Biosynthesis of Nitrogenase Cofactors

作者：Stefan Burén, Emilio Jiménez‐Vicente, Carlos Echávarri‐Erasun, Luis Manuel Rubio · 发表于：Chemical Reviews · 年份：2020 · DOI：10.1021/acs.chemrev.9b00489 · 被引用次数：279 · 研究领域：Metalloenzymes and iron-sulfur proteins、Electrocatalysts for Energy Conversion、RNA modifications and cancer

Abstract Nitrogenase harbors three distinct metal prosthetic groups that are required for its activity. The simplest one is a [4Fe-4S] cluster located at the Fe protein nitrogenase component. The MoFe protein component carries an [8Fe-7S] group called P-cluster and a [7Fe-9S-C-Mo-R-homocitrate] group called FeMo-co. Formation of nitrogenase metalloclusters requires the participation of the structural nitrogenase components and many accessory proteins, and occurs both in situ, for the P-cluster, and in external assembly sites for FeMo-co. The biosynthesis of FeMo-co is performed stepwise and involves molecular scaffolds, metallochaperones, radical chemistry, and novel and unique biosynthetic intermediates. This review provides a critical overview of discoveries on nitrogenase cofactor structure, function, and activity over the last four decades.