Title: Understanding and Harnessing Enzymatic Control Over Reactive Intermediates
Abstract: Metalloenzymes catalyze a vast assortment of kinetically and thermodynamically challenging reactions essential to primary and secondary metabolism. Their unique reactivity is enabled by a combination of metal-dependent coordination chemistry and the spatial control over reactive intermediates afforded by a protein scaffold. In this talk, I will describe the synthesis of synthetic iron-sulfur clusters and how understanding the organometallic chemistry of these clusters provides lessons for achieving selectivity in radical S-adenosylmethionine enzymes. I will additionally describe how the protein scaffold influences the selectivity of radical reactions, applied to the directed evolution of radical photoenzymes for stereoselective hydroamination reactions.
Bio: I am an Arnold O. Beckman postdoctoral fellow in Prof. Todd Hyster’s lab at Princeton University, where I am developing engineered flavin containing enzymes for selective photobiocatalytic reactivity. I carried out my PhD research with Prof. Dan Suess at MIT studying synthetic iron sulfur clusters to understand the unique structural and electronic features that enable these cofactors to perform challenging redox chemistry. My PhD research was supported by the NSF GRFP and a Fannie and John Hertz foundation fellowship. I received my Bachelor’s degree in chemistry from UC Berkeley where I worked on synthetic inorganic chemistry in in Prof. John Arnold’s lab.
Keywords: inorganic chemistry, organic chemistry, biocatalysis, coordination chemistry, enzyme catalysis
Host: Eszter Boros