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 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

Key Publications

  1. A B12-dependent radical SAM enzyme involved in oxetanocin A biosynthesis. Bridwell-Rabb, J, Zhong, A, Sun, HG, Drennan, CL, Liu, HW. 2017. Nature 544, 322-326.
    doi: 10.1038/nature21689PMID:28346939
  2. Crystallographic snapshots of sulfur insertion by lipoyl synthase. McLaughlin, MI, Lanz, ND, Goldman, PJ, Lee, KH, Booker, SJ, Drennan, CL. 2016. Proc Natl Acad Sci U S A 113, 9446-50.
    doi: 10.1073/pnas.1602486113PMID:27506792
  3. Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli. Zimanyi, CM, Chen, PY, Kang, G, Funk, MA, Drennan, CL. 2016. Elife 5, e07141.
    doi: 10.7554/eLife.07141PMID:26754917
  4. Structural basis for gene regulation by a B12-dependent photoreceptor. Jost, M, Fernández-Zapata, J, Polanco, MC, Ortiz-Guerrero, JM, Chen, PY, Kang, G, Padmanabhan, S, Elías-Arnanz, M, Drennan, CL. 2015. Nature 526, 536-41.
    doi: 10.1038/nature14950PMID:26416754
  5. Visualizing molecular juggling within a B12-dependent methyltransferase complex. Kung, Y, Ando, N, Doukov, TI, Blasiak, LC, Bender, G, Seravalli, J, Ragsdale, SW, Drennan, CL. 2012. Nature 484, 265-9.
    doi: 10.1038/nature10916PMID:22419154

Recent Publications

  1. Biochemical and crystallographic investigations into isonitrile formation by a non-heme 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.. 2020. J Biol Chem , .
    doi: 10.1074/jbc.RA120.015932PMID:33361191
  2. 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
  3. 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
  4. 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
  5. 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
  6. 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
  7. Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets. Greene, BL, Kang, G, Cui, C, Bennati, M, Nocera, DG, Drennan, CL, Stubbe, J. 2020. Annu Rev Biochem 89, 45-75.
    doi: 10.1146/annurev-biochem-013118-111843PMID:32569524
  8. A Stable Ferryl Porphyrin at the Active Site of Y463M BthA. Rizzolo, K, Weitz, AC, Cohen, SE, Drennan, CL, Hendrich, MP, Elliott, SJ. 2020. J Am Chem Soc 142, 11978-11982.
    doi: 10.1021/jacs.0c04023PMID:32564595
  9. Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex. Kang, G, Taguchi, AT, Stubbe, J, Drennan, CL. 2020. Science 368, 424-427.
    doi: 10.1126/science.aba6794PMID:32217749
  10. Molecular basis for catabolism of the abundant metabolite trans-4-hydroxy-L-proline by a microbial glycyl radical enzyme. Backman, LR, Huang, YY, Andorfer, MC, Gold, B, Raines, RT, Balskus, EP, Drennan, CL. 2020. Elife 9, .
    doi: 10.7554/eLife.51420PMID:32180548
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