XAS STUDIES OF THE BINUCLEAR METALLOENZYME PURPLE ACID PHOSPHATES AND THEIR BIOM

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 提出了异双核无机模型化合物和金属蛋白活性中心的多边XAS表征，以确定紫色酸性磷酸酶的关键几何和电子结构特征。将收集一系列FeIIIMII络合物的数据，其中M=Mn，Ni，Cu，Zn，在每个金属的K-和L边，用于EXAFS和XANES分析，这是金属蛋白活性中心的仿生类似物。XAS结果将与小分子结晶学数据和电子结构计算相关联。这些无机模型络合物将为不同pH值下含有紫色酸性磷酸酶的FeIIIMnII样品的分析和解释提供背景。这两个金属中心之间的桥联O-配体作为催化中的亲核剂，有望在催化中发挥重要作用。对紫色酸性磷酸酶化学功能的分子理解有望为新陈代谢功能障碍的药物开发提供新的思路，如骨吸收。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Multi-edge XAS characterization of hetero-binuclear inorganic model complexes and metalloprotein active sites are proposed to define the key geometric and electronic structural features of purple acid phosphatases. Data will be collected for a series of FeIIIMII complexes, where M=Mn, Ni, Cu, Zn, at each metal K- and L-edges for EXAFS and XANES analysis that are biomimetic analogues of the metalloprotein active site. The XAS results will be correlated with small molecule crystallographic data and electronic structure calculations. These inorganic model complexes will provide the background for the analysis and interpretation of FeIIIMnII containing purple acid phosphatase samples at various pH values. The bridging O-ligand between the two metal center is expected to play an important role in catalysis as the nucleophile in catalysis. The molecule understanding of chemical function of purple acid phosphatase is expected to generate new ideas for drug development related to metabolic disfunctions, such as bone resorption.