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

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.
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Submitted on : Monday, November 29, 2021 - 10:25:54 AM
Last modification on : Tuesday, January 4, 2022 - 6:47:57 AM

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

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