Maturation of the [FeFe]‐Hydrogenase: Direct Transfer of the (κ3‐cysteinate)FeII(CN)(CO)2 Complex‐B from HydG to HydE - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Angewandte Chemie International Edition Année : 2023

Maturation of the [FeFe]‐Hydrogenase: Direct Transfer of the (κ3‐cysteinate)FeII(CN)(CO)2 Complex‐B from HydG to HydE

Résumé

FeFe]‐hydrogenases efficiently catalyze the reversible oxidation of molecular hydrogen. Their prowess stems from the intricate H‐cluster, combining a [Fe4S4] center with a binuclear iron center ([2Fe]H). In the latter, each iron atom is coordinated by a CO and CN ligand, connected by a CO and an azadithiolate ligand. The synthesis of this active site involves a unique multiprotein assembly, featuring radical SAM proteins HydG and HydE. HydG initiates the transformation of L‐tyrosine into cyanide and carbon monoxide to generate complex‐B, which is subsequently transferred to HydE to continue the biosynthesis of the [2Fe]H‐subcluster. Due to its instability, complex‐B isolation for structural or spectroscopic characterization has been elusive this far. Nevertheless, the use of a biomimetic compound of complex‐B allowed circumventing the need for the HydG protein during in vitro functional investigations, implying a similar structure for complex‐B. Here, we used the HydE protein as a nanocage to encapsulate and stabilize the complex‐B product generated by HydG. Using X‐ray crystallography, we successfully determined its structure at 1.3 Å resolution. Furthermore, we demonstrated that complex‐B is directly transferred from HydG to HydE, thus not being released into the solution post‐synthesis, highlighting a transient interaction between the two proteins.

Dates et versions

hal-04285940 , version 1 (14-11-2023)

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Citer

Juneina Omeiri, Lydie Martin, Anthony Usclat, Mickael Cherrier, Yvain Nicolet. Maturation of the [FeFe]‐Hydrogenase: Direct Transfer of the (κ3‐cysteinate)FeII(CN)(CO)2 Complex‐B from HydG to HydE. Angewandte Chemie International Edition, 2023, pp.e202314819. ⟨10.1002/anie.202314819⟩. ⟨hal-04285940⟩
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