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Article Dans Une Revue Frontiers in Chemistry Année : 2017

On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes

Résumé

The canonical CysXXXCysXXCys motif is the hallmark of the Radical-SAM superfamily. This motif is responsible for the ligation of a [4Fe-4S] cluster containing a free coordination site available for SAM binding. The five enzymes MoaA, TYW1, MiaB, RimO and LipA contain in addition a second [4Fe-4S] cluster itself bound to three other cysteines and thus also displaying a potentially free coordination site. This review article summarizes recent important achievements obtained on these five enzymes with the main focus to delineate the role of this additional [4Fe-4S] cluster in catalysis.
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hal-01509710 , version 1 (18-04-2017)

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Etienne Mulliez, Victor Duarte, Simon Arragain, Marc Fontecave, Mohamed Atta. On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes. Frontiers in Chemistry, 2017, 5, pp.17. ⟨10.3389/fchem.2017.00017⟩. ⟨hal-01509710⟩
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