Catherine Drennan

Catherine Drennan

Professor of Biology and Chemistry; Investigator and Professor, Howard Hughes Medical Institute; Undergraduate Officer

Catherine Drennan takes “snapshots” of metalloenzymes using crystallography and/or cryo-electron microscopy.

617-253-5622

Phone

68-680

Office

cdrennan@mit.edu

Email

Lab Website

Education

  • PhD,1995, University of Michigan
  • BS, 1985, Chemistry, Vassar College

Research Summary

We use X-ray crystallography to investigate the structure and function of enzymes that are medically important in environmental remediation. We are particularly interested in metalloprotein biochemistry, and in the role of conformational change in catalysis.

Awards

  • American Society for Biochemistry and Molecular Biology, Fellow, 2021
  • American Academy of Arts and Sciences, Member, 2020
  • Dorothy Crowfoot Hodgkin Award, Protein Society, 2020
  • Margaret MacVicar Faculty Fellow, 2015-2025
  • Howard Hughes Medical Institute, HHMI Investigator, 2008
  • Howard Hughes Medical Institute, HHMI Professor, 2006

Recent Publications

  1. The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes. Vaccaro, FA, Drennan, CL. 2022. Metallomics , .
    doi: 10.1093/mtomcs/mfac030PMID:35485745
  2. The Atypical Cobalamin-Dependent S-Adenosyl-l-Methionine Nonradical Methylase TsrM and Its Radical Counterparts. Ulrich, EC, Drennan, CL. 2022. J Am Chem Soc 144, 5673-5684.
    doi: 10.1021/jacs.1c12064PMID:35344653
  3. Visualizing the gas channel of a monofunctional carbon monoxide dehydrogenase. Biester, A, Dementin, S, Drennan, CL. 2022. J Inorg Biochem 230, 111774.
    doi: 10.1016/j.jinorgbio.2022.111774PMID:35278753
  4. XFEL serial crystallography reveals the room temperature structure of methyl-coenzyme M reductase. Ohmer, CJ, Dasgupta, M, Patwardhan, A, Bogacz, I, Kaminsky, C, Doyle, MD, Chen, PY, Keable, SM, Makita, H, Simon, PS et al.. 2022. J Inorg Biochem 230, 111768.
    doi: 10.1016/j.jinorgbio.2022.111768PMID:35202981
  5. Ribonucleotide reductase, a novel drug target for gonorrhea. Narasimhan, J, Letinski, S, Jung, SP, Gerasyuto, A, Wang, J, Arnold, M, Chen, G, Hedrick, J, Dumble, M, Ravichandran, K et al.. 2022. Elife 11, .
    doi: 10.7554/eLife.67447PMID:35137690
  6. Effects of chameleon dispense-to-plunge speed on particle concentration, complex formation, and final resolution: A case study using the Neisseria gonorrhoeae ribonucleotide reductase inactive complex. Levitz, TS, Brignole, EJ, Fong, I, Darrow, MC, Drennan, CL. 2022. J Struct Biol 214, 107825.
    doi: 10.1016/j.jsb.2021.107825PMID:34906669
  7. Rescuing activity of oxygen-damaged pyruvate formate-lyase by a spare part protein. Andorfer, MC, Backman, LRF, Li, PL, Ulrich, EC, Drennan, CL. 2021. J Biol Chem 297, 101423.
    doi: 10.1016/j.jbc.2021.101423PMID:34801558
  8. Crystal Structure of the [4Fe-4S] Cluster-Containing Adenosine-5'-phosphosulfate Reductase from Mycobacterium tuberculosis. Feliciano, PR, Carroll, KS, Drennan, CL. 2021. ACS Omega 6, 13756-13765.
    doi: 10.1021/acsomega.1c01043PMID:34095667
  9. Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase. Dawson, CD, Irwin, SM, Backman, LRF, Le, C, Wang, JX, Vennelakanti, V, Yang, Z, Kulik, HJ, Drennan, CL, Balskus, EP et al.. 2021. Cell Chem Biol 28, 1333-1346.e7.
    doi: 10.1016/j.chembiol.2021.03.001PMID:33773110
  10. Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase. Cohen, SE, Can, M, Wittenborn, EC, Hendrickson, RA, Ragsdale, SW, Drennan, CL. 2020. ACS Catal 10, 9741-9746.
    doi: 10.1021/acscatal.0c03033PMID:33495716
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