Updated Apr 2025
Westmoreland, D.E., Feliciano‡, P.R., Kang, G., Cui, C., Kim, A., Stubbe, J., Nocera, D.G., and Drennan*, C.L. (2024) 2.6-Å Resolution Cryo-EM Structure of a Class Ia Ribonucleotide Reductase Trapped with Mechanism-based Inhibitor N3CDP, Proc. Natl. Acad. Sci. U.S.A. 121 (45) e2417157121, doi: 10.1073/pnas.2417157121. PMID: 39475643; PMCID: PMC11551348. PDBID: 9DB2, EMPIAR: 12249 , EMDB: EMD-46711.
Biester, A., Grahame, D.A., Drennan*, C.L. (2024) Capturing a Methanogenic Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase Complex via Cryogenic Electron Microscopy Proc. Natl. Acad. Sci. 121 (41) e2410995121, doi: 10.1073/pnas.2410995121 (2024). PMID: 39361653; PMCID: PMC11474084. PDBID: 9C0Q, 9C0R, 9C0S, 9C0T. EMPIAR: 12108, 12124. EMDB: EMD-45089, EMD-45090, EMD-45091, EMD-45092.
Adak, S., Ye, N., Calderone, L.A. et al. A single diiron enzyme catalyses the oxidative rearrangement of tryptophan to indole nitrile. Nat. Chem. 16, 1989–1998 (2024). doi: 10.1101/2023.08.03.551874 PMID: 37577561; PBD: 8TWN , 8TWT, 8TWW
Funk, M.A., Zimanyi, C.M., Andree, G.A., Hamilos, A.E., Drennan, C.L. (2024) How ATP and dATP Act as Molecular Switches to Regulate Enzymatic Activity in the Prototypical Bacterial Class Ia Ribonucleotide Reductase, Biochemistry Special Issue in Honor of Christopher T. Walsh, doi: 10.1021/acs.biochem.4c00329. PMID: 39164005. PMCID: PMC11447812 ; PDBID: 8VHN, 8VHO, 8VHP, 8VHQ, 8VHR, 8VHU
Coco, L.B., Toci, E.M., Chen, P.T-Y., Drennan*, C.L., and Freel Meyers*, C.L. (2024) Potent Inhibition of E. coli DXP Synthase by a gem-Diaryl Bisubstrate Analog, ACS Infect. Dis., 1312-1326 accepted. DOI: 10.1021/acsinfecdis.3c00734 PMCID: PMC11019550. PMID: 38513073 PDB: 6OUV , 6OUW
Vasquez, S., Marquez, M.D., Brignole, E.J., Vo, A., Kong, S. Park, C., Perlstein*, D.L., and Drennan*, C.L. (2023) Structural and Biochemical Investigations of a HEAT-repeat Protein Involved in the Cytosolic Iron-Sulfur Cluster Assembly Pathway, Commun. Biol. 6, 1276. doi:10.1038/s42003-023-05579-3. PMID: 38110506 PMCID: PMC10728100
Vaccaro, F.A., Faber, D.A., Andree, G.A., Born, D.A., Kang, G., Fonseca, D.R., Jost, M., and Drennan*, C.L. (2023) Structural Insight into G-protein Chaperone-mediated Maturation of a Bacterial Adenosylcobalamin-dependent Mutase, J. Biol. Chem. 299, 105109. doi: 10.1016/j.jbc.2023.105109 PMCID: PMC10481361. PMID: 37517695 PDB: 8SSL, 8STA EMDB: EMD-40751, EMD-40758
Andorfer, M.C., King-Roberts, D.T., Imrich, C.N., Brotheridge, B.G., and Drennan*, C.L. (2023) Development of an in vitro Method for Activation of X-succinate Synthases for Fumarate Hydroalkylation, iScience 26(6), 106902. doi: 10.1016/j.isci.2023.106902. PMCID: PMC10239695. PMID: 37283811
Cui, C., Song, D.Y., Drennan, C.L., Stubbe*, J., and Nocera*, D.G. (2023) Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase, J. Am. Chem. Soc. ASAP February 22, 2023 doi: 10.1021/jacs.2c11483 PMCID: PMC10561588. PMID: 36812162
Vaccaro, F.A., Born, D.A, and Drennan*, C.L. (2023) Structure of Metallochaperone in Complex with the Cobalamin-binding Domain of its Target Mutase Provides Insight into Cofactor Delivery, Proc. Natl. Acad. Sci. doi: 10.1073/pnas.2214085120. PMCID: PMC9974510.PMID: 36787360 PDB: 8DPB
Levitz, T.S. and Drennan*, C.L. (2022) Starting a New Chapter on Class Ia Ribonucleotide Reductases, Curr. Opin. Struct. Biol. 77,102489. PMID: 36272229 doi: 10.1016/j.sbi.2022.102489.
Biester, A., Marcano-Delgado, A.N., Drennan*, C.L. (2022) Structural Insights into Microbial One-Carbon Metabolic Enzymes Ni−Fe−S-dependent Carbon Monoxide Dehydrogenases and Acetyl-CoA Synthases, Biochemistry 61(24), 2797-2805. doi: 10.1021/acs.biochem.2c00425. PMCID: PMC9782325. PMID: 36137563
Sankari, S., Babu, V.M.P, Bian, K., Alhazmi, A., Andorfer, M.C., Avalos, D.M., Smith, T.A., Yoon, K., Drennan, C.L., Yaffe M.B., Lourido, S., and Walker*, G.C. (2022) Haem-sequestering Plant Peptide Drives Iron Uptake in Symbiotic Bacteria, Nat. Microbiol. 7(9), 1453-1465. doi: 10.1038/s41564-022-01192-y. PMCID: PMC9420810. PMID: 35953657 | Highlighted in MIT News
Levitz, T.S., Weckener, M. Fong, I., Naismith, J.H., Drennan, C.L., Brignole, E.J., Clare, D.K., Darrow*, M.C. (2022) Approaches to Using the chameleon: Robust, Automated, Fast-plunge CryoEM Specimen Preparation, Front. Mol. Biosci. 9, 903148. doi: 10.3389/fmolb.2022.903148. PMCID: PMC9260054. PMID: 35813832
Vaccaro, F.A. and Drennan*, C.L (2022) The Role of Nucleoside Triphosphate Hydrolase Metallochaperones in Making Metalloenzymes, Metallomics 14(6), mfac030. In honor of Deborah Zamble. doi:10.1093/mtomcs/mfac030. PMCID: PMC9164220
Ulrich, E.C. and Drennan*, C.L. (2022) The Atypical Cobalamin-Dependent S–Adenosyl-L-Methionine Nonradical Methylase TsrM and its Radical Counterparts, J. Am. Chem. Soc. 144(13), 5673-5684. https://doi.org/10.1021/jacs.1c12064. PMCID: PMC8992657. PMID: 35344653
Biester, A., Dementin, S., and Drennan*, C.L. (2022) Visualizing the Gas Channels of a Monofunctional Carbon Monoxide Dehydrogenase, J. Inorg. Biochem. 230, 111774. Special issue in honor of Dick Holm. doi:10.1016/j.jinorgbio.2022.111774. PMCID: PMC9093221. PMID: 35278753 PDB: 7TSJ
Ohmer, C.J., Dasgupta, M., Patwardhan, A., Bogacz, I., Kaminsky, C., Doyle, M.D., Chen, P. Y.-T., Keable, S.M., Makita, H., Simon, P.S., Massad, R., Fransson, T., Chatterjee, R., Bhowmick, A., Paley, D.W., Moriarty, N.W., Brewster, A.S., Gee, L.B., Alonso-Mori, R., Moss, F., Fuller, F.D., Batyuk, A., Sauter, N.K., Bergmann, U., Drennan, C.L., Yachandra, V.K., Yano*, J., Kern*, J.F., Ragsdale*, S.W. (2022) XFEL Serial Crystallography Reveals the Room Temperature Structure of Methyl-Coenzyme M Reductase, J. Inorg. Biochem. 230, 111768. Special issue in honor of Dick Holm. doi: 10.1016/j.jinorgbio.2022.111768. PMID: 35202981 PMCID: PMC8930625 PDB: 7SXM, 7SUC
Narasimhan*, J., Letinski, S., Jung, S., Gerasyuto, A., Wang, J., Arnold, M., Chen, G., Hedrick, J., Dumble, M., Ravichandran, K., Levitz, T.L., Chang, C., Drennan, C.L., Stubbe*, J., Karp, G., and Branstrom*, A. (2022) Ribonucleotide Reductase, A Novel Drug Target for Gonorrhea, eLife 11:e67447. doi:10.7554/eLife.67447. PMCID: PMC886584. PMID: 35137690.
