The University of Texas at Arlington

Brad S. Pierce

Brad  Pierce

Assistant Professor

Office: 300F SH, Email: bspierce@uta.edu, Phone: 817-272-9066, FAX: 817-272-3808

Research ProfileCoursesPersonal Page

Modern research is frequently at the interface of (or crosses) traditional divisional boundaries within chemistry departments (organic, inorganic, analytical, biochemistry, and physical).  The breadth of research efforts conducted in the Pierce group embrace this interdisciplinary approach, thus providing training in methods and instrumentation typically outside traditional divisional boundaries.  Research in the Pierce group employs modern biophysical and bioinorganic techniques to investigate mechanisms of metalloenzyme function and regulation.  The scope of research in our group is fairly ambitious in that it spans work at the genetic level (PCR cloning, expression vector design, and site directed mutagenesis) all the way up to spectroscopic characterization (UV-visible, CD, EPR, and Mössbauer) of purified enzyme systems.  In particular, dual-mode EPR spectroscopy, in combination with spectroscopic simulations, is a highly sensitive method for probing the active site electronic structure of metalloenzymes.  Specific topics of interest to our group include the oxidation of sulfur-containing bimolecules, non-heme iron enzymes involved in tRNA modification, and pathogenic adaptation to oxidative/nitrosative stress.

Wei Li, Elizabeth J. Blaesi; Michael D. Pecore, Joshua K. Crowell, and Brad S. Pierce “Second-sphere interactions between the C93-Y157 cross-link and the substrate-bound Fe-site influence O2-coupling efficiency in mouse cysteine dioxygenase”; Biochemistry 2013 (Just Accepted); Publication Date (Web): November 26, 2013; DOI: 10.1021/bi4010232

Andra L. Corder, Bishnu P. Subedi, Siai Zhang, Amanda M. Dark, Frank W. Foss, Jr., and Brad S. Pierce “Peroxide-shunt substrate-specificity for the Salmonella typhimurium O2-dependent tRNA modifying monooxygenase (MiaE)”; Biochemistry 2013 52 (36) 6182-6196. PMID: 23906247.

Joshua A. Crawford, Wei Li, Brad S. Pierce “Single turnover of substrate-bound ferric cysteine dioxygenase (CDO) with superoxide anion: enzymatic reactivation, product formation, and a transient intermediate” Biochemistry, 2011, 50 (47), pp 10241–10253.

David M. Granum, Paul J. Riedel, Joshua A. Crawford, Thomas K. Mahle, Chelsea M. Wyss, Anastasia K. Begej, Navamoney Arulsamy, Brad S. Pierce, and Mark P. Mehn "Synthesis and Characterization of Sterically Encumbered ß-Ketoiminate Complexes of Iron(II) and Zinc(II)" Dalton Trans., 2011, 40 (22), 5881 - 589

Shane Z Sullivan; Alexandru S Biris; Sharon Pulla; Anna M Brezden; Samuel L Collom; Ross M Woods; Pradip Munshi; Laura Schnackenberg; Brad S. Pierce; Ganesh K Kannarpady; Anindya Ghosh "Fe Complex of a Tetraamido Macrocyclic Ligand: Spectroscopic Characterization and Catalytic Oxidation Studies" Chem Phys Lett 2010 (498) 359-365

Jessica D. Gardner; Brad S. Pierce, Brian G. Fox, and Thomas C. Brunold "Spectroscopic and Computational Characterization of Substrate-Bound Mouse Cysteine Dioxygenase: Nature of the Ferrous and Ferric Cysteine Adducts and Mechanistic Implications" Biochemistry 2010 (49) 6033-6041

Michelle Oppenheimer, Brad S. Pierce, Joshua A. Crawford, Keith Ray, Richard R. Helm, and Pablo Sobrado "Recombinant expression, purification, and characterization of ThmD, the oxidoreductase component of tetrahydrofuran monooxygenase" Biochimica et Biophysica Acta 2010 492(2); 423-31

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 Jan; 57 (1): 9-16

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 off Proteins of Biomedical Interest from the Center for Eukaryotic Structural Genomics" J. Struct Funct Genomics. 2007 Sep;8(2-3):73-84

