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Article Dans Une Revue Nature Chemical Biology Année : 2013

Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic

Résumé

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.

Dates et versions

hal-01069155 , version 1 (28-09-2014)

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Citer

Julian Esselborn, Camilla Lambertz, Agnieszka Adamska-Venkatesh, Trevor Simmons, Gustav Berggren, et al.. Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic. Nature Chemical Biology, 2013, 9 (10), pp.607-9. ⟨10.1038/nchembio.1311⟩. ⟨hal-01069155⟩
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