Bridwell-Rabb*, J., Li, B., Drennan, C.L. (2022) Cobalamin-dependent Radical S-adenosylmethionine Enzymes: Capitalizing on Old Motifs for New Functions, ACS Bio. & Med. Chem. 2(3), 173-186. doi: 10.1021/acsbiomedchemau.1c00051. PMCID: PMC9204698
Levitz, T.S., Brignole, E.J., Fong, I., Darrow*, M.C., and Drennan*, C.L. (2021) Effects of chameleon Dispense-to-plunge Speed on Particle Concentration, Complex Formation, and Final Resolution: A Case Study Using the Neisseria gonorrhoeae Ribonucleotide Reductase Inactive Complex, J. Struct. Biol. 214, 107825. doi: 10.1016/j.jsb.2021.107825. PMCID: PMC8994553. PMID: 34906669 PDB: 7MDI, EMD-23773
Andorfer, M.C., Backman, L.R.F., Li, P.L., Ulrich, E.C., and Drennan*, C.L. (2021) Rescuing Activity of Oxygen-damaged Pyruvate Formate-Lyase By a Spare Part Protein, J. Biol. Chem. 297(6), 101423. doi: 10.1016/j.jbc.2021.101423. PMCID: PMC8683613. PMID: 34801558
Feliciano, P.R., Carroll, K.S., and Drennan*, C.L. (2021) Crystal Structure of the [4Fe-4S] Cluster-containing Adenosine-5′-Phosphosulfate Reductase from Mycobacterium tuberculosis, ACS Omega 6(21), 13756-13765. ao1c01043. doi: 10.1021/acsomega.1c01043. PMCID: PMC8173546 PDB: 7LHR, 7LHS, 7LHU
Andorfer*, M.C. and Drennan, C.L. (2021) Fixing Nature’s Carbon Inefficiencies, Joule 5, 765–767. doi: 10.1016/j.joule.2021.03.025
Dawson ‡, C.D., Irwin‡, S.M., Backman, L.R.F., Le, C., Wang, J.X., Vennelakanti, V., Yang, Z., Kulik*, H.J., Drennan*, C.L., and Balskus*, E.P. (2021) Molecular Basis of C–S Bond Cleavage in the Glycyl Radical Enzyme Isethionate Sulfite-Lyase, Cell Chem. Biol. 28(9), 1333-1346. doi: 10.1016/j.chembiol.2021.03.001. PMCID: PMC8473560. PMID: 33773110 PDB: 7KQ3, 7KQ4
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) Structural Basis for Non-Radical Catalysis by TsrM, a Radical SAM Methylase, Nat. Chem. Biol. 17(4), 485-491. doi: 10.1038/s41589-020-00717-y PMCID: PMC7990684. PMID: 33462497 PDB: 6WTE, 6WTF
Jonnalagadda‡, R., Del Rio Flores‡, A., Cai, W., Mehmood, R., Narayanamoorthy, M., Ren, C., Zaragoza, J.P.T., Kulik*, H.J., Zhang*, W., and Drennan*, C.L. (2021) Biochemical and Crystallographic Investigations into Isonitrile Formation by a Nonheme Iron-Dependent Oxidase/Decarboxylase, J. Biol. Chem. 296, 100231. doi: 10.1074/jbc.RA120.015932. PMCID: PMC7949033. PMID: 33361191 PDB: 6XN6, 6XO3, 6XOJ, 6XPA
Cui, C., Greene*, B.L., Kang, G., Drennan, C.L., Stubbe*, J., Nocera*, D.G. (2020) Gated Proton Release during Radical Transfer at the Subunit Interface of Ribonucleotide Reductase, J. Am. Chem. Soc. 143, 176-183. doi: 10.1021/jacs.0c07879. PMCID: PMC7904477
Cohen, S.E., Brignole, E.J., Wittenborn, E.C., Can, M., Thompson, S., Ragsdale, S.W., and Drennan*, C.L. (2021) Negative Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase, Structure 29, 43-49. doi: 10.1016/j.str.2020.08.011. PMCID: PMC7796957. PMID: 32937101
Cohen, S.E., Can, M., Wittenborn, E.C., Hendrickson, R.A., Ragsdale, S.W., Drennan*, C.L. (2020) Crystallographic Characterization of the Carbonylated A-cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase, ACS Catalysis 10(17), 9741-9746. doi: 10.1021/acscatal.0c03033. PMCID: PMC7819276. PMID: 33495716 PDB: 6X5K
Reinhardt, C., Li, P., Kang, G., Stubbe, J., Drennan, C.L., Hammes-Schiffer*, S. (2020) Conformational Motions and Water Networks at the α/β Interface in E. coli Ribonucleotide Reductase. J. Am. Chem. Soc. 142(32), 13768-13778. doi: 10.1021/jacs.0c04325. PMCID: PMC7594210
Greene, B.L., Kang, G., Cui, C., Bennati, M., Nocera, D.G., Drennan, C.L., and Stubbe, J. (2020) Ribonucleotide Reductases (RNRs): Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets, Ann. Rev. Biochem. 89, 45-75. doi: 10.1146/annurev-biochem-013118-111843. PMCID: PMC7316142
Rizzolo, K., Weitz, A.C., Cohen, S.E., Drennan, C.L, Hendrich, M.P., and Elliott*, S.J. (2020) A Stable Ferryl Porphyrin at the Active Site of Y463M BthA, J. Am. Chem. Soc. 142(28), 11978-11982. doi: 10.1021/jacs.0c04023. PMCID: PMC8667324
Wittenborn, E.C., Guendon, C., Merrouch, M., Benvenuti, M., Fourmond, V., Léger, C., Drennan*, C.L., and Dementin*, S. (2020) The Solvent-Exposed Fe-S D-cluster Contributes to Oxygen-Resistance in D. vulgaris Ni-Fe Carbon Monoxide Dehydrogenase, ACS Catalysis 10(13), 7328-7335. doi: 10.1021/acscatal.0c00934. PMCID: PMC7343238 PDB: 6VWY, 6VWZ, 6VX0, 6VX1
Kang, G., Taguchi, A.T., Stubbe*, J., and Drennan*, C.L. (2020) Structure of a Trapped Radical Transfer Pathway within a Ribonucleotide Reductase Holocomplex, Science 368(6489), 424-427. DOI: 10.1126/science.aba6794. PMCID: PMC7774503. PMID: 32217749 PDB: 6W4X | EMD-21540
Bollenbach, M., Ortega, M. Orman, M. Drennan, C.L., and Balskus*, E.P. (2020) Discovery of a Cyclic Choline Analog that Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria, ACS Med. Chem. Let. 11(10), 1980-1985. doi: 10.1021/acsmedchemlett.0c00005. PMCID: PMC7549264. PMID: 33062182 PDB: 6VUE
Backman‡, L.R.F., Huang‡, Y.Y., Andorfer, M.C., Gold, B., Raines, R.T., Balskus*, E.P., and Drennan*, C.L. (2020) Molecular Basis for Catabolism of the Abundant Metabolite Trans–4-hydroxy-L-Proline by a Microbial Glycyl Radical Enzyme, eLife 9, e51420. doi: 10.7554/eLife.51420. PMCID: PMC7077986. PMID: 32180548 PDB: 6VXC, 6VXE
Highlighted by MIT News, “Bacterial enzyme could become a new target for antibiotics” by Anne Trafton
Feliciano*, P.R. and Drennan*, C.L. (2019) Structural and Biochemical Investigations of the [4Fe4S] Cluster-containing Fumarate Hydratase from Leishmania major, Biochemistry58(49), 5011-5021. doi: 10.1021/acs.biochem.9b00923. PMCID: PMC7065722 PDB: 6UNZ, 6UO0, 6UOI, 6UOJ, 6UP9, 6UPM, 6UPO, 6UQ8, 6UQ9, 6UQB, 6UQL, 6UQM, 6UQN
Wittenborn, E.C., Cohen, S.E., Merrouch, M., Léger, C., Fourmond, V., Dementin*, S., and Drennan*, C.L. (2019) Structural Insight into Metallocofactor Maturation in Carbon Monoxide Dehydrogenase, J. Biol. Chem. 294(35), 13017-13026. doi: 10.1074/jbc.RA119.009610. PMCID: PMC6721931. PDB: 6ONC, 6OND, 6ONS
Faculty of 1000 Recommended.
