HEME PROTEINS, LIPID OXIDATION, AND HUMAN HEALTH
The PI, Dr. Mark Richards is a Professor at the University of Wisconsin-Madison who specializes in oxidative processes mostly in relation to lipids and functional aspects of hemoglobin and myoglobin. Dr. Richards received his BS in Food Science from Ohio State University in 1992, his MS,PhD, and Postdoc at U-Mass Amherst from 1997-2001. One focal point has been to elucidate the mechanisms by which there is a wide range of variation in auto-oxidation and heme dissociation when comparing mammalian, avian, and fish hemoglobins. This has led to the identification of the key amino acid sites of hemoglobins that control these functional properties. His use of site-directed mutagenesis to alter protein functionality has been a complementary piece to this endeavor. For example, site CD3, E10, E11 and E14 vary among the different hemoglobins so that providing the mammalian residue at these sites is stabilizing whereas the fish residue is destabilizing. Protein crystallography is an additional tool that has been used to characterize the functional properties of different hemoglobins. By understanding the stereo-chemical aspects of protein functionality obtained from crystal structures, this allows the design of strategies to enhance or disrupt protein-protein interactions. Dr. Richards has also focused on mechanisms of vitamin E (alpha and gamma-tocopherol) metabolism in vivo which has implicated particular cytochrome P450s hydroxylases that are more active in certain animal species than others. Dr. Richards actively collaborates with researchers in food science, chemistry, and electrical engineering departments.