BURGESS PRT TIME (UNIVERSITY OF CALIFORNIA)

伯吉斯 PRT 时间（加利福尼亚大学）

• 批准号: 6119639
• 负责人: BARBARA K BURGESS
• 金额: --
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-03-01 至 2000-04-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6119639
• 关键词: biomaterials; proteins; 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.