Research in the Hargrove laboratory involves the structure, function, folding, and expression of heme proteins. Heme proteins exhibit marked differences in reactivity toward diatomic ligands such as O2, CO, and NO, all of which are important biological molecules. However, unlike most enzymatic reactions which rely on the exact shape and charge distribution of the substrate molecule to determine specificity, selective recognition of small diatomic ligands by heme proteins occurs after the heme-ligand complex is formed.
Myoglobin and hemoglobin have long been ideal systems for developing an understanding of the relationship between the structure and function of proteins. More recently, these proteins have found renewed interest due to the application of modern methods of time-resolved crystallography, site-directed mutagenesis, and molecular dynamics to explore molecular recognition and ligand binding with high resolution. Furthermore, heme proteins which are less understood physiologically and biophysically have been discovered which appear to have a wide variety of novel signaling and oxygen storage functions. My laboratory uses site-directed mutagenesis, kinetic and spectroscopic methods, and X-ray crystallography to study the high resolution structure and function of heme proteins.