Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic.
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ABSTRACT:
SUBMITTER: Esselborn J
PROVIDER: S-EPMC3795299 | biostudies-literature | 2013 Oct
REPOSITORIES: biostudies-literature
Publications
Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic.
Esselborn Julian J Lambertz Camilla C Adamska-Venkates Agnieszka A Simmons Trevor T Berggren Gustav G Noth Jens J Siebel Judith J Hemschemeier Anja A Artero Vincent V Reijerse Edward E Fontecave Marc M Lubitz Wolfgang W Happe Thomas T
Nature chemical biology 20130811 10
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 ...[more]
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