Dr. Todd Hyster will be awarded the ENY-ACS Buck-Whitney Award for 2022. He will speak at our March 16 meeting.
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 are able to develop biocatalysts to solve long-standing selectivity challenges in chemical synthesis.
Todd is a native of Apple Valley, Minnesota, and did his undergraduate studies at the University of Minnesota. In 2008 he joined Tomislav Rovis’ group at Colorado State University for his graduate studies to develop Rhodium-catalyzed C–H activation reactions. During his Ph.D., Todd did an internship with Thomas Ward at the University of Basel where he prepared an artificial metalloenzyme for an asymmetric C–H activation reaction. After graduating, he joined the group of Frances Arnold at Caltech as an NIH Postdoctoral Fellow. In the Arnold group, Todd evolved P450s to catalyze nitrene transfer reactions. In 2015 he started his independent career at Princeton University and in 2021 moved to Cornell University, where he is currently an Associate Professor of Chemistry and Chemical Biology. Todd’s group has developed photochemical strategies to expand the synthetic utility of common enzymes, enabling them to address long-standing selectivity challenges in the chemical synthesis literature.