Journal
NATURE CHEMICAL BIOLOGY
Volume 9, Issue 10, Pages 607-609Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1311
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Funding
- Bundesministerium fur Bildung und Forschung Bio-H2 project
- Max Planck Society
- French National Research Agency [NiFe-Cat ANR-10-BLAN-711, ARCANE 11-LABX-003]
- European Research Council under the European Union's Seventh Framework Programme (FP/ERC) [306398]
- Swedish Research Council for Environment, Agricultural Sciences and Spatial Planning [213-2010-563]
- Deutsche Forschungsgemeinschaft [HA 255/2-1]
- Volkswagen foundation (LigH2t)
- Studienstiftung des deutschen Volkes
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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 H-2-producing catalysts.
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