Radical SAM Enzymes and Metallocofactor Assembly: A Structural Point of View - Groupe Métalloprotéines / Metalloproteins Group (IBS-METALLO) Access content directly
Journal Articles ACS Bio & Med Chem Au Year : 2021

Radical SAM Enzymes and Metallocofactor Assembly: A Structural Point of View

Yvain Nicolet
Patricia Amara

Abstract

This Review focuses on the structure–function relationship of radical S-adenosyl-l-methionine (SAM) enzymes involved in the assembly of metallocofactors corresponding to the active sites of [FeFe]-hydrogenase and nitrogenase [MoFe]-protein. It does not claim to correspond to an extensive review on the assembly machineries of these enzyme active sites, for which many good reviews are already available, but instead deals with the contribution of structural data to the understanding of their chemical mechanism (Buren et al. Chem. Rev. 2020, 142 (25) 11006−11012; Britt et al. Chem. Sci. 2020, 11 (38), 10313–10323). Hence, we will present the history and current knowledge about the radical SAM maturases HydE, HydG, and NifB as well as what, in our opinion, should be done in the near future to overcome the existing barriers in our understanding of this fascinating chemistry that intertwine organic radicals and organometallic complexes.
Fichier principal
Vignette du fichier
Nicolet et al. acsbiomed.pdf (3.31 Mo) Télécharger le fichier
Origin : Publisher files allowed on an open archive

Dates and versions

hal-03454299 , version 1 (29-11-2021)

Identifiers

Cite

Yvain Nicolet, Mickael Cherrier, Patricia Amara. Radical SAM Enzymes and Metallocofactor Assembly: A Structural Point of View. ACS Bio & Med Chem Au, inPress, ⟨10.1021/acsbiomedchemau.1c00044⟩. ⟨hal-03454299⟩
81 View
127 Download

Altmetric

Share

Gmail Facebook X LinkedIn More