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

本研究旨在了解含Mo的DMSOR（二甲基亚砜还原酶）酶的结构、光谱性质和氧化还原行为。该方法将基于x射线晶体结构合成含有Mo的模型化合物，其内部配位球与球形红杆菌和荚膜红杆菌天然酶的配位球相似。新的OMo（S2C2RR”）2型化合物将通过循环伏安法、NMR、FT-IR、UV-VIS、MS、ESEEM、EPR、PES、XPS和CCD x射线衍射等多种技术进行表征。有了这个POWRE奖，化学部门正在支持宾夕法尼亚州布林莫尔学院化学系的Sharon N. Burgmayer的工作。这项研究是为了了解以钼为中心金属的二甲基sulo氧化物还原酶的行为和光谱性质。人类钼酶的遗传功能障碍是致命的联合氧化酶缺乏症的原因。这项工作有望提供光谱和结构基准，以帮助解释酶的类似数据，并提供对其活性位点化学的见解。它还有望在化学和生物化学的交叉领域为本科生提供优秀的培训，并激励女学生从事研究工作。

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.