BURGESS PRT TIME (UNIVERSITY OF CALIFORNIA)

伯吉斯 PRT 时间（加利福尼亚大学）

• 批准号: 6658765
• 负责人: BARBARA K BURGESS
• 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/6658765
• 关键词: biological products; biomaterials; biomedical resource; proteins; spectrometry; structural biology

The MoFe protein of nitrogenase is under intense study as the catalytic component of the biological N2 fixation system. We are using x-ray absorption spectroscopic examination of the Mo site of its Mo-Fe-S cluster active site, both in the intact enzyme and in its isolated form (called FeMoco). These experiments have so far been limited to wild-type enzyme. Recently, we have been able to obtain large quantities of altered forms of the MoFe protein from mutant organisms and have also obtained altered forms of FeMoco. EXAFS analysis of these species should define both the portions of FeMoco that are required for biological activity and the transformation that occurs at the Mo site during FeMoco biosynthesis. We are further studying the effects of substrates and inhibitor on the structure of the active site.

固氮酶的 MoFe 蛋白正在被深入研究 生物 N2 固定系统的催化成分。 我们是 使用X射线吸收光谱检查其Mo位点 Mo-Fe-S 簇活性位点，在完整的酶及其中 分离形式（称为 FeMoco）。 这些实验迄今为止 仅限于野生型酶。 近期，我们已经能够获得 来自突变体的大量改变形式的 MoFe 蛋白 有机体，并且还获得了 FeMoco 的改变形式。 EXAFS 对这些物种的分析应该定义 FeMoco 的两个部分 生物活性和转化所需的 FeMoco 生物合成过程中发生在 Mo 位点。 我们更进一步 研究底物和抑制剂对结构的影响 活性位点。