Direct Observation of an Iron-Bound Terminal Hydride in [FeFe]-Hydrogenase by Nuclear Resonance Vibrational Spectroscopy.

@article{Reijerse2017DirectOO,
  title={Direct Observation of an Iron-Bound Terminal Hydride in [FeFe]-Hydrogenase by Nuclear Resonance Vibrational Spectroscopy.},
  author={Edward J. Reijerse and Cindy C Pham and Vladimir Pelmenschikov and Ryan Gilbert-Wilson and Agnieszka Adamska-Venkatesh and Judith F Siebel and Leland B Gee and Yoshitaka Yoda and K. Tamasaku and Wolfgang Lubitz and Thomas B Rauchfuss and Stephen P Cramer},
  journal={Journal of the American Chemical Society},
  year={2017},
  volume={139 12},
  pages={4306-4309}
}
[FeFe]-hydrogenases catalyze the reversible reduction of protons to molecular hydrogen with extremely high efficiency. The active site ("H-cluster") consists of a [4Fe-4S]H cluster linked through a bridging cysteine to a [2Fe]H subsite coordinated by CN- and CO ligands featuring a dithiol-amine moiety that serves as proton shuttle between the protein proton channel and the catalytic distal iron site (Fed). Although there is broad consensus that an iron-bound terminal hydride species must occur… CONTINUE READING
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