The Inorganic and Bioinorganic Division has two faculty with projects focused on the role metals, typically found in cofactors, play in catalysis vital to life. We are broadly interested in the interplay between metal, cofactor, and peptide environment to facilitate difficult reactions while minimizing toxic side reactions or dead-end intermediates. Research projects are highly interdisciplinary with impacts on protein and cellular function, and environmental roles of the metallocofactors. Typical techniques student researchers learn include: protein design, Protein expression and purification, UV-vis spectroscopy, kinetics (steady state and pre-steady state), use of an anoxic glove box, nuclear magnetic resonance (NMR) spectroscopy, electron paramagnetic resonance (EPR) spectroscopy, electrochemistry, and inorganic synthesis. Projects currently focus on heme-, molybdenum-, and/or iron-sulfur containing enzymes with the research projects focused on the roles of these cofactors. More details about research projects led by each individual faculty can be found below as well as their specific research group website.
Faculty Research
Research interests primarily focus on heme containing enzymes with two active projects: 1) the investigations into the mechanism of nitrite conversion to ammonia in a heme containing enzyme with focus on characterization of reaction intermediates by various kinetic and spectroscopic methods, and 2) Investigations of a Mycobacterium tuberculosis protein known as truncated Hemoglobin N (trHbN). The protein neutralizes nitric oxide produced by the immune system to kill bacteria, thus helping M. tuberculosis to evade the body’s defenses.
Research interests include molybdenum containing enzymes, the radical S-adenosyl Methionine (SAM) superfamily, heme reactivity, and technique development/application in EPR spectroscopy. Generally, all of our projects focus on the interplay between cofactor and peptide investigating the role of the primary and secondary coordination environment in tuning the functionality of metalloenzymes. In one project we are developing an artificial metalloenzyme to better understand the role of the peptide averment in a highly controllable/tunable (peptide and cofactor) environment.