Our laboratory works to elucidate the geometric and electronic properties of metal centers in proteins and cofactors through a combined spectroscopic and computational approch. Current areas of research include studies of coenzyme-B₁₂ dependent enzymes and associated adenosyltransferases, Mn- & Fe-dependent as well as Ni-dependent superoxide dismutases (SODs), and the non-heme iron-dependent enzyme, cysteine dioxygenase (CDO).

The experimental techniques used in this research include electronic absorption (Abs), circular dichroism (CD), magnetic circular dichroism (MCD), resonance Raman (rR), and electron paramagnetic resonance (EPR) spectroscopies. These tools are complemented by the use of density functional theory (DFT) and combined quantum mechanics/molecular mechanics (QM/MM) electronic structure calculations to develop experimentally validated bonding descriptions.

With this combined spectroscopic/computational methodology we can selectively probe the geometric and electronic properties of the catalytically active metal centers in both proteins and model complexes. We are also able to explore the nature of transient catalytic intermediates that are inaccessible to structural studies using X-ray crystallography.