Carbon-sulfur bond-forming reaction catalysed by the radical SAM enzyme HydE. - Université Grenoble Alpes Accéder directement au contenu
Article Dans Une Revue Nature Chemistry Année : 2016

Carbon-sulfur bond-forming reaction catalysed by the radical SAM enzyme HydE.

Résumé

Carbon-sulfur bond formation at aliphatic positions is a challenging reaction that is performed efficiently by radical S-adenosyl-L-methionine (SAM) enzymes. Here we report that 1,3-thiazolidines can act as ligands and substrates for the radical SAM enzyme HydE, which is involved in the assembly of the active site of [FeFe]-hydrogenase. Using X-ray crystallography, in vitro assays and NMR spectroscopy we identified a radical-based reaction mechanism that is best described as the formation of a C-centred radical that concomitantly attacks the sulfur atom of a thioether. To the best of our knowledge, this is the first example of a radical SAM enzyme that reacts directly on a sulfur atom instead of abstracting a hydrogen atom. Using theoretical calculations based on our high-resolution structures we followed the evolution of the electronic structure from SAM through to the formation of S-adenosyl-L-cysteine. Our results suggest that, at least in this case, the widely proposed and highly reactive 5'-deoxyadenosyl radical species that triggers the reaction in radical SAM enzymes is not an isolable intermediate.
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Dates et versions

hal-01341083 , version 1 (04-07-2016)

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Roman Rohac, Patricia Amara, Alhosna Benjdia, Lydie Martin, Pauline Ruffié, et al.. Carbon-sulfur bond-forming reaction catalysed by the radical SAM enzyme HydE.. Nature Chemistry, 2016, 8 (5), pp.491-500. ⟨10.1038/NCHEM.2490⟩. ⟨hal-01341083⟩
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