Catherine Drennan

Catherine Drennan

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

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

617-253-5622

Phone

68-680

Office

cdrennan@mit.edu

Email

Building 68 - Koch Biology Building

Location

Lab Website
Martha Pham

Assistant

617-258-7851

Assistant Phone

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

  • National Academy of Sciences, 2023
  • 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. Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity. Imrich, CN, Chakraborty, A, Backman, LRF, Andorfer, MC, Drennan, CL. 2026. Biochemistry , .
    doi: 10.1021/acs.biochem.6c00318PMID:42361324
  2. The Structural Basis of Malodorant Skatole Formation by the Glycyl Radical Enzyme Indoleacetate Decarboxylase. Imrich, CN, Backman, LRF, Allworth, AP, Andorfer, MC, Paris, JC, Greeley, NM, Fu, B, Balskus, EP, Drennan, CL. 2026. bioRxiv , .
    doi: 10.64898/2026.05.24.727522PMID:42244603
  3. A highly dynamic mononuclear non-heme iron enzyme for the two-step isonitrile biosynthesis. Ye, N, Del Rio Flores, A, Zhang, W, Drennan, CL. 2026. Nat Commun 17, .
    doi: 10.1038/s41467-026-68588-wPMID:41587996
  4. The cobalamin-binding domain of cobalamin-dependent radical S-adenosylmethionine enzymes: Familiarity in unfamiliar places. Avalos, DM, Drennan, CL. 2026. J Inorg Biochem 277, 113204.
    doi: 10.1016/j.jinorgbio.2025.113204PMID:41478053
  5. PexR is a noncanonical regulator of the peroxide stress response in bacteria. Bastida-Martínez, E, Del Rey-Navalón, I, Ye, N, Drennan, CL, Padmanabhan, S, Elías-Arnanz, M. 2025. Nucleic Acids Res 53, .
    doi: 10.1093/nar/gkaf1408PMID:41474264
  6. How ATP and dATP reposition class III ribonucleotide reductase cone domains to regulate enzyme activity. Andree, GA, Miller-Brown, KR, Zhao, Z, Smith, AK, Dawson, CD, Deredge, DJ, Drennan, CL. 2025. Sci Adv 11, eady9156.
    doi: 10.1126/sciadv.ady9156PMID:41313771
  7. Structural basis for anaerobic alkane activation by a multisubunit glycyl radical enzyme. Andorfer, MC, Levitz, TS, Liu, J, Chakraborty, A, King-Roberts, DT, Nweneka, D, Imrich, CN, Drennan, CL. 2025. Proc Natl Acad Sci U S A 122, e2510389122.
    doi: 10.1073/pnas.2510389122PMID:40758891
  8. 2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor N3CDP. Westmoreland, DE, Feliciano, PR, Kang, G, Cui, C, Kim, A, Stubbe, J, Nocera, DG, Drennan, CL. 2024. Proc Natl Acad Sci U S A 121, e2417157121.
    doi: 10.1073/pnas.2417157121PMID:39475643
  9. 2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor N3CDP. Westmoreland, DE, Feliciano, PR, Kang, G, Cui, C, Kim, A, Stubbe, J, Nocera, DG, Drennan, CL. 2024. bioRxiv , .
    doi: 10.1101/2024.10.09.617422PMID:39416103
  10. Capturing a methanogenic carbon monoxide dehydrogenase/acetyl-CoA synthase complex via cryogenic electron microscopy. Biester, A, Grahame, DA, Drennan, CL. 2024. Proc Natl Acad Sci U S A 121, e2410995121.
    doi: 10.1073/pnas.2410995121PMID:39361653
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