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: 6586758
• 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: 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/6586758
• 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.

最近的晶体学突显了重大进展 结构决定，已在理解结构中做出 复合固氮酶中的多核金属中心。 Mo-Fe-S 簇的存在是已知的，并且它在 蛋白质成立。 仍然存在重要问题，包括 i) FeMoco 结构外部与内部的关系 蛋白质; ii) 了解高柠檬酸盐和 pH 依赖性的作用 对固氮酶的影响； iii) 确定底物的位置和方式 抑制剂结合； iv) 建立高度准确的度量细节 对于蛋白质内部和外部的 FeMoco。 X射线吸收 使用 SR 的光谱（边缘和 EXAFS）非常适合 提供对选定的电子和计量结构的见解 原子站点。