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Título: | Biosynthesis of Nitrogenase Cofactors |
Autor: | Burén, Stefan; Jiménez-Vicente, Emilio; Echávarri-Erasun, Carlos; Rubio, Luis M. | Palabras clave: | Cluster chemistry Metal clusters Metal organic frameworks Monomers Peptides and proteins |
Fecha de publicación: | 24-ene-2020 | Editor: | American Chemical Society | Citación: | Chemical Reviews - Columbus 120(12): 4921-4968 (2020) | Resumen: | 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. | Descripción: | 48 Pág. | Versión del editor: | https://doi.org/10.1021/acs.chemrev.9b00489 | URI: | http://hdl.handle.net/10261/340054 | DOI: | 10.1021/acs.chemrev.9b00489 | ISSN: | 0009-2665 | E-ISSN: | 1520-6890 |
Aparece en las colecciones: | (INIA) Artículos |
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Fichero | Descripción | Tamaño | Formato | |
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Biosynthesis_of_Nitrogenase_Cofactors.pdf | revisión | 53,67 MB | Adobe PDF | Visualizar/Abrir |
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