Investigating Metal Identity and Active Site Details in Metalloproteins Using Combined Structural and Spectroscopic Approaches

Metals in proteins enable a range of chemical functionality due to different redox states, electronic structures, and coordination environments, empowering an expansive breadth of biomolecular reactivity. This talk will highlight several research projects in the Bowman Lab on metalloprotein biology and the methods available to interrogate how structure contributes to their unique chemistry. Metals in proteins are ubiquitous, involving up to 50% of the proteome, and involved in many of the reactions that define life, from transfer of energy and photosynthesis to metabolism and response to reactive species. In structural research, X-ray and electron sources used in diffraction and CryoEM studies can cause radiation damage, which is often exacerbated in metalloproteins. Additionally, changes in metal oxidation state can occur with standard structural methods. We are working to address this gap in available methods for studying metal-containing chemical biology systems with structural techniques by developing ways to couple spectroscopic tools for probing metal centers to structural tools for structure determination.