FE XAS L2,3 EDGE STUDIES OF NON HEME IRON ENZYMES

非血红素铁酶的 FE XAS L2,3 边缘研究

• 批准号: 6586703
• 负责人: KEITH O HODGSON
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586703
• 关键词: biological products; biomaterials; biomedical resource; proteins; spectrometry; structural biology; technology /technique

We propose to study the geometric and electronic structure of non-heme mononuclear and dinuclear iron enzymes using Fe L-edge X-ray absorption spectroscopy. Current studies at the Fe K-edge are limited by certain characteristics of the experiment. The 1s.3d transition is electric dipole forbidden and the energy resolution at the Fe K-edge is of the same order of magnitude as splittings of the d-orbitals by a ligand field. In contrast, at the metal L2,3-edges 2p.3d transitions are electric dipole allowed, providing a direct probe of the energy levels and populations of the d-orbitals. A systematic study of Fe L-edge spectra of model compounds with varying ligation, geometries and oxidation states will be used to develop a basis of understanding which will be applied to the active sites in mononuclear and dinuclear non-heme iron enzymes.

我们建议研究的几何和电子结构的 使用Fe L边X射线的非血红素单核和双核铁酶 吸收光谱学 目前在铁K边的研究是有限的 实验的某些特征。 1s.3d转换是 电偶极禁戒和Fe K边的能量分辨 与d轨道分裂的数量级相同， 配体场 相反，在金属L2处，3边2p.3d跃迁 是电偶极允许的，提供能量的直接探测 d轨道的能级和布居。 铁的系统研究 具有不同连接构型的模型化合物的L边光谱 和氧化态将被用来建立理解的基础 这将适用于单核和双核中的活性位点， 非血红素铁酶