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My research with undergraduates is focused on hemoproteins, proteins that incorporate an iron containing prophyrin molecule known as heme at the active center of the protein. I am currently concentrating on peroxidase hemoproteins, which are a class of enzymes that oxidize a range of diverse substrates in the presence of hydrogen peroxide. Peroxidases have been implicated in a number of physiological processes; however, their primary role is as an antimicrobial agent. Peroxidases contribute to the nonimmune defense system by oxidizing endogenous halogens or thiocyanate in the presence of hydrogen peroxide to generate active species that will attack foreign pathogens. In addition to their function as defense agents, however, peroxidases have also been implicated in the formation of reactive DNA-binding species in mammary tissue, which can lead to cancer. To understand the mechanism of these proteins on a molecular level is to take a step forward in the understanding of both the physiological defense system of the body and how this system can potentially backfire to produce undersired reactive molecules. While much is known about the general redox reaction that most peroxidases undergo, gaps remain in how electrons are transferred through the participating molecules of the reaction. Knowledge of both the mechanism of electron transfer and the structural features of the peroxidases that encourage this electron transfer will provide vital clues into the function of peroxidases. Moreover, delineation of the electron transfer mechanism and structural features of the peroxidases will provide insight into the development of novel pharmaceutical agents that can interact and modulate peroxidase activity. To this end, the students working in my lab are investigating the structure and function of lactoperoxidase and horseradish peroxidase using organic synthetic methods, enzyme kinetics, substrate binding studies and spectroscopy.