, if the models are accurate reflections of the real enzyme then QM/MM and QM cluster approaches come to the same conclusions and find the same results. In this presentation, I will give examples of validating and benchmarking computational models and show how the second coordination sphere of nonheme iron dioxygenases play a crucial role into substrate and oxidant positioning and the catalytic selectivity patterns. Moreover, long-range perturbations from charged groups and dipole moments often incur a local electric field effect that guides the reactivity.
报告人简介：
S. P. de Visser，曼彻斯特大学教授，1997年获阿姆斯特丹大学博士学位，1999-2004年在耶路撒冷希伯来大学Sason Shaik教授课题组担任研究助理，随后在英国曼斯特大学从事科学研究和教育工作。S. P. de Visser教授的主要研究兴趣是理论研究金属蛋白酶及其仿生模型的结构-活性关系，迄今为止，已在Chem. Rev., Coord. Chem. Rev. JACS, Angew. Chem. Int. Ed., ACS Catal.等著名期刊上发表近300篇论文，他的工作被超过20000次，H指数为81。
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