XAS STRUCTURAL CHARACTERIZATION OF MANGANESE ENZYME, PROLIDASE

我们正在使用X射线吸收光谱(EXAFS和XANES)来 研究一种锰酶--氨基内酯酶中的金属位置。虽然 锰酶是一类具有重要生物学意义的蛋白质。 金属的功能、配位及其原因 锰(II)是酶活性所必需的 到目前为止，几乎没有人关注这一问题。丙氨酸氨基转移酶具有特殊的性质 之所以感兴趣，是因为酶的缺陷被鉴定为特定的 先天性分子疾病的临床症状。计划中的 Pro酶及其抑制剂的X射线吸收光谱测定 在络合物之前，先对模型络合物进行了详细的研究 为了对EXAFS参数以及新软件进行基准测试 可用于结构适配计算。

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.