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  Brad S. Pierce          

Phone: 817-272-9066     FAX: 817-272-3808     E-mail: bspierce@uta.edu     Office: 300F SH      Personal Page

Research interests:

Bioinorganic chemistry

Biophysical chemistry and Spectroscopy

Mechanistic metalloenzymology

Research in the Pierce group focuses on the interface of inorganic chemistry and biology. Approximately one third of all proteins contain a catalytically or structurally essential metal cofactor (V, Cr, Mn, Fe, Co, Ni, Cu, Zn, Mo, and W). In most instances the high selectivity, regiospecificity, and chemical reactivity associated with a metalloenzyme is regulated by outer sphere protein-ligand, protein-protein, and even protein-DNA interactions. Thus, central to our understanding of biological chemistry is how these interactions modulate the physical properties of the metal within the enzymatic active site.

Current projects within the Pierce group:

1. Characterization of mammalian thiol dioxygenase enzymes.
2. Mechanisms of bacterial environmental adaptation to oxidative stress.
3. Non-heme diiron enzymes involved in post-transcriptional modification of tRNA.

Given the breadth of research within the field of bioinorganic chemistry students in the Pierce lab have the opportunity to learn from a variety of skills ranging from traditional biochemistry (cloning and recombinant DNA technology, expression by bacterial fermentation, and enzyme kinetics) to inorganic spectroscopic methods (UV-visible, EPR, and Mössbauer spectroscopy).

Selected Recent Publications:

Lucas J. Bailey, Nathaniel L. Elsen, Brad S. Pierce, Brian G. Fox “Soluble Expression and Purification of the Oxidoreductase Component of Toluene-4-Monooxygenase” Protein Expr. Purif. 2008, 57(1), 9-16. (Epub 2007 Sep 19)

Brad S. Pierce, Jessica D. Gardner, Lucas J. Bailey, Thomas C. Brunold, and Brian G. Fox “Characterization of the Nitrosyl Adduct of Substrate-Bound Mouse Cysteine Dioxygenase by Electron Paramagnetic Resonance: Electronic Structure of the Active Site and Mechanistic Implications” Biochemistry 2007, 46(29), 8569-78.

George N. Phillips, Jr., Brian G. Fox, John L. Markley, Euiyoung Bae, Eduard Bitto, Craig A. Bingman, Ronn Frederick, Jason McCoy, Brad Pierce,  Jikui Song, Brian Volkman “Structures of Proteins of Biomedical Interest from the Center for Eukaryotic Structural Genomics” J. Struct. Funct. Genomics 2007, 8(2-3),73-84. (Epub 2007 Sep 6)

Brad S. Pierce and Michael P. Hendrich; “Local and Global Effects of Metal Binding Within the small Subunit of Ribonucleotide Reductase” J. Am. Chem. Soc. 2005, 127(10),  3613-3623.

Brad S. Pierce, Timothy E. Elgren, and Michael P. Hendrich; “Mechanistic Implications for the Formation of the Diiron Cluster in Ribonucleotide Reductase Provided by Quantitative EPR Spectroscopy” J. Am. Chem. Soc. 2003, 125(29), 8748-8759.

David M. Arciero, Brad S. Pierce, Michael P. Hendrich, and Alan B. Hooper; “Nitrosocyanin, a Red Cupredoxin-like Protein from Nitrosomonas europaea” Biochemistry 2002, 41(6), 1703-1709.  (Accelerated Publication)

Dongwhan, Lee, Brad Pierce, Carsten Krebs, Michael P. Hendrich, Boi Hanh Huynh, and Stephan J. Lippard; “Functional Mimic of Dioxygen-Activating Centers in Non-Heme Diiron Enzymes: Mechanistic Implication of Paramagnetic Intermediates in the Reactions between Diiron(II) Complexes and Dioxygen” J. Am. Chem. Soc. 2002, 124(15), 3993-4007.

 Dongwhan Lee, Jennifer L. DuBois, Brad Pierce, Britt Hedman, Keith O. Hodgson, Michael P. Hendrich, and Stephan J. Lippard; “Structural and Spectroscopic Studies of Valence-Delocalized Diiron(II, III) Complexes Supported by Carboxylate-Only Bridging Ligands” Inorg. Chem. 2002, 41(12), 3172-3182.

Department of Chemistry and Biochemistry
The University of Texas at Arlington
Arlington, Texas 76019-0065, USA
Phone: 817-272-3171 | Fax: 817-272-3808
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