Publications

Found 69 results
Filters: Author is Drennan, Catherine L  [Clear All Filters]
Journal Article
Wong, C., Fujimori, D. Galonić, Walsh, C. T., and Drennan, C. L. (2009) Structural analysis of an open active site conformation of nonheme iron halogenase CytC3. J Am Chem Soc. 131, 4872-9
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, 11978-11982
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 Ni-Fe Carbon Monoxide Dehydrogenase. ACS Catal. 10, 7328-7335
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., and Moore, B. S. (2024) A single diiron enzyme catalyses the oxidative rearrangement of tryptophan to indole nitrile. Nat Chem. 16, 1989-1998
Chen, P. Yang- Ting, Li, B., Drennan, C. L., and Elliott, S. J. (2019) A reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes C-C bonds from CO. Joule. 3, 595-611
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. Elife. 10.7554/eLife.39451
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, 106-12
Coco, L. B., Toci, E. M., Chen, P. Yang- Ting, Drennan, C. L., and Meyers, C. L. Freel (2024) Potent Inhibition of DXP Synthase by a -Diaryl Bisubstrate Analog. ACS Infect Dis. 10, 1312-1326
Adak, S., Ye, N., Calderone, L. A., Schäfer, R. J. B., Lukowski, A. L., Pandelia, M. - E., Drennan, C. L., and Moore, B. S. (2023) Oxidative rearrangement of tryptophan to indole nitrile by a single diiron enzyme. bioRxiv. 10.1101/2023.08.03.551874
Gibson, M. I., Chen, P. Yang- Ting, 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 U S A. 113, 320-5
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. 10.1021/jacs.7b01212
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. 10.1016/j.chembiol.2021.03.001
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 Acids Res. 44, 9965-9976
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, 1206-1216
Backman, L. Rf, 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 -4-hydroxy-L-proline by a microbial glycyl radical enzyme. Elife. 10.7554/eLife.51420
Zimanyi, C. M., Chen, P. Yang- Ting, Kang, G., Funk, M. A., and Drennan, C. L. (2016) Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli. Elife. 5, e07141
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, 1788-1801
Gagnon, D. M., Brophy, M. Brunjes, Bowman, S. E. J., Stich, T. A., Drennan, C. L., R Britt, 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, 3004-16
Berkovitch, F., Behshad, E., Tang, K. - H., Enns, E. A., Frey, P. A., and Drennan, C. L. (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, 15870-5
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 Chem Int Ed Engl. 57, 9707-9710
Andree, G. A., Miller-Brown, K. R., Zhao, Z., Smith, A. K., Dawson, C. D., Deredge, D. J., and Drennan, C. L. (2025) How ATP and dATP reposition class III ribonucleotide reductase cone domains to regulate enzyme activity. Sci Adv. 11, eady9156
Funk, M. A., Zimanyi, C. M., Andree, G. A., Hamilos, A. E., and 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. 63, 2517-2531
Bridwell-Rabb, J., Kang, G., Zhong, A., Liu, H. -wen, and Drennan, C. L. (2016) An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis. Proc Natl Acad Sci U S A. 113, 13750-13755
Hamill, M. J., Jost, M., Wong, C., Elliott, S. J., and Drennan, C. L. (2011) Flavin-induced oligomerization in Escherichia coli adaptive response protein AidB. Biochemistry. 50, 10159-69
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 Lett. 11, 1980-1985

Pages