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On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes
Etienne Mulliez1, Victor Duarte1, Simon Arragain2
1Biosciences and Biotechnology Institute of Grenoble, Laboratoire de Chimie et Biologie des Métaux, UMR 5249 CEA-Centre National de la Recherche Scientifique-UGA Grenoble, France.
Abstract:
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.