A major aspect of our research focuses on the structure, function, and catalytic mechanisms of bacterial and archaeal non-heme iron enzymes that reductively scavenge diatomic oxygen and nitrogen species. These scavenging and sensing reactions require specialized active sites with novel iron coordination environments and novel mechanisms, which we follow by rapid kinetic and spectroscopic techniques as well as protein X-ray crystallography. We are also attempting to develop an oxygen-carrying protein as a blood substitute.
A related project focuses on proteins that catalyze storage and release of intracellular iron. An exciting new development is the use of these iron storage proteins as scaffolds to enclose metal and semiconductor nanoparticles for photochemical H2 production and photo-initiated delivery of toxic iron to cancer cells.