This research will focus on the spectroscopic characterization of polycyclic aromatic hydrocarbons (PAH) and their interactions with proteins. Peroxidases have been recently studied as plausible candidates for the biodegradation of polycyclic aromatic compounds and other highly dangerous dioxin pollutants. This study will include a complete determination of the optical properties of the heme prosthetic group upon adduct formation, and an assessment of the kinetic and thermodynamic manifestation in relation to the proposed oxidizing mechanism of PAH pollutants by peroxidases. Haloperoxidases, lactoperoxidases and myeloperoxidases will be prepared and characterized and their interaction with aromatic compounds such as 2,4,6-trochlorophenol will be studied to clarify the general mechanisms of action of peroxidases with PAH compounds. The interaction of PAH compounds with DNA and the role of cytochrome P450 enzymes in the biodegradation of hazardous materials will also be studied.
