XAS STUDIES OF NITROGENASE, ITS COFACTOR & COFACTOR CLUSTER

最近的晶体学研究突出了这一重大进展， 结构的决定，已经在理解结构， 复合固氮酶中多核金属中心的位置。 Mo-Fe-S簇的存在是已知的，并且其在该簇内的连接是已知的。 蛋白质建立。 重要的问题仍然存在，包括i） FeMoco结构外部与内部的关系， 蛋白质; ii）理解高柠檬酸盐和pH依赖性的作用 对固氮酶的影响; iii）确定底物和 抑制剂结合;和iv）建立高度精确的测量细节 蛋白质内外的FeMoco x射线吸收 使用SR的光谱（边缘和EXAFS）非常适合于 提供深入了解电子和韵律结构的选择 原子站

Significant progress, highlighted by recent crystallographic structual determinations, has been made in understanding the structure of the polynuclear metal centers in the complex nitrogenase enzyme. The presence of a Mo-Fe-S cluster is known and its ligation within the protein established. Important questions remain that include i) relationship of the FeMoco structure outside of, to that within, the protein; ii) understanding the role of homocitrate and of pH-dependent effects on nitrogenase; iii) determining where and how substrate and inhibitors bind; and iv) establishing highly accurate metrical details for the FeMoco both within and outside the protein. X-ray absorption spectroscopy (both edge and EXAFS) using SR is well-suited to providing insights into electronic and metrical structure of selected atomic sites.