Biomimetic assembly and activation of [FeFe]-hydrogenases

@article{Berggren2013BiomimeticAA,
  title={Biomimetic assembly and activation of [FeFe]-hydrogenases},
  author={Gustav Berggren and Anna Julia Adamska and Camilla Lambertz and Trevor R. Simmons and J Esselborn and Mohamed Magdi E. Atta and Serge Gambarelli and J.-M. Mouesca and Edward J. Reijerse and Wolfgang Lubitz and Thomas Happe and Vincent Artero and Marc Fontecave},
  journal={Nature},
  year={2013},
  volume={499},
  pages={66-69}
}
Hydrogenases are the most active molecular catalysts for hydrogen production and uptake, and could therefore facilitate the development of new types of fuel cell. In [FeFe]-hydrogenases, catalysis takes place at a unique di-iron centre (the [2Fe] subsite), which contains a bridging dithiolate ligand, three CO ligands and two CN– ligands. Through a complex multienzymatic biosynthetic process, this [2Fe] subsite is first assembled on a maturation enzyme, HydF, and then delivered to the apo… CONTINUE READING
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Identification and Characterization of the “Super-Reduced” State of the HCluster in [FeFe] Hydrogenase: A New Building Block for the Catalytic Cycle

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