XAS LIGAND K EDGE STUDIES OF OPEN SHELL METAL IONS IN PROTEINS & MODELS

蛋白质中开壳金属离子的 XAS 配体 K 边缘研究

• 批准号: 6437594
• 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: 2001
• 资助国家: 美国
• 起止时间: 2001-03-01 至 2002-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6437594
• 关键词: biomaterials; biomedical resource; proteins; spectrometry; structural biology; technology /technique

Analysis of a series of M(SR)4n- complexes to understand the relationship of Cl to S K-edge XAS and develop a comparable sulfur based approach to study electronic structure and bonding. The methodology of the S K-edges will then be applied to a series of multi-nuclear Fe-S centers in model complexes and proteins also to heterometal systems containing M-Fe-S moieties similar to those of nitrogenase. These studies will be used to understand covalency and electronic structure of bioinorganic systems such as blue copper, iron sulfur, and heterometal cluster-containing proteins.

分析一系列M（SR）4 n-配合物以理解 Cl与S K-边XAS的关系，并开发出可比较的硫 的方法来研究电子结构和键合。 的 然后将S K边缘的方法应用于一系列 模型复合物和蛋白质中的多核Fe-S中心， 含M-Fe-S结构部分的杂金属系统类似于 固氮酶 这些研究将用于了解共价性， 电子结构的生物无机系统，如蓝铜，铁 硫和含杂金属簇的蛋白质。