Chen, P.Y.T., DeColli, A.A., Freel Meyers*, C.L., and Drennan*, C.L. (2019) X-ray Crystallography–based Structural Elucidation of Enzyme-bound Intermediates Along the 1–Deoxydxylulose 5-phosphate Synthase Reaction Coordinate, J. Biol. Chem. 294(33), 12405-12414. doi: 10.1074/jbc.RA119.009321. PMCID: PMC6699841 PDB: 6OUV, 6OUW
Bowman, S.E.J, Backman, L.R.F., Bjork, R.E., Andorfer, M.C., Yori, S., Caruso, A., Stultz, C.M., and Drennan*, C.L., (2019) Solution Structure and Biochemical Characterization of a Spare Part Protein That Restores Activity to an Oxygen-damaged Glycyl Radical Enzyme, J. Biol. Inorg. Chem. Special Issue in Honor of Joan Broderick 24(6), 817-829. doi: 10.1007/s00775-019-01681-2. PMCID: PMC6754787. PMID: 31250200 PDB: 6OWR
Highlighted by MIT Biology: “Bacteria use ‘spare part’ proteins to repair damage and survive inhospitable conditions” by Saime Sidik.
Bian, K., Lenz, S.A.P., Tang, Q., Chen, F., Qi, R., Jost, M., Drennan, C.L., Essigmann, J.M., Wetmore, S.D., Li*, D. (2019) DNA Repair Enzymes ALKBH2, ALKBH3, and AlkB Oxidize 5-Methylcytosine to 5-Hydroxymethylcytosine, 5-Formylcytosine and 5-Carboxylcytosine in vitro, Nucleic Acids Res. 47(11), 5522-5529. doi: 10.1093/nar/gkz395. PMCID: PMC6582317
Rizzolo, K., Cohen, S.E., Weitz, A.C., López Muñoz, M.M., Hendrich, M.P., Drennan, C.L., and Elliott*, S.J. (2019) A Widely Distributed Diheme Enzyme from Burkholderia that Displays an Atypically Stable bis–Fe(IV) State, Nature Comm. 10, 1101. doi: 10.1038/s41467-019-09020-4. PMCID: PMC6405878 PDB: 6NXO
Feliciano, P.R., Drennan*, C.L., and Nonato*, M.C. (2019) Crystal Structures of Fumarate Hydratases from Leishmania major in a Complex with Inhibitor 2-Thiomalate, ACS Chem. Biol. 14(2), 266-275. doi: 10.1021/acschembio.8b00972. PMCID: PMC6380369 PDB: 6MSN , 6MSO
Chen‡, P.Y-T., Li‡, B., Drennan*, C.L., and Elliott*, S.J. (2019) A Reverse TCA Cycle 2-Oxoacid:ferredoxin Oxidoreductase that Makes C-C Bonds from CO₂, Joule 3(2), 595-611. doi: 10.1016/j.joule.2018.12.006. PMCID: PMC6508887. PMID: 31080943 PDB: 6N2N , 6N2O
Orman, M., Bodea, S., Funk, M.A., Martinez-del Campo, A., Bollenbach, M., Drennan, C.L., and Balskus*, E.P. (2019) Structure-Guided Identification of a Small Molecule that Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria. J. Am. Chem. Soc. 141, 33-37. doi: 10.1021/jacs.8b04883. PMCID: PMC6475491 PDB: 6ND3
Grell, T.A.J., Bell, B.N., Nguyen, C., Dowling, D.P., Bruender, N.A., Bandarian, V., and Drennan*, C.L. (2019) Crystal Structure of AdoMet Radical Enzyme 7-Carboxy-7-Deazaguanine Synthase from Escherichia coli Suggests How Modifications Near [4Fe-4S] Cluster Engender Flavodoxin Specificity, Protein Science 28, 202-215. doi: 10.1002/pro.3529. PMCID: PMC6295903. PMID: 30341796. PDB: 6NHL
Grell, T.A.J., Kincannon, W.M., Bruender, N.A., Blaesi, E.J., Krebs*, C., Bandarian*, V., and Drennan*, C.L. (2018) Structural and Spectroscopic Analysis of Sporulation Killing Factor Biosynthetic Enzyme SkfB, a bacterial AdoMet Radical Sactisynthase, J. Biol. Chem. 293(45), 17349-17361. doi: 10.1074/jbc.RA118.005369. PMCID: PMC6231123. PMID: 30217813
Wittenborn, E.C., Merrouch, M., Ueda, C., Fradale, L., Léger, C., Fourmond, V., Pandelia, M-E., Dementin*, S., and Drennan*, C.L. (2018) Redox-Dependent Rearrangements of the NiFeS Cluster of Carbon Monoxide Dehydrogenase, eLife7, e39451. doi: 10.7554/eLife.39451. PMCID: PMC6168284. PMID: 30277213
Highlighted by MIT News and APS highlights: “An Unexpected Enzyme Structure” by Anne Trafton; and by Chemical and Engineering News: “Metal Secrets of CO2-converting Enzyme Revealed” by Cici Zhang; Faculty of 1000 Recommended
Ryan, K.S., and Drennan, C.L. (2018) Metalloenzymes in Natural Product Biosynthetic Pathways, Nat. Prod. Rep. 35(7), 612-614. doi: 10.1039/C8NP90023J
Harris, N.C., Born, D.A., Cai, W., Huang, Y., Martin, J., Khalaf, R., Drennan, C.L., and Zhang*, W. (2018) Isonitrile Formation by a Non-Heme Iron(II)-Dependent Oxidase/Decarboxylase, Angew. Chemie Int. Ed. 57(31), 9707-9710. doi: 10.1002/anie.201804307. PMCID: PMC6191297. PMID: 29906336
Grell‡, T.A.J., Young‡, A.P., Drennan*, C.L., and Bandarian*, V. (2018) Biochemical and Structural Characterization of a Schiff Base in the Radical-Mediated Biosynthesis of 4-Demethylwyosine by TYW1, J. Am. Chem. Soc. 140(22), 6842-6852. doi: 10.1021/jacs.8b01493. PMCID: PMC5994729. PMID: 29792696
Faculty of 1000 Recommended
Nakashige, T.G., Bowman, S.E.J., Zygiel, E.M., Drennan*, C.L., and Nolan*, E.M. (2018) Biophysical Examination of the Calcium-Modulated Nickel-Binding Properties of Human Calprotectin Reveals Conformational Change in the EF-Hand Domains and His3Asp Site, Biochemistry 57(28), 4155-4164. doi: 10.1021/acs.biochem.8b00415. PMCID: PMC6050108
Chen‡, P.Y.-T., Funk‡, M.A., Brignole, E.J., and Drennan*, C.L. (2018) Disruption of an Oligomeric Interface Prevents Allosteric Inhibition of Escherichia coli class Ia Ribonucleotide Reductase, J. Biol. Chem. 293(26), 10404-10412. doi: 10.1074/jbc.RA118.002569. PMCID: PMC6028975. PMID: 29700111
Chen, P.Y.-T., Aman, H., Can, M., Ragsdale, S.W., and Drennan*, C.L. (2018) Binding Site for Coenzyme A Revealed in the Structure of Pyruvate:Ferredoxin Oxidoreducatase from Moorella thermoacetica, Proc. Natl. Acad. Sci. 115(15), 3846-3851. doi: 10.1073/pnas.1722329115. PMCID: PMC5899475. PMID: 29581263
Brignole ‡, E.J, Tsai ‡, K.-L., Chittuluru, J., Li, H., Aye, Y., Penczek, P.A., Stubbe*, J., Drennan*, C.L., and Asturias*, F. (2018) 3.3-Å Resolution Cryo-EM Structure of Human Ribonucleotide Reductase with Substrate and Allosteric Regulators Bound, eLife 7, e31502. doi: 10.7554/eLife.31502. PMCID: PMC5819950
Highlighted by MIT News: “Scientists Deliver High-Resolution Glimpse of Enzyme Structure” by Anne Trafton, and by Forbes.com, “This Tiny Difference Between Human Cells and Bacteria Could Lead to New Antibiotics,” by Fiona McMillan.
