Bridging Hydride at Reduced H-Cluster Species in [FeFe]-Hydrogenases Revealed by Infrared Spectroscopy, Isotope Editing, and Quantum Chemistry.

@article{Mebs2017BridgingHA,
  title={Bridging Hydride at Reduced H-Cluster Species in [FeFe]-Hydrogenases Revealed by Infrared Spectroscopy, Isotope Editing, and Quantum Chemistry.},
  author={Stefan Mebs and Moritz Senger and Jifu Duan and Florian Wittkamp and Ulf-Peter Apfel and Thomas Happe and Martin Winkler and Sven Timo Stripp and Michael Haumann},
  journal={Journal of the American Chemical Society},
  year={2017},
  volume={139 35},
  pages={
          12157-12160
        }
}
[FeFe]-Hydrogenases contain a H2-converting cofactor (H-cluster) in which a canonical [4Fe-4S] cluster is linked to a unique diiron site with three carbon monoxide (CO) and two cyanide (CN-) ligands (e.g., in the oxidized state, Hox). There has been much debate whether reduction and hydrogen binding may result in alternative rotamer structures of the diiron… CONTINUE READING