Department of Molecular Biology and Biochemistry and.
Department of Chemistry, University of California, Irvine, California 92697-2025; email:
Annu Rev Biochem. 2016 Jun 2;85:455-83. doi: 10.1146/annurev-biochem-060614-034108. Epub 2016 Feb 1.
Nitrogenase is a versatile metalloenzyme that is capable of catalyzing two important reactions under ambient conditions: the reduction of nitrogen (N2) to ammonia (NH3), a key step in the global nitrogen cycle; and the reduction of carbon monoxide (CO) and carbon dioxide (CO2) to hydrocarbons, two reactions useful for recycling carbon waste into carbon fuel. The molybdenum (Mo)- and vanadium (V)-nitrogenases are two homologous members of this enzyme family. Each of them contains a P-cluster and a cofactor, two high-nuclearity metalloclusters that have crucial roles in catalysis. This review summarizes the progress that has been made in elucidating the biosynthetic mechanisms of the P-cluster and cofactor species of nitrogenase, focusing on what is known about the assembly mechanisms of the two metalloclusters in Mo-nitrogenase and giving a brief account of the possible assembly schemes of their counterparts in V-nitrogenase, which are derived from the homology between the two nitrogenases.
固氮酶是一种多功能的金属酶，能够在环境条件下催化两个重要反应：氮气 (N2) 还原为氨 (NH3)，这是全球氮循环中的关键步骤；以及一氧化碳 (CO) 和二氧化碳 (CO2) 还原为烃类，这两个反应有助于将碳废物回收成碳燃料。钼 (Mo)-和钒 (V)-固氮酶是该酶家族的两个同源成员。它们都包含 P 簇和辅因子，这两个高核金属簇在催化中起着关键作用。本综述总结了阐明固氮酶 P 簇和辅因子物种生物合成机制的进展，重点介绍了 Mo-固氮酶中两个金属簇的组装机制，以及简要描述了 V-固氮酶中相应金属簇的可能组装方案，这些方案源自两种固氮酶之间的同源性。
