| Literature DB >> 23934246 |
Camilla Lambertz1, Agnieszka Adamska-Venkates2, Trevor Simmons3, Julian Esselborn1, Gustav Berggren3, Jens Noth1, Judith Siebel2, Anja Hemschemeier1, Vincent Artero3, Edward Reijerse2, Marc Fontecave3,4, Wolfgang Lubitz2, Thomas Happe1.
Abstract
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.Entities:
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Year: 2013 PMID: 23934246 PMCID: PMC3795299 DOI: 10.1038/nchembio.1311
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040