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: 6119606
• 负责人: KEITH O HODGSON
• 金额: --
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-03-01 至 2000-04-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6119606
• 关键词: biomaterials; proteins; 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.

一系列M(SR)4N-络合物的分析 氯与S K边X射线吸收光谱的关系及可比硫的发展 基于研究电子结构和成键的方法。这个 S K边的方法论将被应用于一系列 模型络合物和蛋白质中的多核Fe-S中心也 含M-Fe-S部分的异金属体系 固氮酶。这些研究将被用来理解共价性和 蓝铜、铁等生物无机体系的电子结构 硫磺和含异金属簇的蛋白质。