The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster.

@article{Fourmond2014TheOI,
  title={The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster.},
  author={Vincent Fourmond and Claudio Greco and Kateryna Sybirna and Carole Baffert and Po-hung Wang and Pierre Ezanno and Marco Montefiori and Maurizio Bruschi and Isabelle Meynial-Salles and Philippe Soucaille and Jochen Blumberger and Herv{\'e} Bottin and Luca de Gioia and Christophe L{\'e}ger},
  journal={Nature chemistry},
  year={2014},
  volume={6 4},
  pages={336-42}
}
Nature is a valuable source of inspiration in the design of catalysts, and various approaches are used to elucidate the mechanism of hydrogenases, the enzymes that oxidize or produce H2. In FeFe hydrogenases, H2 oxidation occurs at the H-cluster, and catalysis involves H2 binding on the vacant coordination site of an iron centre. Here, we show that the reversible oxidative inactivation of this enzyme results from the binding of H2 to coordination positions that are normally blocked by intrinsic… CONTINUE READING
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