This two-year standard grant, supported by the Chemistry and Molecular and Cellular Biosciences Divisions, facilitates investigations into the structure of enzymes that have been modified with polyethylene glycol. Spectroscopic studies, including circular dichroism, uv-visible, and electron spin resonance will be used to characterize the structure of the modified enzymes as they exist in organic solvents. Horseradish peroxidase, and the related enzyme, cytochrome P 450, will be the focus of these investigations. These studies should permit the characterization of enzyme intermediates that are not easily studied in aqueous environments, due to their extremely short lifetimes, and will allow enzymes to be used for targeted synthesis in organic solvents. Professor Mabrouk and her students will characterize the structure of enzymes that have been modified with polymers, which allow for stabilization of these species in organic solvents. One of the enzymes to be characterized in this study, cytochrome P 450, is an important partner in the biochemical pathway for conversion of oxygen to carbon dioxide. The implications of this research include the ability to characterize normally inaccessible intermediate structures, and the development of viable commercial catalysis methods based on enzyme chemistry.