Bridwell-Rabb*, J., Grell, T.A.J., and Drennan*, C.L. (2018) A Rich Man, Poor Man Story of S-Adenosylmethionine and Cobalamin Revisited, Ann. Rev. of Biochem. 87, 555-584. PMC exempt, invited review. doi: 10.1146/annurev-biochem-062917-012500. PMID: 29925255
Born‡, D.A., Ulrich‡, E.C., Ju, K.-S., Peck, S.C., van der Donk*, W.A., and Drennan*, C.L. (2017) Structural Basis for Methylphosphonate Biosynthesis, Science 358(6368), 1336-1339. doi: 10.1126/science.aao3435. PMCID: PMC5901744. PMID: 29217579
Backman, L.R.F., Funk, M.A., Dawson, C.D., and Drennan*, C.L. (2017) New Tricks for the Glycyl Radical Enzyme Family, Crit. Rev. Biochem. Mol. Biol.52(6), 674-695. doi: 10.1080/10409238.2017.1373741. PMCID: PMC5911432
Shisler, K.A., Hutcheson, R.U., Horitani, M., Duschene, K.S., Crain, A.V., Byer, A.S., Shepard, E.M., Rasmussen, A., Yang, J., Broderick, W.E., Vey, J.L., Drennan, C.L., Hoffman, B.M., and Broderick*, J.B. (2017) Monovalent Cation Activation of the Radical SAM Enzyme Pyruvate Formate–Lyase Activating Enzyme, J. Am. Chem. Soc. 139(34), 11803-11813. doi: 10.1021/jacs.7b04883. PMCID: PMC5579537
Bridwell-Rabb‡, J., Zhong‡, A., Sun, H.G., Drennan*, C.L., and Liu*, H.-W. (2017) A B12–Dependent Radical SAM Enzyme Involved in Oxetanocin A Biosynthesis, Nature 544(7650), 322-326. doi: 10.1038/nature21689. PMCID: PMC5398914. PMID: 28346939
Kung*, Y., and Drennan, C.L. (2017) One-Carbon Chemistry of Nickel-Containing Carbon Monoxide Dehydrogenase and Acetyl-CoA Synthase in The Biological Chemistry of Nickel, Deborah Zamble, Magdalena Rowińska-Żyrek, and Henryk Kozlowski (eds), Cambridge, UK: Royal Soc. of Chemistry, pp. 121-148. PMC exempt, book chapter. doi: 10.1039/9781788010580-00121
Cory, S.A., Van Vranken, J.G., Brignole, E.J., Patra, S., Winge, D.R., Drennan, C.L., Rutter, J., and Barondeau*, D.P. (2017) Structure of Human Fe-S Assembly Subcomplex Reveals Unexpected Cysteine Desulfurase Architecture and Acyl-ACP-ISD11 Interactions, Proc. Natl. Acad. Sci. 114(27), E5325-E5334. doi: 10.1073/pnas.1702849114. PMCID: PMC5502623
Highlighted as an SSRL Science Highlight: “Structure of the Human Cysteine Desulfurase Complex”. Faculty of 1000 Recommended.
Lin, Q., Parker, M.J., Taguchi, A.T., Ravichandran, K., Kim, A., Kang, G., Drennan*, C.L., and Stubbe*, J. (2017) Glutamate 52-β at the ɑ/β Subunit Interface of Escherichia coli Class Ia Ribonucleotide Reductase is Essential for Conformational Gating of Radical Transfer, J. Biol. Chem. 292(22), 9229-9239. doi: 10.1074/jbc.M117.783092. PMCID: PMC5454104
Nakashige‡, T.G., Zygiel‡, E.M., Drennan*, C.L., and Nolan*, E.M. (2017) Nickel Sequestration by the Host-Defense Protein Human Calprotectin, J. Am. Chem. Soc. 139(26), 8828-8836. doi: 10.1021/jacs.7b01212. PMCID: PMC5754018
Padmanabhan*, S., Jost*, M., Drennan*, C.L., and Elias-Arnanz*, M. (2017) A New Facet of Vitamin B12: Gene Regulation by Cobalamin-Based Photoreceptors, Ann. Rev. Biochem. 86, 485-514. PMC exempt, invited review. doi: 10.1146/annurev-biochem-061516-044500
Bridwell-Rabb*, J., and Drennan*, C.L. (2017) Vitamin B12 in the Spotlight Again, Curr. Op. Chem. Biol. 37, 63-70. doi: 10.1016/j.cbpa.2017.01.013. PMCID: PMC5540639
Bruender, N.A., Grell, T.A.J., Dowling, D.P., McCarty, R.M., Drennan, C.L., and Bandarian*, V. (2017) 7-Carboxy-7-Deazaguanine Synthase: A Radical S-Adenosyl-L-methionine Enzyme with Polar Tendencies, J. Am. Chem. Soc.139(5), 1912-1920. doi: 10.1021/jacs.6b11381. PMCID: PMC5301278
Bridwell-Rabb, J., Kang, G., Zhong, A., Liu, H.-W., and Drennan*, C.L. (2016) An HD Domain Phosphohydrolase Active Site Tailored for Oxetanocin-A Biosynthesis, Proc. Natl. Acad. Sci. 113(48), 13750-13755. doi: 10.1073/pnas.161310113. PMCID: PMC5137760
Wittenborn, E.C., Jost, M., Wei, Y., Stubbe*, J., and Drennan*, C.L. (2016) Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator, J. Biol. Chem. 291(48), 25264-25277. doi: 10.1074/jbc.M116.756833. PMCID: PMC5122792
Highlighted by MIT News: “A Step Toward Biodegradable Plastics” by Anne Trafton, and by The Hindu on November 26, 2016: “A Clue into Making of Biodegradable Plastic” by Shubashree Desikan. Selected for JBC: Virtual Issue on Enzymology. Protein Data Bank’s Molecule of the Month 12/17.
