研究领域

Bioinorganichemistr ;Non-hemiroenzymes

A major aspect of our research focuses on the structure, function, and catalytic mechanisms of bacterial and archaeal non-heme iron enzymes that reductively scavenge diatomic oxygen and nitrogen species. These scavenging and sensing reactions require specialized active sites with novel iron coordination environments and novel mechanisms, which we follow by rapid kinetic and spectroscopic techniques as well as protein X-ray crystallography. We are also attempting to develop an oxygen-carrying protein as a blood substitute. A related project focuses on proteins that catalyze storage and release of intracellular iron. An exciting new development is the use of these iron storage proteins as scaffolds to enclose metal and semiconductor nanoparticles for photochemical H2 production and photo-initiated delivery of toxic iron to cancer cells.

近期论文

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Rosanne E. Frederick; Jonathan D. Caranto; Cesar A. Masitas; Linda L. Gebhardt; Charles E. MacGowan; Ronald J. Limberger; Donald M. Kurtz Dioxygen and nitric oxide scavenging by Treponema denticola flavodiiron protein: a mechanistic paradigm for catalysis Journal of Biological Inorganic Chemistry. 2015. 0 Matteo Miriani; Stefania Iametti; Donald M. Kurtz; Francesco Bonomi Rubredoxin refolding on nanostructured hydrophobic surfaces: Evidence for a new type of biomimetic chaperones Proteins: Structure, Function and Bioinformatics. 2014. 0 Jonathan D. Caranto; Andrew Weitz; Nitai Giri; Michael P. Hendrich; Donald M. Kurtz A diferrous-dinitrosyl intermediate in the N2O-generating pathway of a deflavinated flavo-diiron protein Biochemistry. 2014;53(35):5631-5637. 1 Yasunori Okamoto; Akira Onoda; Hiroshi Sugimoto; Yu Takano; Shun Hirota; Donald M. Kurtz; Yoshitsugu Shiro; Takashi Hayashi H2O2-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin Chemical Communications. 2014;50(26):3421-3423. 0 Denisa Hathazi; Augustin C. Mot; Anetta Vaida; Florina Scurtu; Iulia Lupan; Eva Fischer-Fodor; Grigore Damian; Donald M. Kurtz; Radu Silaghi-Dumitrescu Oxidative protection of hemoglobin and hemerythrin by cross-linking with a nonheme iron peroxidase: Potentially improved oxygen carriers for use in blood substitutes Biomacromolecules. 2014;15(5):1920-1927. 1 Jonathan D. Caranto; Andrew Weitz; Michael P. Hendrich; Donald M. Kurtz The nitric oxide reductase mechanism of a flavo-diiron protein: Identification of active-site intermediates and products Journal of the American Chemical Society. 2014;136(22):7981-7992. 5 Kyle D. Miner; Karl E. Klose; Donald M. Kurtz An HD-GYP cyclic di-guanosine monophosphate phosphodiesterase with a non-heme diiron-carboxylate active site Biochemistry. 2013;52(32):5329-5331. 4 Yasunori Okamoto; Akira Onoda; Hiroshi Sugimoto; Yu Takano; Shun Hirota; Donald M. Kurtz; Yoshitsugu Shiro; Takashi Hayashi Crystal structure, exogenous ligand binding, and redox properties of an engineered diiron active site in a bacterial hemerythrin Inorganic Chemistry. 2013;52(22):13014-13020. 1 Takahiro Hayashi; Jonathan D. Caranto; Hirotoshi Matsumura; Donald M. Kurtz; Pierre Moënne-Loccoz Vibrational analysis of mononitrosyl complexes in hemerythrin and flavodiiron proteins: Relevance to detoxifying no reductase Journal of the American Chemical Society. 2012;134(15):6878-6884. 13 Jonathan D. Caranto; Linda L. Gebhardt; Charles E. MacGowan; Ronald J. Limberger; Donald M. Kurtz Treponema denticola Superoxide Reductase: In Vivo Role, in Vitro Reactivities, and a Novel [Fe(Cys)4] Site Biochemistry. 2012;51(28):5601-5610. 2 Ruth A. Schaller; Syed Khalid Ali; Karl E. Klose; Donald M. Kurtz A bacterial hemerythrin domain regulates the activity of a Vibrio cholerae diguanylate cyclase Biochemistry. 2012;51(43):8563-8570. 5 Han Fang; Jonathan D. Caranto; Rosalinda Mendoza; Alexander B. Taylor; P. John Hart; Donald M. Kurtz Histidine ligand variants of a flavo-diiron protein: Effects on structure and activities Journal of Biological Inorganic Chemistry. 2012;17(8):1231-1239. 5 Anna Morleo; Francesco Bonomi; Stefania Iametti; Victor W. Huang; Donald M. Kurtz Jr. Iron-nucleated folding of a metalloprotein in high urea: Resolution of metal binding and protein folding events Biochemistry. 2010;49(31):6627-6634. 11 Takahiro Hayashi; Jonathan D. Caranto; David A. Wampler; Donald M. Kurtz Jr.; Pierre Moënne-Loccoz Insights into the nitric oxide reductase mechanism of flavodiiron proteins from a flavin-free enzyme Biochemistry. 2010;49(33):7040-7049. 18 Augustin C. Mot; Alina Roman; Iulia Lupan; Donald M. Kurtz Jr.; Radu Silaghi-Dumitrescu Towards the development of hemerythrin-based blood substitutes Protein Journal. 2010;29(6):387-393. 6 Falk Hillmann; Oliver Riebe; Ralf-Jörg Fischer; Augustin Mot; Jonathan D. Caranto; Donald M. Kurtz Jr.; Hubert Bahl Reductive dioxygen scavenging by flavo-diiron proteins of Clostridium acetobutylicum FEBS Letters. 2009;583(1):241-245. 18 Oliver Riebe; Ralf-Jorg Fischer; David A. Wampler; Donald M. Kurtz Jr.; Hubert Bahl Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum Microbiology. 2009;155(1):16-24. 31 Francesco Bonomi; Stefania Iametti; Pasquale Ferranti; Donald M. Kurtz Jr.; Anna Morleo; Enzio Maria Ragg Iron priming guides folding of denatured aporubredoxins Journal of Biological Inorganic Chemistry. 2008;13(6):981-991. 4 Donald M. Kurtz Jr. Flavo-diiron enzymes: Nitric oxide or dioxygen reductases? Dalton Transactions. 2007;(37):4115-4121. 29 Victor W. Huang; Joseph P. Emerson; Donald M. Kurtz Jr. Reaction of Desulfovibrio vulgaris two-iron superoxide reductase with superoxide: Insights from stopped-flow spectrophotometry Biochemistry. 2007;46(40):11342-11351.