SAM
Coordination of SAM to the unique site of the site-differentiated radical SAM cluster.

Metalloenzymes catalyze remarkably diverse and sometimes extremely difficult reactions in biological systems. The theme of our research is the use of biochemical, spectroscopic, and synthetic approaches to elucidate detailed chemical mechanisms for some of nature's metal catalysts. A central theme in our group is the detailed chemical mechanism of radical generation by the Fe/S-S-adenosylmethionine (the so-called radical SAM) superfamily of enzymes. These enzymes span a remarkably diverse range of reactions and are represented across the phylogenetic kingdom with hundreds of radical SAM enzymes identified. The widespread occurrence of these enzymes throughout biology, from bacteria to humans, is indicative of the significance of the chemistry catalyzed by these enzymes, and may represent one of the most ancient and widespread biological means to carry out radical-based chemistry.

Areas of Research

Pyruvate Formate Lyase-Activating Enzyme

Pyruvate Formate Lyase-Activating Enzyme

Hydrogenase

Hydrogenase

Spore Photoproduct Lyase

Spore Photoproduct Lyase

Desulfitobacteria Bioremediation

Desulfitobacteria Bioremediation

Radical SAM and Astrobiology

Radical SAM and Astrobiology