Dowling*, D.P., Kung, Y., Croft, A.K., Taghizadeh, K., Kelly, W.L., Walsh, C.T., and Drennan*, C.L. (2016) Structural Elements of an NRPS Cyclization Domain and its Intermodule Docking Domain, Proc. Natl. Acad. Sci. 113(44), 12432-12437. doi: 10.1073/pnas.1608615113. PMCID: PMC5098645
Dowling, D.P., Miles, Z.D., Köhrer, C., Maiocco, S.J., Elliott, S.J., Bandarian, V., and Drennan*, C.L. (2016) Molecular Basis of Cobalamin-Dependent RNA Modification, Nucleic Acid Res.44(20), 9965-9976. doi: 10.1093/nar/gkw806. PMCID: PMC5175355
Bodea‡, S., Funk‡, M.A., Balskus*, E.P., and Drennan*, C.L. (2016) Molecular Basis of C–N Bond Cleavage by the Glycyl Radical Enzyme Choline Trimethylamine-Lyase, Cell Chem. Biol.23(10), 1206-1216. doi: 10.1016/j.chembiol.2016.07.020. PMCID: PMC5493019. PMID: 27642068
Feliciano, P.R., Drennan*, C.L., and Nonato*, M.C. (2016) Crystal Structure of an Fe-S Cluster–Containing Fumarate Hydratase Enzyme from Leishmania major Reveals a Unique Protein Fold, Proc. Natl. Acad. Sci. 113(35), 9804-9809. doi: 10.1073/pnas.1605031113. PMCID: PMC5024648. PMID: 27528683
Highlighted by MIT News: “Targeting Neglected Diseases: New Enzyme-Mapping Advance Could Help Drug Development” by Peter Dizikes. Highlighted on the Universidade de São Paulo website on September 22, 2016.
Gibson, M.I., Chen, P.Y.-T., and Drennan*, C.L. (2016) A Structural Phylogeny for Understanding 2-Oxoacid Oxidoreductase Function, Curr. Opin. Struct. Biol. 41, 54-61. DOI: 10.1016/j.sbi.2016.05.011. PMCID: PMC5381805
McLaughlin, M.I., Lanz, N.D., Goldman, P.J., Lee, K.-H., Booker, S.J., and Drennan*, C.L. (2016) Crystallographic Snapshots of Sulfur Insertion by Lipoyl Synthase, Proc. Natl. Acad. Sci. 113(34), 9446-9450. doi: 10.1073/pnas.1602486113. PMCID: PMC5003258
Highlighted by MIT News and MITEI News, and Office of Science homepage as a University Research Highlight: “Research by MIT Undergrad Helps Crack Chemical Mystery” by Peter Dizikes.
Oyala, P.H., Ravichandran, K.R., Funk, M.A., Stucky, P.A., Stich, T.A., Drennan*, C.L., Britt*, R.D., and Stubbe*, J. (2016) Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase as an Example, J. Am. Chem. Soc. 138(25), 7951–7964. doi: 10.1021/jacs.6b03605. PMCID: PMC4929525
Highlighted as JACS Spotlight
Bridwell-Rabb*, J., and Drennan*, C.L. (2016) A Radically Unexpected Mechanism, Science 351(6279), 1266-1267. PMC exempt, perspective. doi: 10.1126/science.aaf4942. PMID: 26989237
Meyer, P.A., et al. (2016) Data Publication with the Structural Biology Data Grid Supports Live Analysis, Nat. Commun. 7, 10882. doi: 10.1038/ncomms10882. PMCID: PMC4786681
Bowman‡, S.E.J., Bridwell-Rabb‡, J., and Drennan*, C.L. (2016) Metalloprotein Crystallography: More than a Structure, Acc. Chem. Res.49(4), 695-702. doi: 10.1021/acs.accounts.5b00538. PMCID: PMC4838947
Highlighted as ACS Editors’ Choice. Featured on cover of Acc. Chem. Res., April 19, 2016.
Chen, F., Tang, Q., Bian, K., Humulock, Z.T., Yang, X., Jost, M., Drennan, C.L., Essigmann, J.M., and Li*, D. (2016) Adaptive Response Enzyme AlkB Preferentially Repairs 1-Methylguanine and 3-Methylthymine Adducts in Double-Stranded DNA, Chemical Res. Toxicol. 29(4), 687-693. doi: 10.1021/acs.chemrestox.5b00522. PMCID: PMC5497687
Chen, P.Y.-T., Wittenborn, E.C., and Drennan*, C.L. (2016) Waltzing Around Cofactors, eLife 5, e13977. doi: 10.7554/eLife.13977. PMCID: PMC4758945
Zimanyi, C.M., Chen, P.Y.-T., Kang, G., Funk, M.A., and Drennan*, C.L. (2016) Molecular Basis for Allosteric Specificity Regulation in Class Ia Ribonucleotide Reductase from Escherichia coli, eLife5, e07141. doi: 10.7554/eLife.07141. PMCID: PMC4728125
Highlighted by MIT News, Science 2.0, and Chemie.de: “DNA Supply Chain: Chemists Discover How a Single Enzyme Maintains a Cell’s Pool of DNA Building Blocks” by Anne Trafton. Highlighted by Genetic Engineering & Biotechnology News: “Strange Effector Mechanism Balances Inventory of DNA Building Blocks” Highlighted by spectroscopyNOW.com: “Balancing Building Blocks: RNR Enzyme X-rayed” by David Bradley.
Gibson, M.I., Chen, P.Y.-T., Johnson, A.C., Pierce, E., Can, M., Ragsdale, S.W., and Drennan*, C.L. (2016) One-carbon Chemistry of Oxalate Oxidoreductase Captured by X-Ray Crystallography, Proc. Natl. Acad. Sci. 113(2), 320-325. doi: 10.1073/pnas.1518537113. PMCID: PMC4720323. PMID: 26712008
Ando*, N., Li, H., Brignole, E.J., Thompson, S., McLaughlin, M.I., Page, J.E., Asturias, F.J., Stubbe, J., and Drennan*, C.L. (2016) Allosteric Inhibition of Human Ribonucleotide Reductase by dATP Entails the Stabilization of a Hexamer, Biochemistry55(2), 373-381. doi: 10.1021/acs.biochem.5b01207. PMCID: PMC4722859
Jost, M., Born, D.A., Cracan, V., Banerjee, R., and Drennan*, C.L. (2015) Structural Basis for Substrate Specificity in Adenosylcobalamin-Dependent Isobutyryl-CoA Mutase and Related Acyl-CoA Mutases, J. Biol. Chem. 290(45), 26882-26898. doi: 10.1074/jbc.M115.676890. PMCID: PMC4646380
Highlighted as JBC (2015) Paper of the Week: “Better Understanding Substrate Specificity of Acyl-CoA Mutase Has Implications for Biotechnology and Bioengineering” vol. 290, 26899. First Author Profile: Marco Jost. Selected for JBC: Virtual Issue on Enzymology.
Jost, M., Fernández-Zapata, J., Polanco, M.C., Ortiz-Guerrero, J.M., Chen, P.Y.-T., Kang, G., Padmanabhan*. S., Elías-Arnanz*, M., and Drennan*, C.L. (2015) Structural Basis for Gene Regulation by a B12-Dependent Photoreceptor, Nature 526(7574), 536-541. doi: 10.1038/nature14950. PMCID: PMC4634937. PMID: 26416754
Highlighted by MIT News, MIT’s ChemFormations, Crystallography News, and Proteomics News: “A Natural Light Switch” by Peter Dizikes. Highlighted in C&EN: “Vitamin B-12 Expands its Regulatory Role” by Stephen K. Ritter, October 5, 2015. Highlighted in Cell (2015): “Seeing the Light through Borrowed Lenses” by Mirna Kvajo vol. 163, 1295. Highlighted in Angewandte Chemie (2016): “Coenzyme B12 Repurposed for Photoregulation of Gene Expression” by Karl Gruber and Bernhard Kraütler vol. 55, 5638-5640.
