Our group employs a combination of theory and spectroscopy to study reactive centers in metalloproteins.  We explore the intimate  details of protein chemistry with hopes that our insights will be parlayed into advances in medicine and/or improved catalysts for industrial applications.

 

One particular area of focus is thiolate-ligated heme proteins. These proteins play critical roles in a number of important physiological processes (e.g. the metabolism of xenobiotics, neurotransmission, blood pressure control, and immune defense against tumor cells).  These enzymes are unique in that they catalyze the insertion of an oxygen atom, derived either from molecular oxygen or peroxide, into a variety of organic substrates, often with high degrees of regio- and stereo-selectivity.  The natural function of non-thiolate ligated systems generally involves one-electron rather than two-electron oxidations or oxygen transfer reactions.  The ability of thiolate-heme enzymes to transfer oxygen has challenged and intrigued chemists for decades.  Alkane hydroxylation and olefin epoxidation are extremely important reactions in the industrial world, and catalysts that could efficiently activate and transfer oxygen would be of considerable economic value to large-scale process chemistry.