Department of Chemistry and Biochemistry
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- Daniel W. Armstrong
- William A. Baker
- Edward Bellion
- Alejandro Bugarin
- Saiful Chowdhury
- Purnendu (Sandy) K. Dasgupta
- Rasika Dias
- Ronald L. Elsenbaumer
- Frank W. Foss
- Robert F. Francis
- Jongyun Heo
- Junha Jeon
- Kayunta Johnson-Winters
- Peter Kroll
- Carl J. Lovely
- Frederick MacDonnell
- Subhrangsu S. Mandal
- Dennis S. Marynick
- Brad S. Pierce
- Martin Pomerantz
- Laszlo Prokai
- Krishnan Rajeshwar
- Jimmy R. Rogers
- Zoltan A. Schelly
- Kevin A. Schug
- E. Thomas Strom
- Norma Tacconi
- Seiichiro Tanizaki
- Richard B. Timmons
- Jennifer Rhinehart
- Research Interests Grid
- Analytical Chemistry
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- ABOUT US
Brad S. Pierce
Office: 300F SH, Email: email@example.com, Phone: 817-272-9066, FAX: 817-272-3808
Fundamental life processes (respiration, photosynthesis, and replication) frequently involve transition metal ions or elements outside the traditional purview of biochemistry. As a result, ground breaking work relevant to chemical biology lies at the interface of (or crosses) traditional divisional boundaries in chemistry. The scope of research conducted by the Pierce group embraces this interdisciplinary approach; we employ modern biophysical and bioinorganic techniques to investigate mechanisms of metalloenzyme function and regulation. This range of effort is fairly ambitious in that it spans work at the genetic level (PCR cloning, vector design/expression, and site directed mutagenesis) all the way up to spectroscopic characterization (UV-visible, CD, EPR, and Mössbauer) of purified enzymes.
Specific topics of interest to our group focus on understanding mechanisms of biochemical thiol-oxidation and the interplay between dysfunction in sulfur metabolism and human neurodegenerative disease states (Alzheimer’s, autism, and Parkinson’s). Enzymes involved in sulfur-oxidation and transfer are increasingly being recognized as potential drug targets for development of antimicrobials, therapies for cancer, and inflammatory disease.
An additional area of focus involves the study of metalloenzymes involved in the post-transcriptional modifications of transfer RNA (tRNA). In many instances, the physiologic role of such modifications is unclear; however, several examples have been identified to suggest that the presence of modified nucleosides in tRNA can impact aminoacyl-tRNA selection, decrease translational frame-shifting, regulate central metabolism, as well as initiate genes involved in bacterial virulence.
Bishnu P. Subedi, Andra L. Corder, Siai Zhang, Frank W. Foss, Jr., and Brad S. Pierce; “Steady-state kinetics and spectroscopic characterization of enzyme-tRNA interactions for the non-heme diiron tRNA-monooxygenase, MiaE” Biochemistry 2014 [Epub ahead of print] PMID:25453905 .
Wei Li and Brad S. Pierce; “Steady-state substrate specificity and O2-coupling efficiency of mouse cysteine dioxygenase” Arch Biochem Biophys. 2014 [Epub ahead of print] PMID:25444857.
Joshua K. Crowell, Wei Li, and Brad S. Pierce; “Oxidative uncoupling in cysteine dioxygenase is gated by a proton-sensitive intermediate” Biochemistry 2014 [Epub ahead of print] PMID: 25387045.
Tiffany A. Pinder, Steven K. Montalvo, Chung-Hung Hsieh, Allen M. Lunsford, Ryan D. Bethel, Brad S. Pierce, and Marcetta Y. Darensbourg ”Metallodithiolates as Ligands to Dinitrosyl Iron Complexes: Towards the Understanding of Structures, Equilbria, and Spin Coupling” Inorg Chem. 2014 53(17):9095-105. PMID:25144614.
Thai Kabbua, Preeyanan Anwised, Atcha Boonmee, Brad S. Pierce, Bishnu P. Subedi, Apisak Dhiravisit, Sompong Thammasirirak “Autoinduction, purification, and characterization of functional soluble α-globin chains of crocodile (Crocodylus siamensis) hemoglobin in Escherichia coli” Protein Expr Purif 2014 103:56-63. PMID: 25175288.
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 52 (51): 9104-9119. PMID:24279989.
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. PMID:21992268.
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. PMID:21541436.
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. PMID:20397631.
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. PMID:20159007.
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. PMID:17964805.
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. PMID:17602574.
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. PMID:17786587.
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. PMID:15755183
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. PMID:12862469. (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. PMID:11827513. (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|
||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|
||NIH Ruth L. Kirschstein National Research Service Award Individual Fellowship|
||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|
||Vice-chair, Graduate Research Seminar in Bioinorganic Chemistry, Gordon Research Conferences|