Jost, M., Simpson, J.H., and Drennan*, C.L. (2015) The Transcription Factor CarH Safeguards Use of Adenosylcobalamin as a Light Sensor by Altering the Photolysis Products, Biochemistry 54(21), 3231-3234. doi: 10.1021/acs.biochem.5b00416. PMCID: PMC4455981
Bewley, K.D., Dey, M., Bjork, R.E., Mitra, S., Chobot, S.E., Drennan, C.L., and Elliott*, S.J. (2015) Rheostat Re-Wired: Alternate Hypotheses for the Control of Thioredoxin Reduction Potentials, PLoS ONE 10(4), e0122466. doi: 10.1371/journal.pone.0122466. PMCID: PMC4395160
Mattaini, K.R., Brignole, E.J., Kini, M., Davidson, S.M., Fiske, B.P., Drennan, C.L., and Vander Heiden*, M.G. (2015) An Epitope Tag Alters Phosphoglycerate Dehydrogenase Structure and Impairs Ability to Support Cell Proliferation, Cancer Metab. 3, 5. doi: 10.1186/s40170-015-0131-7. PMCID: PMC4414297
Funk, M.A., Marsh, E.N.G., and Drennan*, C.L. (2015) Substrate-Bound Structures of Benzylsuccinate Synthase Reveal How Toluene is Activated in Anaerobic Hydrocarbon Degradation, J. Biol. Chem. 290(37), 22398-22408. doi: 10.1074/jbc.M115.670737. PMCID: PMC4566215. PMID: 26224635
Gibson, M.I., Brignole, E.J., Pierce, E., Can, M., Ragsdale, S.W., and Drennan*, C.L. (2015) The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism, Biochemistry 54(26), 4112-4120. doi: 10.1021/acs.biochem.5b00521. PMCID: PMC4498597
Chang, S.-c., Fedeles, B.I., Wu, J., Delaney, J.C., Li, D., Zhao, L., Christov, P.P., Yau, E., Singh, V., Jost, M., Drennan, C.L., Marnett, L.J., Rizzo, C.J., Levine, S.S., Guengerich, F.P., and Essigmann*, J.M. (2015) Next-Generation Sequencing Reveals the Biological Significance of the N2,3-Ethenoguanine Lesion in vivo, Nucleic Acids Res. 43(11), 5489-5500. doi: 10.1093/nar/gkv243. PMCID: PMC4477646
Highlighted by MIT News: “New Evidence for How a Rare Form of Liver Cancer Arises” by Anne Trafton. NAR Breakthrough Article.
Jost, M., Cracan, V., Hubbard, P.A., Banerjee, R., and Drennan*, C.L. (2015) Visualization of a Radical B12 Enzyme with its G-protein Chaperone, Proc. Natl. Acad. Sci. 112(8), 2419-2424. doi: 10.1073/pnas.1419582112. PMCID: PMC4345561
Gagnon, D.M., Brophy, M.B., Bowman, S.E.J., Stich, T.A., Drennan, C.L., Britt*, R.D., and Nolan*, E.M. (2015) Manganese Binding Properties of Human Calprotectin Under Conditions of High and Low Calcium: X-ray Crystallographic and Advanced Electron Paramagnetic Resonance Spectroscopic Analysis, J. Am. Chem. Soc. 137(8), 3004-3016. doi: 10.1021/ja512204s. PMCID: PMC4354957
Grell, T.A.J., Goldman, P.J., and Drennan*, C.L. (2015) SPASM and Twitch Domains in S–Adenosylmethionine (SAM) Radical Enzymes, J. Biol. Chem. 290(7), 3964-3971. doi: 10.1074/jbc.R114.581249. PMCID: PMC4326806
Highlighted on cover of JBC February 13, 2015
Setser, J.W., Heemstra, J.R. Jr., Walsh, C.T., and Drennan*, C.L. (2014) Crystallographic Evidence of Drastic Conformational Changes in the Active Site of a Flavin-Dependent N-Hydroxylase, Biochemistry 53(38), 6063-6077. doi: 10.1021/bi500655q. PMCID: PMC4179590
Wei*, Y., Funk, M.A., Rosado, L.A., Baek, J., Drennan*, C.L., and Stubbe*, J. (2014) The Class III Ribonucleotide Reductase from Neisseria bacilliformis Can Utilize Thioredoxin as a Reductant, Proc. Natl. Acad. Sci. 111(36), E3756-E3765. doi: 10.1073/pnas.1414396111. PMCID: PMC4246965
Liu, D.S., Nivón, L.G., Richter, F., Goldman, P.J., Deerinck, T.J., Yao, J.Z., Richardson, D., Phipps, W.S., Ye, A.Z., Ellisman, M.H., Drennan, C.L., Baker, D., and Ting*, A.Y. (2014) Computational Design of a Red Fluorophore Ligase for Site-Specific Protein Labeling Inside Living Cells, Proc. Natl. Acad. Sci. 111(43), E4551-E4559. doi: 10.1073/pnas.1404736111. PMCID: PMC4217414
Funk, M.A., Judd, E.T., Marsh, E.N.G., Elliott, S.J., and Drennan*, C.L. (2014) Structures of Benzylsuccinate Synthase Elucidate Roles of Accessory Subunits in Glycyl Radical Enzyme Activation and Activity, Proc. Natl. Acad. Sci. 111(28), 10161-10166. doi: 10.1073/pnas.1405983111. PMCID: PMC4104874. PMID: 24982148
Dowling, D.P., Bruender, N.A., Young, A.P., McCarty, R.M., Bandarian, V., and Drennan*, C.L. (2014) Radical SAM Enzyme QueE Defines a New Minimal Core Fold and Metal-Dependent Mechanism, Nat. Chem. Biol. 10(2), 106-112. doi: 10.1038/nchembio.1426. PMCID: PMC3939041
Goldman, P.J., Grove, T.L., Booker, S.J., and Drennan*, C.L. (2013) X-ray Analysis of Butirosin Biosynthetic Enzyme BtrN Redefines Structural Motifs for AdoMet Radical Chemistry, Proc. Natl. Acad. Sci. 110(40), 15949-15954. doi: 10.1073/pnas.1312228110. PMCID: PMC3791736
Goldman, P.J., Grove, T.L., Sites, L.A., McLaughlin, M.I., Booker, S.J., and Drennan*, C.L. (2013) X-Ray Structure of an AdoMet Radical Activase Reveals an Anaerobic Solution for Formylglycine Posttranslational Modification, Proc. Natl. Acad. Sci. 110(21), 8519-8524. doi: 10.1073/pnas.1302417110. PMCID: PMC3666706
Li, D., Fedeles, B.I., Shrivastav, N., Delaney, J.C., Yang, X., Wong, C., Drennan, C.L., and Essigmann*, J.M. (2013) Removal of N-Alkyl Modifications from N2-Alkylguanine and N4-Alkylcytosine by the Adaptive Response Protein AlkB, Chem. Res. Toxicol. 26(8), 1182-1187. doi: 10.1021/tx400096m. PMCID: PMC3748507
Sydor, A.M., Jost, M., Ryan, K.S., Turo, K.E., Douglas, C.D., Drennan*, C.L., and Zamble*, D.B. (2013) Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases, Biochemistry 52(10), 1788-1801. doi: 10.1021/bi301600z. PMCID: PMC3596956
Kulik*, H.J., and Drennan, C.L. (2013) Substrate Placement Influences Reactivity in Non-Heme Fe(II) Halogenases and Hydroxylases, J. Biol. Chem. 288(16), 11233-11241. doi: 10.1074/jbc.M112.415570. PMCID: PMC3630895
Minnihan, E.C., Ando, N., Brignole, E.J., Olshansky, L., Chittuluru, J., Asturias*, F.J., Drennan*, C.L., Nocera*, D.G., and Stubbe*, J. (2013) Generation of a Stable, Aminotyrosyl Radical-Induced α2β2 Complex of Escherichia coli Class Ia Ribonucleotide Reductase, Proc. Natl. Acad. Sci. 110(10), 3835-3840. doi: 10.1073/pnas.1220691110. PMCID: PMC3593893
Chang, W.-C., Dey, M., Liu, P., Mansoorabadi, S.O., Moon, S.-J., Zhao, Z.K., Drennan, C.L., and Liu*, H.-W. (2013) Mechanistic Studies of an Unprecedented Enzyme-catalyzed 1,2-Phosphono-Migration Reaction, Nature 496(7443), 114-118. doi: 10.1038/nature11998. PMCID: PMC3725809
Brignole‡, E.J., Ando‡, N., Zimanyi, C.M., and Drennan*, C.L. (2012) The Prototypic Class Ia Ribonucleotide Reductase from Escherichia coli: Still Surprising After All These Years, Biochem. Soc. Trans.40(3), 523-530. doi: 10.1042/BST20120081. PMCID: PMC5912335.
