XAS STRUCTURAL CHARACTERIZATION OF MANGANESE ENZYME, PROLIDASE

我们正在使用X射线吸收光谱（EXAFS和XANES）， 研究锰酶中的金属位点，氨酰基脯氨酸二肽酶。 虽然 锰酶是一类具有重要生物活性的蛋白质， 功能，金属的配位和原因， 锰（II）是酶活性所必需的， 迄今为止，很少受到关注。 氨脯氨酸酶具有特殊性 感兴趣，因为酶中的缺陷被鉴定为具有特定的 先天性分子疾病的临床症状。 计划 氨酰基脯氨酸二肽酶及其抑制剂的X射线吸收测量 通过对模型配合物的详细研究， 为了对EXAFS参数和新软件进行基准测试， 用于结构拟合计算。

We are using X-ray absorption spectroscopy (EXAFS and XANES) to study the metal site in a manganese-enzyme, prolidase. Although manganese-enzymes are a class of proteins with important biological functions, the coordination of the metal and the reasons why manganese(II) is required for the activity of the enzymes have hitherto received little attention. Prolidase is of particular interest because defects in the enzyme are identified with specific clinical symptoms of a congenital molecular disease. The planned X-ray absorption measurements on prolidase and prolidase-inhibitor complexes have been preceeded by a detailed study of model complexes in order to benchmark the EXAFS parameters as well as new software to be used in the structure-fitting calculations.