Nitrogenase Assembly Mechanism

固氮酶组装机制

• 批准号: 8197578
• 负责人: Markus W Ribbe
• 金额: $ 28.94万
• 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 2012-11-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8197578
• 关键词: Address; Ammonia; Azotobacter vinelandii; Binding Sites; Bioavailable; Biochemical; Biogenesis; Biological; Biological Models; Chemicals; Complex; Development; Funding; Future; Genetic; Goals; Health; Human; In Situ; Investigation; Metalloproteins; Metals; Molecular; Molybdenum; Molybdoferredoxin; Nitrogen; Nitrogenase; Nucleic Acids; Nucleotides; Outcome Study; Pathway interactions; Population; Process; Proteins; Reaction; Research; Role; Site; biological systems; chemical synthesis; cost; economic value; interest; metalloenzyme

PROJECT SUMMARY/ABSTRACT Nitrogenase is a complex metalloenzyme that catalyzes one of the most remarkable chemical transformations in biological systems: the nucleotide-dependent reduction of atmospheric dinitrogen to bioavailable ammonia. There is an outstanding interest in decoding the assembly mechanism of nitrogenase, not only because of its significant relevance to nitrogenase-specific reactions, but also because of its tremendous implication for general metalloprotein biogenesis. Here we propose to greatly expand our understanding of the nitrogenase assembly process by combined genetic, biochemical, spectroscopic and structural approaches. The MoFe protein of the molybdenum nitrogenase of Azotobacter vinelandii will be the focus of the proposed investigation. Through our proposed studies, we expect to further refine the biosynthetic pathways of MoFe protein and its associated clusters, a continuous effort with an ultimate goal to unravel the molecular mechanism of nitrogenase assembly. Furthermore, using nitrogenase as a model system, we also hope to provide general themes of biological metal cluster assembly, which may, in the long run, prove instrumental in developing successful strategies for the chemical synthesis of complex metalloclusters. .

项目概要/摘要 固氮酶是一种复杂的金属酶，可催化最显着的化学转化之一 在生物系统中：大气二氮依赖于核苷酸还原为生物可利用的氨。 人们对解析固氮酶的组装机制有着浓厚的兴趣，这不仅是因为它 与固氮酶特异性反应具有显着相关性，而且还因为它对 一般金属蛋白生物发生。在这里，我们建议大大扩展我们对 结合遗传、生化、光谱和结构的固氮酶组装过程 接近。维氏固氮菌 (Azotobacter vinelandii) 钼固氮酶的 MoFe 蛋白将是 拟议调查的重点。通过我们提出的研究，我们期望进一步完善生物合成 MoFe 蛋白及其相关簇的途径，不断努力，最终目标是解开 固氮酶组装的分子机制。此外，使用固氮酶作为模型系统，我们还 希望提供生物金属簇组装的一般主题，从长远来看，这可能证明 有助于制定复杂金属簇化学合成的成功策略。 。