XRAY ABSORPTION SPECT OF MANGANESE IN PHOTOSYNTHETIC OXYGEN EVOLVING COMPLEX

光合放氧复合物中锰的X射线吸收光谱

• 批准号: 6437676
• 负责人: MELVIN P KLEIN
• 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/6437676
• 关键词: biomaterials; biomedical resource; plants; proteins; spectrometry; structural biology

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.

重大进展，由最近的结晶学突显 在理解结构时，已经做出了结构上的决定 复合固氮酶中的多核金属中心。 已知存在一个Mo-Fe-S团簇，它在 蛋白质已建立。重要问题仍然存在，包括i) FeMoco结构外部与内部的关系 蛋白质；ii)了解高柠檬酸和pH依赖的作用 对固氮酶的影响；iii)确定底物的位置和方式 抑制剂结合；以及iv)建立高精度的测量细节 对于蛋白质内部和外部的FeMoco。X射线吸收 使用SR的光谱学(EDGE和EXAFS)非常适合于 提供对选定的电子和节拍结构的见解 原子弹的位置。