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  (Recommended by Amy Rosenzweig: Faculty of 1000 Biology, 24 July 2003)  http://f1000biology.com/article/id/1009123/evaluation

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" Inorganic Chemistry, 2002, 41 (12), 3172-3182

B.S., Chemistry, California State University, Chico (1996)

Ph.D., Chemistry, Carnegie Mellon University (2003)
(Graduate advisor Michael P. Hendrich)

NIH NRSA Postdoctoral Fellow, University of Wisconsin-Madison (2004-2008)
(Laboratory of Brian Fox, Department of Biochemistry)

Brad Pierce joined the faculty of the department of Chemistry & Biochemistry at the University of Texas at Arlington in 2008. The breadth of research efforts conducted in the Pierce group follows an interdisciplinary approach; providing training in methods and instrumentation typically outside traditional divisional boundaries within chemistry departments (organic, inorganic, analytical, biochemistry, and physical).  Research in the Pierce group employs modern biophysical and bioinorganic techniques to investigate mechanisms of metalloenzyme function and regulation. The scope of research in our group is fairly ambitious in that it spans work at the genetic level (PCR cloning, expression vector design, and site directed mutagenesis) all the way up to spectroscopic characterization (UV-visible, CD, EPR, and Mössbauer) of purified enzyme systems. In particular, the Pierce group specializes in the use of dual-mode EPR spectroscopy which, in combination with spectroscopic simulations, is a highly sensitive method for probing the active site electronic structure of metalloenzymes.

In addition to this research, Dr. Pierce is a dedicated instructor.  Indeed, in 2012 Dr. Pierce was awarded the President’s Award for Excellence in Teaching for an untenured professor.  He currently offers courses in both biophysical chemistry and inorganic chemistry at the graduate and undergraduate level.  Prior to his appointment at UT-Arlington, Dr. Pierce was an NIH postdoctoral researcher in the lab of Professor Brian Fox (Department of Biochemistry) at the University of Wisconsin. Within the Fox lab, his work focused on the mechanistic investigation of non-heme iron metalloproteins and the protein-protein interactions which influence their O2- and substrate reactivity. In 2003, Dr. Pierce received his Doctorate in Chemistry from Carnegie Mellon University under the supervision of Professor Michael P. Hendrich.  His work focused on the use of dual-mode and multifrequency electron paramagnetic resonance (EPR) spectroscopy to characterize transition metal model complexes and metalloproteins.

Brad Pierce received his B.S in Chemistry with a minor in Biology from California State University at Chico. Following graduation, Dr. Pierce worked for several years as research associate within the drug delivery R&D division at Matrix Pharmaceuticals in Fremont, CA. At Matrix he assisted Dr. Kathy Roskos on the development and characterization of gel-based cisplatin/epinephrine antineoplastic formulations.  Dr. Pierce currently lives in Fort Worth with his wife Christy.

April 2013 President's Award for Excellence in Teaching, The University of Texas at Arlington
08/2012-07/2015
NSF-CHE (1213655), “Mechanistic and spectroscopic investigation of sulfur-oxidizing non-heme iron enzymes
04/2012-04/2013 The University of Texas at Arlington (Research Enhancement Award), “A proton-inventory study of substrate binding in cysteine dioxygenase
2011-present Co-coordinator for the U.S. National Chemistry Olympiad for the Dallas/Fort-Worth Section of the American Chemical Society
2005-2007  
NIH Ruth L. Kirschstein National Research Service Award Individual Fellowship
2006-2007  
Co-Chair/Organizer for the Metals in Biology Research Seminar Series, University of Wisconsin, Madison
2004-2005 Chair, Graduate Research Seminar in Bioinorganic Chemistry, Gordon Research Conferences
2003-2004
 Vice-chair, Graduate Research Seminar in Bioinorganic Chemistry, Gordon Research Conferences

Department of Chemistry and Biochemistry

The University of Texas at Arlington · Arlington, Texas 76019-0065 USA

Phone: 817-272-3171 | Fax: 817-272-3808

© 2014 The University of Texas at Arlington

All rights reserved