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

Martha Pham

Assistant Phone

(617) 258-7851

Lab Website

Catherine L. Drennan

John and Dorothy Wilson Professor of Biochemistry
Investigator and Professor, Howard Hughes Medical Institute

Research Areas

Office

68-680

Phone

617-253-5622

cdrennan@mit.edu

Administrative Assistant

Martha Pham

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

2.6-Å Resolution Cryo-EM Structure of a Class Ia Ribonucleotide Reductase Trapped with Mechanism-based Inhibitor N3CDP

Westmoreland‡, D.E., Feliciano‡, P.R., Kang, G., Cui, C., Kim, A., Stubbe, J., Nocera, D.G., and Drennan*, C.L. (2024) Proc. Natl. Acad. Sci. U.S.A. 121 (41), e2417157121 https://doi.org/10.1073/pnas.2417157121. PMID: 39475643.

Full Text at PNAS

Capturing a Methanogenic Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase Complex via Cryogenic Electron Microscopy

Biester, A., Grahame, D.A., Drennan*, C.L. (2024) Proc. Natl. Acad. Sci. 121 (41) e2410995121 https://doi.org/10.1073/pnas.2410995121 PMCID: PMC11474084. PMID: 39361653

Full Text at PNAS

Oxidative Rearrangement of Tryptophan to Indole Nitrile by a Single Diiron Enzyme

Adak‡, S., Ye‡, N., Calderone, L.A., Duan, M., Lubeck, W., Schäfer, R.J.B., Lukowski, A.L., Houk, K.N., Pandelia*, M.-E., Drennan*, C.L., Moore, B.S. (2024) Nat. Chem. doi:10.1038/s41557-024-01603-z. PMID: 37577561

Full Text at PubMed

Structure of Metallochaperone in Complex with the Cobalamin-binding Domain of its Target Mutase Provides Insight into Cofactor Delivery

Vaccaro, F.A., Born, D.A, and Drennan*, C.L. (2023) Proc. Natl. Acad. Sci. doi: 10.1073/pnas.2214085120. PMCID: PMC9974510. PMID: 36787360

Full Text at PNAS

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

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

Visualizing the Gas Channels of a Monofunctional Carbon Monoxide Dehydrogenase

Biester, A., Dementin, S., and Drennan*, C.L. (2022) J. Inorg. Biochem. 230, 111774. Special issue in honor of Dick Holm. doi: 10.1016/j.jinorgbio.2022.111774. PMCID: PMC9093221. PMID: 35278753

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

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