By combining X-ray crystallography, cryo-electron microscopy and other biophysical methods, the goal of the Drennan lab is to “visualize” molecular processes by obtaining snapshots of enzymes in action.

Office

Phone

617-253-5622

cdrennan@mit.edu

Administrative Assistant

Read Schusky

Assistant Phone

(617) 258-7851

Lab Website

Catherine L. Drennan

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

Research Areas

Office

68-680

Phone

617-253-5622

cdrennan@mit.edu

Administrative Assistant

Read Schusky

Assistant Phone

(617) 258-7851

Lab Website

By combining X-ray crystallography, cryo-electron microscopy, cryo-electron microscopy, and other biophysical methods, the goal of the Drennan lab is to “visualize” molecular processes by obtaining snapshots of enzymes in action.

Read more about the Drennan Lab’s research on the group’s website.

Key Publications

See all on the Drennan Group Website

Structural Basis for Non-Radical Catalysis by TsrM, a Radical SAM Methylase

Knox, H.L., Chen, P. Y.T., Blaszczyk, A.J., Mukherjee, A., Grove, T.L., Schwalm, E.L., Wang, B., Drennan*, C.L., and Booker*, S.J. (2021), Nat. Chem. Biol. DOI: 10.1038/s41589-020-00717-y.

Full Text on PubMed

Structure of a Trapped Radical Transfer Pathway within a Ribonucleotide Reductase Holocomplex

Kang, G., Taguchi, A.T., Stubbe*, J., and Drennan*, C.L. (2020) Science 368, 424-427. DOI:10.1126/science.aba6794 PMCID: PMC7774503

Full Text at PubMed

Molecular Basis for Catabolism of the Abundant Metabolite Trans-4-hydroxy-L-Proline by a Microbial Glycyl Radical Enzyme

Backman‡, L.R.F., Huang‡, Y.Y., Andorfer, M.C., Gold, B., Raines, R.T., Balskus*, E.P., and Drennan*, C.L. (2020), eLife 9, e51420 doi: 10.7554/eLife.51420

Full Text at PubMed

Crystallographic Characterization of the Carbonylated A-cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase

Cohen, S.E., Mehmet, C., Wittenborn, E.C., Hendrickson, R.A., Ragsdale, S.W., Drennan, C.L. (2020), ACS Catalysis, DOI: 10.1021/acscatal.0c03033

Full Text at PubMed

The Solvent-Exposed Fe-S D-cluster Contributes to Oxygen-Resistance in D. vulgaris Ni-Fe Carbon Monoxide Dehydrogenase

Wittenborn, E.C., Guendon, C., Merrouch, M., Benvenuti, M., Fourmond, V., Léger, C., Drennan*, C.L., and Dementin*, S. (2020), ACS Catalysis doi: 10.1021/acscatal.0c00934

Full Text at PubMed

A Reverse TCA Cycle 2-Oxoacid:ferredoxin Oxidoreductase that Makes C-C Bonds from CO₂

Chen‡, P.Y-T., Li‡, Bin, Drennan*, C.L., and Elliott*, S.J. (2019), Joule 3, 595-611. PMCID: PMC6508887.

Full Text at PubMed

Biochemical and Structural Characterization of a Schiff Base in the Radical-Mediated Biosynthesis of 4-Demethylwyosine by TYW1

Grell‡, T.A.J., Young‡, A.P., Drennan*, C.L., and Bandarian*, V. (2018). J. Am. Chem. Soc. 140, 6842-6852. PMCID: PMC5994729

Full Text at PubMed

Redox-Dependent Rearrangements of the NiFeS Cluster of Carbon Monoxide Dehydrogenase

Wittenborn, E.C., Merrouch, M., Ueda, C., Fradale, L., Léger, C., Fourmond, V., Pandelia, M-E., Dementin*, S., and Drennan*, C.L. (2018), eLife 7, e39451. PMCID:PMC6168284

Full Text at PubMed

Structural Basis for Methylphosphonate Biosynthesis

Born, D.A. ‡, Ulrich, E.C. ‡, Ju, K.-S., Peck, S.C., van der Donk, W.A.*, and Drennan, C.L.* (2017). Science 358, 1336-1339. 29217579. PMID: 29217579. DOI:10.1126/science.aao3435 ‡The authors contributed equally to this work. *Corresponding Authors

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A B12-dependent radical SAM enzyme involved in Oxetanocin-A biosynthesis

Bridwell-Rabb, J. ‡, Zhong, A. ‡, Sun, H.G., Drennan, C.L.*, and Liu, H.-w.* (2017). Nature 544, 322-326. PMCID: PMC5398914 ‡The authors contributed equally to this work. *Corresponding Authors

Full Text at PubMed