Part I: Introduction to Metalloproteins
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Dr. Drennan begins her lecture by explaining what metalloproteins are and how the inclusion of a metal in the protein structure results in amazingly reactive proteins. She describes techniques, such as X-ray crystallography and electron microscopy, which her group uses to get “snapshots” of metalloproteins in action. These “snapshots” allow them to better understand how metalloproteins function in many critical biological reactions.
In Part 2, Drennan focuses on experiments her lab has done to understand the mechanism of action of ribonucleotide reductase (RNR), a key enzyme required for DNA synthesis and repair and, consequently, cell viability. By taking “snapshots” of bacterial RNR, Drennan and her colleagues deciphered how changes in the structure of RNR regulated its activity. Interestingly, the structure of bacterial RNR appears to differ from that of human RNR suggesting a possible new target for antibiotics.
In the last part of her talk, Drennan explains how cobalt based metalloproteins allow acetogenic bacteria to live on CO2. This group of bacteria convert more than 1010 tons of CO2 to acetate each year and scientists are interested in understanding and using these metalloproteins to remove CO2 from the atmosphere. Structures determined by Drennan’s lab have provided information on the mechanism of action of these important enzymes.
Cathy Drennan is a Professor of Chemistry and Biology at the Massachusetts Institute of Technology and a Professor and Investigator of the Howard Hughes Medical Institute. She studied chemistry as an undergraduate at Vassar College, received her PhD in biological chemistry from the University of Michigan, was a post-doc at the California Institute of Technology and in 1999, Drennan joined the faculty at MIT. Her lab uses X-ray crystallography and other techniques to study the structure and function of metalloproteins.
Drennan is also very involved in efforts to make chemistry education more exciting for students; perhaps due, in part, to time she spent as a high school science and drama teacher after college. Drennan helps to train graduate student teaching assistants and to develop free resources for educators. She has been recognized with several awards for excellence in undergraduate teaching, as well as outstanding research.
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For Part 2
Brignole EJ, Ando N, Zimanyi CM, Drennan CL. (2013) The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years. Biochemical Society Transactions40 523–530. Review.
Full text online.
Ando N, Brignole EJ, Zimanyi CM, Funk MA, Yokoyama K, Asturias FJ, Stubbe J, Drennan CL. (2011) Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase. Proc. Natl. Acad. Sci. U.S.A. 108, 21046-21051.
Zimanyi CM, Ando N, Brignole EJ, Asturias FJ, Stubbe J, Drennan CL. (2012) Tangled Up in Knots: Structures of Inactivated Forms of E. coli Class Ia Ribonucleotide Reductase. Structure. 20 (8), 1374-1383.
For Part 3
Kung Y and Drennan CL. (2011) A Role for Nickel-Iron Cofactors in Biological Carbon Monoxide and Carbon Dioxide Utilization. Curr. Opin. Biol. Chem. 15, 276-283.
Kung Y, Ando N, Doukov TI, Blasiak LC, Bender G, Seravalli J, Ragsdale SW, and Drennan CL. (2012) Visualizing molecular juggling within a B12-dependent methyltransferase complex. Nature 48, 265-269.