XAS STUDIES OF NITROGENASE, ITS COFACTOR & COFACTOR CLUSTER

固氮酶及其辅助因子的 XAS 研究

• 批准号: 6658671
• 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/6658671
• 关键词: biological products; biomaterials; biomedical resource; plants; proteins; spectrometry; structural biology; technology /technique

Significant progress, highlighted by recent crystallographic structual determinations, has been made in understanding the structure of the polynuclear metal centers in the complex nitrogenase enzyme. The presence of a Mo-Fe-S cluster is known and its ligation within the protein established. Important questions remain that include i) relationship of the FeMoco structure outside of, to that within, the protein; ii) understanding the role of homocitrate and of pH-dependent effects on nitrogenase; iii) determining where and how substrate and inhibitors bind; and iv) establishing highly accurate metrical details for the FeMoco both within and outside the protein. X-ray absorption spectroscopy (both edge and EXAFS) using SR is well-suited to providing insights into electronic and metrical structure of selected atomic sites.

最近的晶体学强调了重大进展 结构确定是在理解结构时做出的 复合氮酶中的多核金属中心的。 已知Mo-Fe-S集群的存在，并在 蛋白质建立。 仍然存在包括我的重要问题 Femoco结构与内部的关系 蛋白质; ii）了解同晶和pH依赖性的作用 对氮酶的影响； iii）确定底物的何处以及如何 抑制剂结合； iv）建立高度准确的度量细节 对于蛋白质内外的Femoco。 X射线吸收 使用SR的光谱法（边缘和EXAFS）非常适合 提供对选定的电子和度量结构的见解 原子地点。