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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.