Brad S. Pierce

Brad S. Pierce

Associate Professor


  • B.S., Chemistry, California State University, Chico, 1996
  • Ph.D., Carnegie Mellon University, 2003
  • Post-Doctoral Associate, University of Wisconsin, Madison, 2004-2008


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 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 include non-heme iron oxygenase enzymes involved in thiol oxidation, post-transcriptional modifications of transfer RNA (tRNA), and arylamine N-oxygenase chemistry.

Selected Publications

11.   Parham Asgari, Yuanda Hua, Apparao Bokka, Chanachon Thiamsiri, Watcharapon Prasitwatcharakorn, Ashif Karedath, Xin Chen, Sinjinee Sardar, Kyung Suk Yum, Gyu Leem, Brad S. Pierce, Kwangho Nam, Jiali Gao, and Junha Jeon*; “Catalytic Hydrogen Atom Transfer from Hydrosilanes to Vinylarenes by Alkali Metal Lewis Base Catalyst for Hydrosilylation and PolymerizationNature-Catalysis. 2019 2, 164-173
10.   Manuel Quiroz, Shengda Ding, Pokhraj Ghosh, Nattamai Bhuvanesh, Chung-Hung Hsieh, Philip M. Palacios,  Brad S. Pierce, Marcetta Y. Darensbourg*, and Michael B. Hall* “Structural and Electronic Responses to the Three Redox Levels of Fe(NO)N2S2-Fe(NO)2Chem Eur J. 2018, 26:24(60), 16003-08
9.     William P. Morrow, Sinjinee Sardar, Pawan Thapa, Mohammad S. Hossain, Frank W. Foss Jr. and Brad S. Pierce* “Thiol dioxygenase turnover yields benzothiazole products from 2-mercaptoaniline and O2-dependent oxidation of primary alcoholsArch Biochem Biophys. 2017 631, 66-74.
8.     Joshua K. Crowell; Sinjinee Sardar; Mohammad S. Hossain; Frank W. Foss Jr.; Brad S. Pierce* “Non-chemical proton-dependent steps prior to O2-activaiton limit Azotobacter vinelandii 3-mercaptopropionic acid dioxygenase (MDO) catalysisArch Biochem Biophys. 2016 604, 86-94.
7.     Brad S. Pierce*; Bishnu P. Subedi; Sinjinee Sardar; Joshua K. Crowell; “The ‘Gln-type’ thiol dioxygenase from Azotobacter vinelandii is a 3-mercaptopropionic acid dioxygenaseBiochemistry 201554(51):7477-90.
6.     Bishnu P. Subedi; Andra L. Corder; Siai Zhang; Frank W. Foss, Jr.; Brad S. Pierce* “Steady-state kinetics and spectroscopic characterization of enzyme-tRNA interactions for the non-heme diiron tRNA-monooxygenase, MiaEBiochemistry 2015 54(2): 363-76.
5.    Wei Li and Brad S. Pierce* “Steady-state substrate specificity and O2-coupling efficiency of mouse cysteine dioxygenaseArch Biochem Biophys. 2015 565: 49-56.
4.    Joshua K. Crowell; Wei Li; Brad S. Pierce* “Oxidative uncoupling in cysteine dioxygenase is gated by a proton-sensitive intermediateBiochemistry 2014 53(48): 7541-8.
3.    Wei Li; Elizabeth J. Blaesi; Michael D. Pecore; Joshua K. Crowell; 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.
2.    Andra L. Corder; Bishnu P. Subedi; Siai Zhang; Amanda M. Dark; Frank W. Foss, Jr.; Brad S. Pierce* “Peroxide-shunt substrate-specificity for the Salmonella typhimurium O2-dependent tRNA modifying monooxygenase (MiaE)”; Biochemistry 2013 52(36):6182-6196.
1.    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 intermediateBiochemistry, 2011, 50 (47), pp 10241–10253.