XAS STUDIES OF OXY-HEMOGLOBIN

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。 铁K边X射线吸收数据将测量单晶的血红蛋白(Hb)，它是哺乳动物中普遍存在的双氧转移蛋白。单晶XAS数据将测量脱氧、MET和OXHb，它们分别是Hb的还原、完全氧化和氧化状态。将进行XAS前缘分析，以与理论产生的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的结合机理。这些数据将与溶液Fe K边XAS数据进行比较，以便比较Hb的溶液和晶型之间的电子结构变化。这些数据将与处于S=0、S=1和S=2态的血红素模型络合物的数据进行比较，以考察自旋态的变化对Fe K边移动的影响。

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. The data will be compared to those obtained from heme model complexes that are in the S=0, S=1 and S=2 states to investigate effects of spin state changes on the Fe K-edge shifts.