Donald Hilvert

Applied chemistry to the study of proteins with immense creativity, scholarship and success. As a postdoctoral fellow, he engineered semisynthetic flavoenzymes with unexpected redox activities. In collaboration with the Rutter lab, he also contributed to some of the earliest experiments in site-directed mutagenesis of enzymes. During his independent career he made seminal contributions to a range of interesting and challenging problems in enzymology and enzyme engineering. They include the engineering and mechanistic analysis of catalytic antibodies, selenoenzymes, naturally occurring enzymes (e.g., chorismate mutase, PLP-dependent enzymes, macrophomate synthase) and, most recently, de novo designed enzymes. In the process, with collaborators he elucidated highly illustrative concepts regarding the similarities and differences between catalysis of proton transfer, Diels-Alder cycloaddition, Claisen rearrangement, decarboxylation and aldol reactions by natural and man-made enzymes.