Li, D., Delaney, J.C., Page, C.M., Yang, X., Chen, A.S. Wong, C., Drennan, C.L., and Essigmann*, J.M. (2012) Exocyclic Carbons Adjacent to the N6 of Adenine are Targets for Oxidation by the Escherichia coli Adaptive Response Protein AlkB, J. Am. Chem. Soc.134(21), 8896-8901. doi: 10.1021/ja3010094. PMCID: PMC3363417
Ando, N., Kung, Y., Can, M., Bender, G., Ragsdale, S.W., and Drennan*, C.L. (2012) Transient B12–Dependent Methyltransferase Complexes Revealed by Small-Angle X-Ray Scattering, J. Am. Chem. Soc.134(43), 17945-17954. doi: 10.1021/ja3055782. PMCID: PMC3484714
Hamill, M.J., Jost, M., Wong, C., Bene, N.C., Drennan, C.L., and Elliott*, S.J. (2012) Electrochemical Characterization of Escherichia coli Adaptive Response Protein AidB, Int. J. Mol. Sci. 13(12), 16899-16915. doi: 10.3390/ijms131216899. PMCID: PMC3546729
Bewley, K.D., Firer-Sherwood, M.A., Mock, J.-Y., Ando, N., Drennan, C.L., and Elliott*, S.J. (2012) Mind the Gap: Diversity and Reactivity Relationships Among Multihaem Cytochromes of the MtrA/DmsE Family, Biochem. Soc. Trans.40(6), 1268-1273. doi: 10.1042/BST20120106. PMCID: PMC5906043
Goldman, P.J., Ryan, K.S, Hamill, M.J., Howard-Jones, A.R., Walsh, C.T., Elliott, S.J., and Drennan*, C.L. (2012) An Unusual Role for a Mobile Flavin in StaC-like Indolocarbazole Biosynthetic Enzymes, Chem. Biol 19(7), 855-865. doi: 10.1016/j.chembiol.2012.05.016. PMCID: PMC3437190
Highlighted as a Chem. Biol. (2012) Preview article: “Babysitting Flavin for Biosynthesis” by Shiou-Chuan Tsai vol. 19, 787-788.
Aye Y, Brignole EJ, Long MJC, Chittuluru J, Drennan CL, Asturias FJ, Stubbe* J. (2012) Clofarabine targets the large subunit (alpha) of human ribonucleotide reductase in live cells by assembly into persistent hexamers. Chemistry & Biology 19:799-805. Full text at Cell Press
Zimanyi CM, Ando N, Brignole EJ, Asturias FJ, Stubbe J, Drennan* CL. (2012) Tangled up in knots: Structures of inactivated forms of E. coli class Ia ribonucleotide reductase. Structure. 20(8):1374-1383. Full text at ScienceDirect
Dowling DP, Vey JL, Croft AK, Drennan* CL. (2012) Structural diversity in the AdoMet radical enzyme superfamily. Biochimica et Biophysica Acta (BBA): Proteins and Proteomics. 1824:1178-1195. Full text at ScienceDirect
Dowling DP, Croft AK, Drennan* CL. (2012) The radical use of Rossmann and TIM barrel architectures for controlling coenzyme B12 chemistry. Annual Review of Biophysics 41:403-427. Full text at Annual Reviews
Kung Y, Ando N, Doukov TI, Blasiak LC, Bender G, Seravalli J, Ragsdale SW, Drennan* CL. (2012) Visualizing molecular juggling within a B12-dependent methyltransferase complex. Nature 48:265-269. Full text at Nature
Setser JW, Lingaraju GM, Davis CA, Samson LD, Drennan* CL. (2012) Searching for DNA lesions: Structural evidence for lower- and higher-affinity DNA binding conformations of human alkyladenine DNA glycosylase. Biochemistry 51, 382-390. Full text at ACS Publications
Ando N, Brignole EJ, Zimanyi CM, Funk MA, Yokoyama K, Asturias FJ, Stubbe J, Drennan* CL. (2011) Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase. Proc. Natl. Acad. Sci. U.S.A. 108, 21046-21051. Full text at PNAS
Anderson WA, Amasino RM, Ares M Jr, Banerjee U, Bartel B, Corces VG, Drennan CL, Elgin SC, Epstein IR, Fanning E, Guillette LJ Jr, Handelsman J, Hatfull GF, Hoy RR, Kelley D, Leinwand LA, Losick R, Lu Y, Lynn DG, Neuhauser C, O’Dowd DK, Olivera T, Pevzner P, Richards-Kortum RR, Rine J, Sah RL, Strobel SA, Walker GC, Walt DR, Warner IM, Wessler S, Willard HF, Zare RN. (2011) Competencies: A cure for pre-med curriculum. Science 334:760-761. Full text at Science
Hamill‡ MJ, Jost‡ M, Wong C, Elliott* SJ, Drennan* CL. (2011) Flavin-induced oligomerization in Escherichia coli adaptive response protein AidB. Biochemistry 50:10159-10169. Full text at ACS Publications
Firer-Sherwood‡ MA, Ando‡ N, Drennan CL, Elliott* SJ. (2011) Solution-based structural analysis of the decaheme cytochrome, MtrA, by small-angle X-ray scattering and analytical ultracentrifugation. J. Phys. Chem. B 115:11208-11214. Full text at ACS Publications
Anderson WA, Banerjee U, Drennan CL, Elgin SC, Epstein IR, Handelsman J, Hatfull GF, Losick* R, O’Dowd* DK, Olivera BM, Strobel SA, Walker GC, Warner IM. (2011) Changing the culture of science education at research universities. Science 331:152-153. Full text at Science
Yun D, Dey M, Higgins LJ, Yan F, Liu H-W, Drennan* CL. (2011) Structural basis of regiospecificity of a mononuclear iron enzyme in antibiotic fosfomycin biosynthesis. J. Am. Chem. Soc. 131:11262-11269. Full text at ACS Publications
Lingaraju GM, Davis CA, Setser JW, Samson* LD, Drennan* CL. (2011) Structural basis for the inhibition of human alkyladenine DNA glycosylase (AAG) by 3,N4-ethenocytosine–containing DNA. J. Biol. Chem. 286:13205-13213. Full text at JBC
Vey JL, Drennan* CL. (2011) Structural insights into radical generation by the radical SAM superfamily. Chem. Rev. 111:2487-2506. Full text at ACS Publications
Kung Y, Drennan* CL. (2011) A role for nickel-iron cofactors in biological carbon monoxide and carbon dioxide utilization. Curr. Opin. Biol. Chem. 15:276-283. Full text at ScienceDirect
Li D, Delaney J, Page C, Chen A, Wong C, Drennan CL, Essigmann* JM. (2010) Repair of DNA alkylation damage by the Escherichia coli adaptive response protein AlkB as studied by ESI-TOF mass spectrometry. J. Nucleic Acids 2010:369434. doi: 10.4061/2010/369434.
