Catherine L. Drennan
Board Member: 2016 -
The primary targets of research in the Drennan lab are enzymes that contain metals or metallocofactors. These metalloenzymes use the enhanced reactivity of transition metals to catalyze challenging chemical reactions including radical-based chemistry and manipulation of organometallic bonds. The lab is also interested in metalloproteins that sense changes in the cellular environment or act as redox mediators.
Dr. Drennan and her research team combine X-ray crystallography with techniques from biochemistry and biophysics to understand enzyme mechanisms. They call this approach “structural enzymology”. At the atomic scale, Dr. Drennan and her research team are interested in providing detailed three-dimensional information about these metallocofactors to help understand how protein environment modulates reactivity. At the protein scale, they are interested in seeing how enzymes are constructed to control substrate access and prevent loss of reactive intermediates or damage to expensive cofactors. At the scale of protein complexes, they want to know how proteins interact and how those interactions explain the observed behavior. Protein complexes are often large, have multiple distinct states, and can have large inter- and intrasubunit motions; therefore a single “snapshot” of their structure usually does not tell the entire story.