Chemical Society Seminar: David Palmer - Biocatalysis: complex catalyst, simple procedure, surprising outcomes

Abstract:

Biocatalysis has become a valuable addition to synthetic methodology, and have been embraced by the pharmaceutical industry in recent years. Enzymes can provide efficient and stereoselective transformations under mild conditions, although they are not without limitations. Our lab has studied aldolases for many years, but recently has begun exploring their utility in preparative-scale reactions. We have put an emphasis on simple and practical processes, and discovered a surprisingly diverse set of carbon-carbon bond forming reactions that can be catalyzed by a single enzyme.

Bio:

Dr. David Palmer is the Thorvaldson Professor of Chemistry at the University of Saskatchewan. He completed his B.Sc. in Chemistry at Queen's University, and stayed there for a Ph.D. in physical organic chemistry co-supervised by Dr. Greg Thatcher and Erwin Buncel. He did postdoctoral work in enzymology with Dr. John Gerlt at the University of Illinois, Urbana-Champaign, before joining the Department of Chemistry at Saskatchewan. His research program focuses on enzyme structure-function relationships, inhibitor design and synthesis, and biocatalysis. He also served as Head of Chemistry from 2010-2019, and served on NSERC Evaluation Group 1504 as section chair for organic and bioorganic chemistry. He became a Fellow of the Chemical Institute of Canada in 2022.