POWRE: Studies of Model Compounds for the Active Site of DMSO Reductase

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This research is aimed at understanding the structures, spectroscopic properties, and redox behavior of Mo containing DMSOR (dimethylsulfoxide reductase) enzymes. The approach will be to synthesize model compounds which contain Mo with an inner coordination sphere similar to that postulated for the natural enzymes from Rhodobacter sphaeroides and R. capsulatus, based on x-ray crystal structures. The new compounds, of the type OMo(S2C2RR")2, will be characterized by a variety of techniques including cyclic voltammetry, NMR, FT-IR, UV-VIS, MS, ESEEM, EPR, PES, XPS, and CCD x-ray diffraction.With this POWRE award, the Chemistry Division is supporting the work of Sharon N. Burgmayer in the Department of Chemistry at Bryn Mawr College in Bryn Mawr, PA. The research is being done to understand behavior and spectroscopic properties of dimethylsuloxide reductase enzymes which contain molybdenum as the central metal. Genetic malfunctions of molybdenum enzymes in humans are the cause of the fatal combined oxidase deficiency disease. The work is expected to provide spectroscopic and structural benchmarks to aid in the interpretation of analogous data on the enzymes, and to provide insights into their active site chemistry. It is also expected to provide excellent training for undergraduates at the interface between chemistry and biochemistry, and to motivate female students to go on to careers in research.