Jackson Research Group
Group members (left to right)
Front: Aruna Munasinghe, Jaycee Mayfield, Allyssa Massie,
Eleanor Stewart-Jones, Shannon Jones, and Elizabeth Grotemeyer
Back: Andrew Burr, Derek Rice Anna Donovan, Melissa Denler,
Joshua Parham, Yuri Lee, Timothy Jackson
Nature uses metalloenzymes containing Mn, Fe, or Cu and oxidants such as molecular oxygen and hydrogen peroxide to carry out remarkable oxidative transformations that are both vital for life and fascinating from a fundamental perspective. Our research focuses on unraveling the reactivity of manganese-dependent enzymes that catalyze oxidative degradation reactions using molecular oxygen or hydrogen peroxide as oxidants. Our laboratory uses a combination of i) reactivity studies of metal ion complexes and enzymes, ii) detailed spectroscopic characterization of transition metal species, particularly unstable intermediates that cannot be characterized using X-ray crystallographic methods, and iii) computational chemistry.
Spectroscopic methods used in our research include electronic absorption (UV-vis), electron paramagnetic resonance (EPR), magnetic circular dichroism (MCD) spectroscopies, and X-ray absorption spectroscopy (XAS). These tools are particularly powerful when used in conjunction with computational methods, as they permit the characterization of the geometric and electronic structures of fleeting intermediates too unstable to be characterized using standard crystallographic methods. By applying this three-pronged approach to both metalloenzymes and transition metal complexes, we will gain detailed insight into how nature uses molecular oxygen and manganese to oxidize substrates and develop transition metal complexes that can perform "green" oxidation reactions.