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的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 提出了异双核无机模型配合物和金属蛋白活性位点的多边缘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K-和L-边缘处用于EXAFS和XANES分析，其是金属蛋白活性位点的仿生类似物。XAS结果将与小分子晶体学数据和电子结构计算相关联。这些无机模型复合物将提供背景的分析和解释的FeIIIMnII含有紫色酸性磷酸酶样品在不同的pH值。在两个金属中心之间的桥联O配体作为催化剂中的亲核试剂，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与代谢功能障碍（如骨吸收）相关的药物开发提供新思路。

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.