Catherine L. Drennan

Biosketch

Catherine L Drennan is a biochemist who is known for combining X-ray crystallography, electron microscopy, and other biophysical methods to “visualize” metalloenzymes in action. Drennan was born in New York City, and was raised in Riverdale, New York, followed by Tenafly, New Jersey and then Patterson, New York. She earned her AB in Chemistry from Vassar College in Poughkeepsie, NY, working with Professor Miriam Rossi. Following three years of teaching high school science and drama, she began her graduate studies at the University of Michigan, working with the late Professor Martha L. Ludwig and Professor Rowena G. Matthews. After receiving her PhD in Biological Chemistry, Drennan carried out her postdoctoral studies at Caltech in the laboratory of Professor Douglas C. Rees. She joined the faculty at the Massachusetts Institute of Technology in 1999 and is currently a Professor of Biology and Chemistry at MIT, a MacVicar Faculty Fellow, and an Investigator and Professor with the Howard Hughes Medical Institute. Drennan, a member of the American Academy of Arts and Sciences, is also known for her efforts in promoting diversity and inclusion in science.

Research Interests

The Drennan lab investigates metalloenzymes using biochemical and biophysical methods. They strive to understand how protein scaffolds are designed to harness the power of metal-based reactivity. Drennan is known for her work elucidating structures of enzymes that catalyze radical-based chemistry, including ribonucleotide reductases, glycyl radical enzymes, mononuclear iron enzymes, and radical SAM enzymes. She is also known for her studies of nickel and cobalamin-dependent enzymes that are involved in the microbial process of acetogenesis, i.e. making acetate from the greenhouse gas carbon dioxide. Her laboratory has specialized in tackling challenging structure determinations of proteins and protein complexes that are oxygen-sensitive, conformationally flexible, and transient. The Drennan lab has provided several long-awaited structures of metalloenzymes, including the first structure of class Ia ribonucleotide reductase trapped in an active state, the first structure of a class II ribonucleotide reductase, and the first structure of biotin synthase, which served to establish the “core” fold for the enormous radical SAM superfamily. The Drennan lab is also recognized for going beyond the single image of an enzyme to elucidate structures of entire enzyme pathways and to capture multiple snapshots of metalloenzymes as they proceed through their reaction cycles.