Biosynthesis of Nitrogenase Cofactors.,Chemical Reviews

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Biosynthesis of Nitrogenase Cofactors.
Chemical Reviews ( IF 51.4 ) Pub Date : 2020-01-24 , DOI: 10.1021/acs.chemrev.9b00489
Stefan Burén ₁ , Emilio Jiménez-Vicente ₂ , Carlos Echavarri-Erasun ₁ , Luis M Rubio ₁

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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.

中文翻译：

固氮酶辅因子的生物合成。

固氮酶具有其活性所需的三个不同的金属辅基。最简单的是位于 Fe 蛋白固氮酶组分处的 [4Fe-4S] 簇。 MoFe 蛋白质成分带有一个称为 P-簇的 [8Fe-7S] 基团和一个称为 FeMo-co 的 [7Fe-9S-C-Mo- R-高柠檬酸盐] 基团。固氮酶金属簇的形成需要结构固氮酶组分和许多辅助蛋白的参与，并且在 P 簇原位发生，以及 FeMo-co 的外部组装位点发生。 FeMo-co 的生物合成是逐步进行的，涉及分子支架、金属伴侣、自由基化学以及新颖独特的生物合成中间体。这篇综述对过去四十年来固氮酶辅因子结构、功能和活性的发现进行了重要概述。

更新日期：2020-01-24

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