In our laboratory, research efforts are directed towards understanding how gas sensing occurs at a metal center, and how changes in the coordination chemistry at the metal center are coupled to allosteric conformational changes in the protein. The interaction of gas molecules with a heme center induces changes in the coordination geometry, and these changes correlate with functional changes in the protein. Our current work aims to elucidate the mechanisms by which the coordination changes are communicated through the protein, resulting in global structural changes. To this end we study several bacterial gas-responsive transcription factors and newly discovered types of heme-containing gas sensors that regulate circadian rhythm in higher organisms.


Another project investigates the role of heme in the enzyme cystathionine-beta-synthase (CBS). CBS is a critical enzyme that regulates sulfur amino acid metabolism, and this protein is the site of disease-causing mutations. We study the effect of these mutations on the biochemistry of the enzyme as a tool to understand how this unusual enzyme uses its heme.


Click on each protein to learn more about specific projects or on the heme molecule to learn about the techniques we use to study these proteins