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Faculty
     
 
Donald Kurtz Jr.

Lutcher Brown Distinguished Professor

Office Phone: (210) 458-7060
Office: BSE 4.324
E-Mail: donald.kurtz@utsa.edu

Areas of Specialization
• Bioinorganic chemistry
• Non-heme iron enzymes





Research Interests

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.

 

 

 

 





Selected Publications

 

 

 

 H2O2-dependent Substrate Oxidation by an Engineered Diiron Site in a Bacterial Hemerythrin

Yasunori Okamoto, Akira Onoda, Hiroshi Sugimoto, Yu Takano, Shun Hirota, Donald M. Kurtz, Yoshitsugu Shiro, Takashi Hayashi
Chem. Commun., 2014, 50, 3421-3423.

 

 

 

 Iron: Non-Heme Proteins with Diiron-Carboxylate Active Sites

Kurtz, D.M., Boice, E., Caranto, J.D., Frederick, R.E., Masitas, C.A. Miner, K.D.
Encyclopedia of Inorganic and Bioinorganic Chemistry, 2013.

 

 

 

 Crystal Structure, Exogenous Ligand Binding, and Redox Properties of an Engineered Diiron Active Site in a Bacterial Hemerythrin

Yasunori Okamoto, Akira Onoda, Hiroshi Sugimoto, Yu Takano, Shun Hirota, Donald M. Kurtz, Jr., Yoshitsugu Shiro, Takashi Hayashi
Inorg. Chem., 2013, 52 (22), 13014Ė13020.

 

 

 

 An HD-GYP Cyclic-Di-Guanosine Monophosphate Phosphodiesterase with a Non-Heme Diiron-Carboxylate Active Site

Miner, K.D., Klose, K.E., Kurtz, D.M., Jr.
Biochemistry, 2013, 52, 5329-5331.

 

 

 

 Histidine Ligand Variants of a Flavo-Diiron Protein: Effects on Structure and Activities

Fang, H., Caranto, J.D., Mendoza, R., Taylor, A.B., Hart, P.J., Kurtz, D.M., Jr.
J. Biol. Inorg. Chem., 2012, 17, 1231-1239.

 

 

 

 A Bacterial Hemerythrin Domain Regulates Activity of a Vibrio cholerae Di-Guanylate Cyclase

Schaller, R.A., Ali, S.K., Klose, K.E., Kurtz, D.M., Jr.
Biochemistry, 2012, 51, 8563–8570.

 

 

 

 Treponema denticola Superoxide Reductase: In Vivo Role, In Vitro Reactivities and a Novel [Fe(Cys)4] Site

Caranto, J.D., Gebhardt, L.L., MacGowan, C.E., Limberger, R.J., Kurtz, D.M., Jr.
Biochemistry, 2012, 51, 5601-5610.

 

 

 

 Vibrational Analysis of Mononitrosyl Complexes in Hemerythrin and Flavodiiron Proteins: Relevance to Detoxifying NO Reductase

Hayashi, T., Caranto, J.D., Matsumura, H., Kurtz, D.M., Jr., Moënne-Loccoz, P
J. Am. Chem. Soc., 2012, 134, 6878-6884.

 

 

 

 Insights into the Nitric Oxide Reductase Mechanism of Flavo-Diiron Proteins from a Flavin-Free Enzyme

Hayashi, T., Caranto, J. D., Wampler, D.A., Kurtz, D.M., Jr., Moënne-Loccoz, P.
Biochemistry, 2010, 49, 7040-7049.

 

 

 

 Iron-nucleated Folding of a Metalloprotein in High Urea: Resolution of Metal Binding and Protein Folding Events

Morleo, A., Bonomi, F., Iametti, S., Huang, V. W., Kurtz, D.M., Jr.
Biochemistry, 2010, 49, 6627-6634.

 

 

 

 Towards the Development of Hemerythrin-based Blood Substitutes

Mot, A.C., Roman, A., Lupan, I., Kurtz, D.M., Jr., Silaghi-Dumitrescu, R.
Protein. J., 2010, 6, 387-393.

 

 

 

 Folding of a Metalloprotein in High Urea: Resolution of Metal Binding and Protein Folding Events

Morleo, A., Bonomi, F., Iametti, S., Huang, V.W., Kurtz, D.M., Jr.
Biochemistry, 2010, 49, 6627-6634.

 

 

 

 Insights into the Nitric Oxide Reductase Mechanism of Flavo-Diiron Proteins from a Flavin-Free Enzyme

Hayashi, T., Caranto, J.D., Wampler, D.A., Kurtz, D.M., Jr., MoŽnne-Loccoz, P.
Biochemistry, 2010, 49, 7040-7049.

 

 

 

 Pathway for H2O2 and O2 Detoxification in Clostridium acetobutylicum

Riebe, O., Fischer, R.-J., Wampler, D.A., Kurtz, D.M., Jr., Bahl, H.
Microbiol., 2009, 155, 16-24.

 

 

 

 Reductive Dioxygen Scavenging by Clostridium acetobutylicum Flavo-Diiron Proteins

Hillman, F., Fischer, R.-J., Mot, A., Caranto, J.D., Kurtz, D.M., Jr., Bahl, H.
FEBS Lett., 2009, 583, 241-245.

 

 

 

 Towards the Development of Hemerythrin-based Blood Substitutes

Mot, A. C., Roman, A., Lupan, I., Kurtz, D.M., Jr., Silaghi-Dumitrescu, R.
FEBS Lett., 2009, 583, 241-245.

 

 

 

 "Iron Priming" Guides Folding of Denatured Aporubredoxins

Bonomi, F., Iametti, S., Ferranti, P., Kurtz, D. M., Jr., Morleo, A., Ragg, E. M.
J. Biol. Inorg. Chem., 2008, 13, 981-991.

 

 

 

 Flavo–Diiron Enzymes: Nitric Oxide or Dioxygen Reductases?

Kurtz, D.M., Jr.
Dalton Trans., 2007, 4115 - 4121.

 

 

 

 The Reaction of Desulfovibrio vulgaris Two-Iron Superoxide Reductase with Superoxide: Insights from Stopped-Flow Spectrophotometry

Huang, V. W., Emerson, J. P., Kurtz, D. M., Jr.
Biochemistry, 2007, 46, 11342-11351.

 

 

 

 Structural Basis for O2 Sensing by the Hemerythrin-like Domain of a Bacterial Chemotaxis Protein: Substrate Tunnel and
Fluxional N-terminus

Isaza, C., Silaghi-Dumitrescu, R., Iyer, R.B., Kurtz, D.M., Jr., Chan, M.K.
Biochemistry, 2006, 45, 9023-9031.

 

 

 

 

 

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