The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site

@article{Shima2008TheCS,
  title={The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site},
  author={Seigo Shima and Oliver Pilak and Sonja Vogt and Michael Bernhard Schick and Marco Salomone Stagni and Wolfram Meyer‐Klaucke and Eberhard Warkentin and Rudolf K Thauer and Ulrich Ermler},
  journal={Science},
  year={2008},
  volume={321},
  pages={572 - 575}
}
Biological formation and consumption of molecular hydrogen (H2) are catalyzed by hydrogenases, of which three phylogenetically unrelated types are known: [NiFe]-hydrogenases, [FeFe]-hydrogenases, and [Fe]-hydrogenase. We present a crystal structure of [Fe]-hydrogenase at 1.75 angstrom resolution, showing a mononuclear iron coordinated by the sulfur of cysteine 176, two carbon monoxide (CO) molecules, and the sp2-hybridized nitrogen of a 2-pyridinol compound with back-bonding properties similar… 

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