XAS STUDIES OF OXY-HEMOGLOBIN

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。 铁K边X射线吸收数据将被测量的血红蛋白（Hb），这是普遍存在的双氧转移蛋白在哺乳动物的单晶。将测量脱氧血红蛋白、蛋氨酸血红蛋白和氧合血红蛋白的单晶XAS数据，脱氧血红蛋白、蛋氨酸血红蛋白和氧合血红蛋白分别是血红蛋白的还原态、完全氧化态和氧合态。将进行XAS前边缘分析，以与理论上产生的XAS光谱（使用密度泛函理论）相关联，以确定氧合血红蛋白的基态电子结构，并了解双氧与血红素蛋白结合的机制。 将数据与溶液Fe K边XAS数据进行比较，以比较溶液和Hb结晶形式之间的电子结构变化。

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. Fe K-edge x-ray absorption data will be measured on single crystals of hemoglobin (Hb), which is the ubiquitous di-oxygen transfer protein in mammals. Single crystal XAS data will be measured for deoxy-, met- and oxyHb, which are the reduced, fully oxidized and oxygenated states of Hb, respectively. XAS pre-edge analysis will be carried out to correlate with theoretically generated XAS spectra (using density functional theory) to determine the ground state electronic structure of oxyhemoglobin and understand the mechanism of di-oxygen binding to heme proteins. The data will be compared to solution Fe K-edge XAS data in order to compare the electronic structure changes between solution and crystalline forms of Hb.