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Biosynthesis of Nitrogenase Cofactors

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Journal Chem Rev
Specialty Chemistry
Date 2020 Jan 25
PMID 31975585
Citations 81
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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--homocitrate] group called FeMo-co. Formation of nitrogenase metalloclusters requires the participation of the structural nitrogenase components and many accessory proteins, and occurs both , 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.

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References
1.
Rangaraj P, Ruttimann-Johnson C, Shah V, Ludden P . Accumulation of 55Fe-labeled precursors of the iron-molybdenum cofactor of nitrogenase on NifH and NifX of Azotobacter vinelandii. J Biol Chem. 2001; 276(19):15968-74. DOI: 10.1074/jbc.M100907200. View

2.
El-Gebali S, Mistry J, Bateman A, Eddy S, Luciani A, Potter S . The Pfam protein families database in 2019. Nucleic Acids Res. 2018; 47(D1):D427-D432. PMC: 6324024. DOI: 10.1093/nar/gky995. View

3.
Poole R, Hill S . Respiratory protection of nitrogenase activity in Azotobacter vinelandii--roles of the terminal oxidases. Biosci Rep. 1997; 17(3):303-17. DOI: 10.1023/a:1027336712748. View

4.
Fay A, Blank M, Lee C, Hu Y, Hodgson K, Hedman B . Spectroscopic characterization of the isolated iron-molybdenum cofactor (FeMoco) precursor from the protein NifEN. Angew Chem Int Ed Engl. 2011; 50(34):7787-90. PMC: 3395727. DOI: 10.1002/anie.201102724. View

5.
Kim C, Bowie J . SAM domains: uniform structure, diversity of function. Trends Biochem Sci. 2003; 28(12):625-8. DOI: 10.1016/j.tibs.2003.11.001. View