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.

氮酶的MOFE蛋白正在接受激烈的研究 生物N2固定系统的催化成分。 我们是 使用其Mo位点的X射线吸收光谱检查 Mo-Fe-S簇活性位点，无论是完整的酶还是在其中 孤立形式（称为Femoco）。 到目前为止，这些实验已经 仅限于野生型酶。 最近，我们能够获得 突变体的大量改变形式的MOFE蛋白 生物体，还获得了改变形式的femoco。 exafs 对这些物种的分析应定义Femoco的两个部分 生物活性和转变所必需的 发生在Femoco生物合成期间的MO部位。 我们进一步 研究底物和抑制剂对 活跃的站点。