【学术报告】Photoenzymatic Catalysis – Using Light to Reveal New Enzyme Functions
日期:2023-10-27 阅读:1678

主题:Photoenzymatic Catalysis – Using Light to Reveal New Enzyme Functions

报告人: Prof. Todd Hyster, Princeton University

时间:2023年10月27日(周五)15:00-16:00

地点:霞光楼200报告厅

邀请人:叶俊涛 副教授

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嘉宾介绍

Todd Hyster is a Professor of Chemistry at Princeton University. He received his B.S. in Chemistry from the University of Minnesota. He did his Ph.D. studies with Tomislav Rovis at Colorado State University. As part of his Ph.D., he was a Marie Curie Fellow with Thomas Ward at the University of Basel. He was an NIH Postdoctoral Fellow with Prof. Frances Arnold at Caltech. He started his independent career at Princeton University in 2015. He joined the faculty at Cornell from 2021-2023 before returning to Princeton. His group is focused on developing new activation modes for enzymes. He has received many awards, including Arthur C. Cope Early Career Scholar Award (2022), Amgen Young Investigator Award (2021), Junior BIOTRANs Award (2021), Eli Lilly Grantee Award (2021), NSF CAREER Award (2019).


报告摘要

Enzymes are exquisite catalysts for chemical synthesis, capable of providing unparalleled levels of chemo-, regio-, diastereo- and enantioselectivity. Unfortunately, biocatalysts are often limited to the reactivity patterns found in nature. In this talk, I will share my groups efforts to use light to expand the reactivity profile of enzymes. In our studies, we have exploited the photoexcited state of common biological cofactors, such as NADH and FMN to facilitate electron transfer to substrates bound within enzyme active sites. In other studies, we found that enzymes will electronically activate bound substrates for electron transfer. In the presence of common photoredox catalysts, this activation can be used to direct radical formation to enzyme active sites. Using these approaches, we can develop biocatalysts to solve long-standing selectivity challenges in chemical synthesis.

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