1 publication
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Spontaneous Activation of [FeFe]-Hydrogenases by an Inorganic [2Fe] Active Site Mimic
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Nat. Chem. Biol. 2013, 9, 607-609, 10.1038/Nchembio.1311
Hydrogenases catalyze the formation of hydrogen. The cofactor ('H-cluster') of [FeFe]-hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose biosynthesis in vivo requires hydrogenase-specific maturases. Here we show that a chemical mimic of the [2Fe] subcluster can reconstitute apo-hydrogenase to full activity, independent of helper proteins. The assembled H-cluster is virtually indistinguishable from the native cofactor. This procedure will be a powerful tool for developing new artificial H2-producing catalysts.
