John T. Groves
Princeton University
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Primary Section: 14, Chemistry Secondary Section: 21, Biochemistry Membership Type:
Member
(elected 2012)
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Research Interests
Using a variety of spectroscopic, kinetic and molecular probes, Groves studies mechanisms of oxygen activation in metalloenzymes. Small molecule models of redox enzyme active sites are also studied by the same techniques. He and his laboratory were the first to prepare and characterized high-valent metalloporphyrin complexes with oxo ligands. Such species are now recognized as the key reactive intermediates formed during drug metabolism by cytochrome P450 enzymes and more generally in the conversion of oxygen to water during respiration. Novel heme-contaiing enzymes of fungal origin have been shown react in ways that are similar to human P450 proteins. Recently, Groves and his group have devised a new method to incorporate fluorine into unreactive C-H bonds using manganese porphyrin catalysts. Current interests include how such aliphatic fluorination reactions may be useful for the creation of a new generation of drug molecules and molecular probes for positron emission imaging applied to medical applications.
