Nitrogenase assembly mechanism

固氮酶组装机制

• 批准号: 8774547
• 负责人: Markus W Ribbe
• 金额: $ 30.88万
• 依托单位: UNIVERSITY OF CALIFORNIA-IRVINE
• 依托单位国家: 美国
• 财政年份: 2003
• 资助国家: 美国
• 起止时间: 2003-05-01 至 2015-11-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8774547
• 关键词: Binding; Binding Sites; Biochemical; Biomimetics; Carbon; Cluster Analysis; Complex; Core Assembly; Enzymes; Event; Genetic; Glutamine; Health; Homologous Gene; Human; Iron; Knowledge; Label; Location; Maps; Metals; Molybdenum; Nitrogen; Nitrogenase; Pathway interactions; Population; Reaction; Research; Scheme; Site; Source; Structure; Testing; Variant; biological systems; catalyst; chemical synthesis; comparative; homocitrate; insight; interstitial; metal complex; protein protein interaction; public health relevance; tetrathiomolybdate

DESCRIPTION (provided by applicant): Nitrogenase reaction represents a major source of the usable form of nitrogen that supports the existence of human population. As such, understanding how small building blocks are assembled into a functional nitrogenase entity is of significant relevance to human health. Using combined genetic, biochemical, spectroscopic and structural approaches, we propose to investigate how M-cluster, the active center of molybdenum nitrogenase, is assembled. Specifically, we will examine the formation of a Fe-S core of M-cluster, the maturation of Fe-S core into an M-cluster, and the transfer of M-cluster from the assembly site to its target location in great detail. Through our proposed studies, we expect to refine the biosynthetic pathway of M-cluster, which will provide crucial insights into th structural-functional relationship of nitrogenase and the general assembly mechanism of complex metal clusters in biological systems.

描述（由申请人提供）：固氮酶反应代表了支持人类生存的可用形式氮的主要来源。因此，了解小构件如何组装成功能性固氮酶实体对人类健康具有重要意义。本文采用遗传学、生物化学、光谱学和结构学相结合的方法，研究钼固氮酶活性中心M簇的组装。具体来说，我们将详细研究M-团簇的Fe-S核心的形成，Fe-S核心成熟为M-团簇，以及M-团簇从组装位点转移到其目标位置。通过我们的研究，我们希望能够进一步完善M-团簇的生物合成途径，这将为固氮酶的结构-功能关系以及复杂金属团簇在生物体系中的组装机制提供重要的见解。