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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

 

 

 

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, 201352, 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., 201217, 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 201251, 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 201049, 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 201049, 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. 20106, 387-393.

 

 

 

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.

 

 

Flavo–Diiron Enzymes: Nitric Oxide or Dioxygen Reductases?
Kurtz, D. M., Jr. Flavo-Diiron
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

 

 

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.

 

 

 

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.

 

 

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.

 

 

 

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.

 

 

 

 

 

 

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