Drennan CL. (2010) In the nickel of time. Nat. Chem. 2:900. Full text
Phillips CM, Schreiter ER, Stultz CM, Drennan* CL. (2010) Structural basis of low-affinity nickel binding to the nickel-responsive transcription factor NikR from Escherichia coli. Biochemistry. 49:7830-7838. Full text at ACS Publications
Phillips CM, Stultz CM, and Drennan* CL. (2010) Searching for the nik operon: How a ligand-responsive transcription factor hunts for its DNA binding site. Biochemistry. 49:7757-7763. Full text
Taylor* EV, Fortune JA, Drennan CL. (2010) A research-inspired laboratory sequence investigating acquired drug resistance. Biochem. Mol. Biol. Educ. 38:247-252. Full text
Taylor* EV, Mitchell R, Drennan CL. (2009) Creating an interdisciplinary introductory chemistry course without time-intensive curriculum changes. ACS Chem. Biol. 4:979-982. Full text at ACS Publications
Kulik* HJ, Blasiak LC, Marzari N, Drennan CL. (2009) First-principles study of non-heme Fe(II) halogenase SyrB2 reactivity. J. Am. Chem. Soc. 131:14426-14433. Full text at ACS Publications
Drennan* CL, Jarrett* JT. (2009) From single molecules to whole organisms: The evolving field of mechanistic enzymology. Curr. Opin. Chem. Biol. 13:433-435. Full text
Kung Y, Doukov TI, Seravalli J, Ragsdale SW, Drennan* CL. (2009) Crystallographic snapshots of cyanide- and water-bound C-Clusters from bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Biochemistry. 48(31):7432-7440. Full text at ACS Publications
Phillips CM, Nerenberg PS, Drennan CL, Stultz* CM. (2009) Physical basis of metal-binding specificity in Escherichia coli NikR. J. Am. Chem. Soc. 131(29):10220-10228. Full text at ACS Publications
Ryan KS, Drennan* CL. (2009) Divergent pathways in the biosynthesis of bisindole natural products. Chem. Biol. 16:351-364. Full article
Wong C, Fujimori DG, Walsh CT, Drennan* CL. (2009) Structural analysis of an open active site conformation of nonheme iron halogenase CytC3. J. Am. Chem. Soc. 131:4872-4879. Full text at ACS Publications
Blasiak, LC and Drennan* CL. (2009) Structural perspective on enzymatic halogenation. Acc. Chem. Res. 42(1):147-155. Full text at ACS Publications
Ryan KS, Chakraborty S, Howard-Jones AR, Walsh CT, Ballou DP, Drennan* CL. (2008) The FAD cofactor of RebC shifts to an IN conformation upon flavin reduction. Biochemistry. 47:13506-13513. Full text at ACS Publications
Vey JL, Yang J, Li M, Broderick WE, Broderick JB, Drennan* CL. (2008) Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme. Proc. Natl. Acad. Sci. U.S.A. 105(42):16137-16141. Full article
Phillips CM, Drennan CL. (2008) Nickel regulatory transcription factor, NikR. Handbook of Metalloproteins, Wiley.
Blasiak LC, Drennan CL. (2008) Nonheme iron halogenases. Handbook of Metalloproteins, Wiley.
Hernandez HH, Jaquez OA, Hamill MJ, Elliott SJ, Drennan* CL. (2008) Thioredoxin reductase from Thermoplasma acidophilum: A new twist on redox regulation. Biochemistry. 47(37):9728-9737. Full text at ACS Publications
Hamill MJ, Chobot SE, Hernandez HH, Drennan CL, Elliott* SJ. (2008) Direct electrochemical analyses of a thermophilic thioredoxin reductase: Interplay between conformational change and redox chemistry. Biochemistry. 47(37):9738-9746. Full text at ACS Publications
Ryan KS, Balibar CJ, Turo KE, Walsh CT, Drennan* CL. (2008) The violacein biosynthetic enzyme VioE shares a fold with lipoprotein transporter proteins. J. Biol. Chem. 283(10):6467-6475. Full article
Doukov TI, Blasiak LC, Seravalli J, Ragsdale SW, Drennan* CL. (2008) Xenon in and at the end of the tunnel of bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Biochemistry 47(11):3474-3483. Full text at ACS Publications
Phillips CM, Schreiter ER, Guo Y, Wang SC, Zamble DB, Drennan* CL. (2008) Structural basis of the metal specificity for nickel regulatory protein NikR. Biochemistry 47(7):1938-1946. Full text at ACS Publications
Hubbard PA, Padovani D, Labunska T, Mahlstedt SA, Banerjee R, Drennan* CL. (2007) Crystal structure and nutagenesis of the netallochaperone MeaB. J. Biol. Chem. 282(43):31308-31316. Full article
Ryan KS, Howard-Jones AR, Hamill MJ, Elliott SJ, Walsh CT, Drennan* CL. (2007) Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC. Proc. Natl. Acad. Sci. U.S.A. 104(39):15311-15316. Full article
Schreiter* ER, Drennan CL. (2007) Ribbon-helix-helix transcription factors: Variations on a theme. Nat. Rev. Microbiol. 5(9):710-720. Full article
Chobot SE, Hernandez HH, Drennan CL, Elliott* SJ. (2007) Direct electrochemical characterization of archeael thioredoxins. Angew. Chem. Int. Ed. Engl. 46(22):4145-4147. Full article
Doukov‡ TI, Hemmi‡ H, Drennan CL, Ragsdale* SW. (2007) Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer: Role of an active site asparagine residue in activation of methyl transfer by methyltransferases. J. Biol. Chem. 282(9):6609-6618. Full article
Yeh E, Blasiak LC, Koglin A, Drennan CL, Walsh* CT. (2007) Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases. Biochemistry. 46(5):1284-1292. Full article
Frick LE, Delaney JC, Wong C, Drennan CL, Essigmann* JM. (2007) Alleviation of 1,N6-ethanoadenine genotoxicity by the Escherichia coli adaptive response protein AlkB. Proc. Natl. Acad. Sci. U.S.A. 104(3):755-760. Full article
Blasiak LC, Vaillancourt FH, Walsh CT, Drennan* CL. (2006) Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis. Nature. 440:368-371. Full article
Schreiter ER, Wang SC, Zamble DB, Drennan* CL. (2006) NikR-operator complex structure and the mechanism of repressor activation by metal ions. Proc. Natl. Acad. Sci. U.S.A. 103(37):13676-13681. Full article
Delaney JC, Smeester L, Wong C, Frick LE, Taghizadeh L, Wishnok JS, Drennan CL, Samson LD, Essigmann* JM. (2005) AlkB reverses etheno DNA lesions caused by lipid oxidation in vitro and in vivo. Nat. Struct. Mol. Biol. 12(10):855-860. Full article
Higgins LJ, Yan F, Liu P, Liu H-W, Drennan* CL. (2005) Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature 437:838-844. Full article
Berkovitch F, Behshad E, Tang KH, Enns EA, Frey PA, Drennan* CL. (2004) A locking mechanism preventing radical damage in the absence of substrate, as revealed by the X-ray structure of lysine-5,6-aminomutase. Proc. Natl. Acad. Sci. U.S.A. 101(45):15870-15875. Full article
Midelfort KS, Hernandez HH, Lippow SM, Tidor* B, Drennan* CL, Wittrup* KD. (2004) Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody. J. Mol. Biol. 343(3):685-701. Full article
Tirupati B, Vey JL, Drennan CL, Bollinger* Jr. JM. (2004) Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803. Biochemistry 43:12210-12219. Full article
Nicolet Y, Drennan* CL. (2004) AdoMet radical proteins—from structure to evolution: Alignment of divergent protein sequences reveals strong secondary structure element conservation. Nucleic Acids Res. 32:4015-4025. Full article
Drennan* CL, Doukov* TI, Ragsdale* SW. (2004) The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: A story in pictures. J. Biol. Inorg. Chem. 9:511-515. Full article
Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan* CL. (2004) Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 303(5654):76-79. Full article
Schreiter ER, Sintchak MD, Guo Y, Chivers PT, Sauer RT, Drennan* CL. (2003) Crystal structure of the nickel-responsive transcription factor NikR. Nat. Struct. Biol. 10(10):794-799. Full article
Drennan* CL, Peters* JW. (2003) Surprising cofactors in metalloenzymes. Curr. Opin. Struct. Biol. 13(2):220-226. Full article
Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan* CL. (2002) A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 298(5593):567-572. Full article
Sintchak MD, Arjara G, Kellogg BA, Stubbe J, Drennan* CL. (2002) The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer. Nat. Struct. Biol. 9(4):293-300. Full article
Drennan* CL, Heo J, Sintchak MD, Schreiter E, Ludden PW. (2001) Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 98(21):11973-11978. Full article
Marsh* EN, Drennan CL. (2001) Adenosylcobalamin-dependent isomerases: New insights into structure and mechanism. Curr. Opin. Chem. Biol. 5(5):499-505. Full article