Faculty Profiles

Katherine J. Franz
Katherine J. Franz
Chair of the Department of Chemistry
Office: 
2103 French Science Center, 124 Science Drive, Durham, NC 27708
Phone: 
(919) 660-1541
katherine.franz@duke.edu
Franz Research Group
Research Interests: 

Research in the Franz group is involved in elucidating the structural and functional consequences of metal ion coordination in biological systems. We are particularly interested in understanding the coordination chemistry utilized by biology to manage essential yet toxic species like copper and iron. Understanding these principles further guides our development of new chemical tools to manipulate biological metal ion location, speciation, and reactivity for potential therapeutic benefit. We use a combination of synthesis, spectroscopy, and biochemistry in our work. Please visit our group website to learn more about our research.

Overview

Education:

Ph.D., Massachusetts Institute of Technology 2000

B.A., Wellesley College 1995

Research Areas:
Biomolecular Structure and Function, Inorganic

Haas, Kathryn L., et al. “Model peptides provide new insights into the role of histidine residues as potential ligands in human cellular copper acquisition via Ctr1..” J Am Chem Soc, vol. 133, no. 12, Mar. 2011, pp. 4427–37. Pubmed, doi:10.1021/ja108890c. Full Text

Ciesienski, Katie L., and Katherine J. Franz. “Keys for unlocking photolabile metal-containing cages..” Angewandte Chemie (International Ed. in English), vol. 50, no. 4, Jan. 2011, pp. 814–24. Epmc, doi:10.1002/anie.201002542. Full Text

Rubino, Jeffrey T., et al. “A comparison of methionine, histidine and cysteine in copper(I)-binding peptides reveals differences relevant to copper uptake by organisms in diverse environments..” Metallomics : Integrated Biometal Science, vol. 3, no. 1, Jan. 2011, pp. 61–73.

Rubino, Jeffrey T., et al. “A comparison of methionine, histidine and cysteine in copper(I)-binding peptides reveals differences relevant to copper uptake by organisms in diverse environments..” Metallomics : Integrated Biometal Science, vol. 3, no. 1, Jan. 2011, pp. 61–73. Epmc, doi:10.1039/c0mt00044b. Full Text

Ciesienski, Katie L., et al. “Development of next-generation photolabile copper cages with improved copper binding properties..” Dalton Transactions (Cambridge, England : 2003), vol. 39, no. 40, Oct. 2010, pp. 9538–46. Epmc, doi:10.1039/c0dt00770f. Full Text Open Access Copy

Rubino, Jeffrey T., et al. “Methionine motifs of copper transport proteins provide general and flexible thioether-only binding sites for Cu(I) and Ag(I)..” Journal of Biological Inorganic Chemistry : Jbic : A Publication of the Society of Biological Inorganic Chemistry, vol. 15, no. 7, Sept. 2010, pp. 1033–49. Epmc, doi:10.1007/s00775-010-0663-9. Full Text

Ciesienski, Katie L., et al. “Toward the detection of cellular copper(II) by a light-activated fluorescence increase..” Inorganic Chemistry, vol. 49, no. 15, Aug. 2010, pp. 6808–10. Epmc, doi:10.1021/ic1004165. Full Text Open Access Copy

Ciesienski, K. L., et al. “A photo-caged platinum(II) complex that increases cytotoxicity upon light activation.” European Journal of Inorganic Chemistry, no. 15, May 2010, pp. 2224–28. Scopus, doi:10.1002/ejic.201000098. Full Text

Franz, Katherine J., and Chuan He. “The highways and byways of bioinorganic chemistry..” Current Opinion in Chemical Biology, vol. 14, no. 2, Apr. 2010, pp. 208–10. Epmc, doi:10.1016/j.cbpa.2010.02.011. Full Text

Folk, Drew S., and Katherine J. Franz. “A prochelator activated by beta-secretase inhibits Abeta aggregation and suppresses copper-induced reactive oxygen species formation..” Journal of the American Chemical Society, vol. 132, no. 14, Apr. 2010, pp. 4994–95. Epmc, doi:10.1021/ja100943r. Full Text Open Access Copy

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