We have produced a number of interesting site-specific mutants of the active site iron coordination which modify the enzyme's spectroscopic and enzymatic properties. Current research interests are in kinetic spectroscopy of transient molecular species, biophysics, and studies of visual transduction. Many of our studies involve the use of nanosecond laser photolysis techniques that are capable of observing absorption spectra of transients, or kinetics of photo-induced reactions with lifetimes of nanoseconds or longer. These techniques are being used to study the mechanisms of the functions of a number of proteins as well as to study early events involved in protein folding. The synthesis of complex natural and unnatural organic molecules continues to stimulate the creativity of organic chemistry students.
Several projects are currently underway, each leading toward a biologically active natural product.
Student researchers will become familiar with modern spectroscopic as well as laboratory techniques. We are interested in understanding the structure of simple peptides which in turn are designed to mimic domains of folded proteins. We use automated peptide synthesis to design particular domains and we probe the detailed structure with electron spin resonance, nuclear magnetic resonance, circular dichroism and Fourier transform infrared spectroscopy. Crystal structures of proteins with bound drugs provide valuable experimental data for drug design. We are developing computer algorithms to study such structures with the aim of being able to predict the binding of a small molecule with protein.