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

  • 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. 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 , .
    doi: 10.1021/acs.biochem.4c00329PMID:39164005
  2. 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
  3. 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
  4. Capturing Snapshots of Ribonucleotide Reductase Using Cryo-Electron Microscopy. Andree, GA, Feliciano, PR, Kang, G, Levitz, TS, Miller, KR, Westmoreland, DE, Drennan, CL. 2023. Microsc Microanal 29, 893.
    doi: 10.1093/micmic/ozad067.441PMID:37613477
  5. 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
  6. 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
  7. 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
  8. Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase. Cui, C, Song, DY, Drennan, CL, Stubbe, J, Nocera, DG. 2023. J Am Chem Soc 145, 5145-5154.
    doi: 10.1021/jacs.2c11483PMID:36812162
  9. Structure of metallochaperone in complex with the cobalamin-binding domain of its target mutase provides insight into cofactor delivery. Vaccaro, FA, Born, DA, Drennan, CL. 2023. Proc Natl Acad Sci U S A 120, e2214085120.
    doi: 10.1073/pnas.2214085120PMID:36787360
  10. Starting a new chapter on class Ia ribonucleotide reductases. Levitz, TS, Drennan, CL. 2022. Curr Opin Struct Biol 77, 102489.
    doi: 10.1016/j.sbi.2022.102489PMID:36272229
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