RESEARCH
SHINING LIGHT ON THE FIELD
OF BIOCATALYSIS
A major area of research focus in the Hyster lab features accessing non-natural enzymatic modes of reactivity through photoexcitation of redox active cofactors or cofactor/substrate complexes in proteins that are cofactor dependent. This approach provides access to enantioselective single electron pathways that are currently unmatched by small molecule organic and transition metal catalysts. We envision that this approach will unlock new synthetic pathways to a range of complex chemical structures in streamlined synthetic operations.
BIOCATALYSIS WITH A SYNTHETIC FOCUS
Our group harnesses the unique reactivity and accompanying high regio- and stereoselectivity of catalytic enzymatic processes to develop synthetically useful organic reactions. Each project is specifically chosen to address challenges in synthetic organic chemistry that are beyond the reach of classical methods. This involves capitalizing on both natural and non-natural reactivity of a myriad of enzyme classes to generate molecular scaffolds with medical and biological relevance.
IDENTIFYING CATALYTIC SYNERGY WITH PROTEIN/CATALYST HYBRIDS
Identifying protein/catalyst hybrids that together can access novel and general modes of reactivity is a major theme in our research. Capitalizing on a variety of potential surface or active site residue interactions with other small molecule or transition metal catalysts, we could overcome energy barriers that are unattainable by current synthetic methods. We envision that the development of these protein/catalyst hybrids is unlimited with the assistance of known chemical biology methods.