In the Wilmot lab we seek to understand the structural basis of catalysis by metalloenzymes. The principle tool of our research is macromolecular X-ray crystallography, in combination with spectroscopic techniques both in the crystal and solution, kinetics, mass spectrometry and mutagenesis. We freeze trap catalytic intermediates in the crystal, which give structural "snapshots" along the reaction pathway. These are then assembled into a "movie of catalysis" at the molecular level. We work on MauG (a di-heme enzyme that is involved in the synthesis of the protein-derived cofactor, tryptophan tryptophylquinone [TTQ]); chlorite dismutase (a key enzyme in bacteria mediated chlorite breakdown in water treatment facilities); nickel homeostasis in bacteria (a potential drug target).
