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

本研究旨在了解含钼DMSOR（二甲基亚砜还原酶）的结构、光谱性质和氧化还原行为。 该方法将是合成模型化合物，其中含有钼与内部配位球类似的天然酶从红细菌sphaeroides和R。capsulatus，基于X射线晶体结构。 新化合物的类型为OMo（S2 C2 RR”）2，将通过多种技术进行表征，包括循环伏安法、NMR、FT-IR、UV-VIS、MS、ESEEM、EPR、PES、XPS和CCD X射线衍射。Burgmayer在宾夕法尼亚州布林莫尔的布林莫尔学院化学系工作。 这项研究是为了了解含有钼作为中心金属的二甲基亚砜还原酶的行为和光谱特性。 人类钼酶的遗传故障是致命的复合氧化酶缺乏症的原因。 这项工作预计将提供光谱和结构基准，以帮助解释酶的类似数据，并提供深入了解其活性位点化学。 它还有望在化学和生物化学之间的界面上为本科生提供出色的培训，并激励女学生继续从事研究工作。

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.