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
Read Schusky

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. 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
  2. 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
  3. 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
  4. Structural basis for non-radical catalysis by TsrM, a radical SAM methylase. Knox, HL, Chen, PY, Blaszczyk, AJ, Mukherjee, A, Grove, TL, Schwalm, EL, Wang, B, Drennan, CL, Booker, SJ. 2021. Nat Chem Biol 17, 485-491.
    doi: 10.1038/s41589-020-00717-yPMID:33462497
  5. Biochemical and crystallographic investigations into isonitrile formation by a nonheme iron-dependent oxidase/decarboxylase. Jonnalagadda, R, Del Rio Flores, A, Cai, W, Mehmood, R, Narayanamoorthy, M, Ren, C, Zaragoza, JPT, Kulik, HJ, Zhang, W, Drennan, CL et al.. J Biol Chem 296, 100231.
    doi: 10.1074/jbc.RA120.015932PMID:33361191
  6. Gated Proton Release during Radical Transfer at the Subunit Interface of Ribonucleotide Reductase. Cui, C, Greene, BL, Kang, G, Drennan, CL, Stubbe, J, Nocera, DG. 2021. J Am Chem Soc 143, 176-183.
    doi: 10.1021/jacs.0c07879PMID:33353307
  7. Discovery of a Cyclic Choline Analog That Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria. Bollenbach, M, Ortega, M, Orman, M, Drennan, CL, Balskus, EP. 2020. ACS Med Chem Lett 11, 1980-1985.
    doi: 10.1021/acsmedchemlett.0c00005PMID:33062182
  8. Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase. Cohen, SE, Brignole, EJ, Wittenborn, EC, Can, M, Thompson, S, Ragsdale, SW, Drennan, CL. 2021. Structure 29, 43-49.e3.
    doi: 10.1016/j.str.2020.08.011PMID:32937101
  9. The Solvent-Exposed Fe-S D-Cluster Contributes to Oxygen-Resistance in Desulfovibrio vulgaris Ni-Fe Carbon Monoxide Dehydrogenase. Wittenborn, EC, Guendon, C, Merrouch, M, Benvenuti, M, Fourmond, V, Léger, C, Drennan, CL, Dementin, S. 2020. ACS Catal 10, 7328-7335.
    doi: 10.1021/acscatal.0c00934PMID:32655979
  10. Conformational Motions and Water Networks at the α/β Interface in E. coli Ribonucleotide Reductase. Reinhardt, CR, Li, P, Kang, G, Stubbe, J, Drennan, CL, Hammes-Schiffer, S. 2020. J Am Chem Soc 142, 13768-13778.
    doi: 10.1021/jacs.0c04325PMID:32631052
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