Andrew T. Torelli, Ph.D., Department of Chemistry
Research in the Torelli Lab is broadly interested in the structural and chemical basis for enzyme function. The current focus is on enzymes that biosynthesize iron-sulfur (Fe-S) clusters (Figure 1), which are essential protein cofactors involved in a wide range of enzyme functions including electron transfer (e.g. respiration, photosynthesis), environmental sensing (e.g. redox homeostasis, iron deprivation), structural stabilization of protein folds and chemical catalysis (e.g. as Lewis Acids).
While the earliest enzymes probably assimilated Fe-S clusters that formed spontaneously in the environment, the evolution of photosynthesis and subsequent oxygenation of the atmosphere depleted available environmental sources of ferrous iron ions through oxidation to insoluble ferric iron species. As a consequence, pathways emerged to biosynthesize and deliver Fe-S clusters to enzymes requiring them for their function. Research in the Torelli lab is focused on several aspects of Fe-S biosynthesis. The specific approaches encompass multiple disciplines and fall into four 'aims': 1) structural and biophysical characterization, 2) determining electrochemical properties, 3) in-vivo validation and 4) application to a disease model for Mycobacterium tuberculosis.
Undergraduate research projects may fall into one or more of the above categories providing students with broad exposure to multiple techniques that have real-world application in industry or academic research. Some examples include designing, producing and purifying mutant proteins for analysis, protein crystallization, structure determination and refinement, biophysical characterization or bacterial fitness trials.
202 Physical Sciences Laboratory Building