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. 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
  2. 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
  3. 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
  4. A single diiron enzyme catalyses the oxidative rearrangement of tryptophan to indole nitrile. Adak, S, Ye, N, Calderone, LA, Duan, M, Lubeck, W, Schäfer, RJB, Lukowski, AL, Houk, KN, Pandelia, ME, Drennan, CL et al.. 2024. Nat Chem 16, 1989-1998.
    doi: 10.1038/s41557-024-01603-zPMID:39285206
  5. How ATP and dATP Act as Molecular Switches to Regulate Enzymatic Activity in the Prototypical Bacterial Class Ia Ribonucleotide Reductase. Funk, MA, Zimanyi, CM, Andree, GA, Hamilos, AE, Drennan, CL. 2024. Biochemistry 63, 2517-2531.
    doi: 10.1021/acs.biochem.4c00329PMID:39164005
  6. Potent Inhibition of E. coli DXP Synthase by a gem-Diaryl Bisubstrate Analog. Coco, LB, Toci, EM, Chen, PY, Drennan, CL, Freel Meyers, CL. 2024. ACS Infect Dis 10, 1312-1326.
    doi: 10.1021/acsinfecdis.3c00734PMID:38513073
  7. Structural and biochemical investigations of a HEAT-repeat protein involved in the cytosolic iron-sulfur cluster assembly pathway. Vasquez, S, Marquez, MD, Brignole, EJ, Vo, A, Kong, S, Park, C, Perlstein, DL, Drennan, CL. 2023. Commun Biol 6, 1276.
    doi: 10.1038/s42003-023-05579-3PMID:38110506
  8. Oxidative rearrangement of tryptophan to indole nitrile by a single diiron enzyme. Adak, S, Ye, N, Calderone, LA, Schäfer, RJB, Lukowski, AL, Pandelia, ME, Drennan, CL, Moore, BS. 2023. bioRxiv , .
    doi: 10.1101/2023.08.03.551874PMID:37577561
  9. Structural insight into G-protein chaperone-mediated maturation of a bacterial adenosylcobalamin-dependent mutase. Vaccaro, FA, Faber, DA, Andree, GA, Born, DA, Kang, G, Fonseca, DR, Jost, M, Drennan, CL. 2023. J Biol Chem 299, 105109.
    doi: 10.1016/j.jbc.2023.105109PMID:37517695
  10. Development of an in vitro method for activation of X-succinate synthases for fumarate hydroalkylation. Andorfer, MC, King-Roberts, DT, Imrich, CN, Brotheridge, BG, Drennan, CL. 2023. iScience 26, 106902.
    doi: 10.1016/j.isci.2023.106902PMID:37283811
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