Carbon monoxide and cyanide as intrinsic ligands to iron in the active site of [NiFe]-hydrogenases. NiFe(CN)2CO, Biology's way to activate H2.

@article{Pierik1999CarbonMA,
  title={Carbon monoxide and cyanide as intrinsic ligands to iron in the active site of [NiFe]-hydrogenases. NiFe(CN)2CO, Biology's way to activate H2.},
  author={Antonio J. Pierik and Winfried Roseboom and Randolph P. Happe and Kimberly A. Bagley and Simon P. J. Albracht},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 6},
  pages={3331-7}
}
Infrared-spectroscopic studies on the [NiFe]-hydrogenase of Chromatium vinosum-enriched in 15N or 13C, as well as chemical analyses, show that this enzyme contains three non-exchangeable, intrinsic, diatomic molecules as ligands to the active site, one carbon monoxide molecule and two cyanide groups. The results form an explanation for the three non-protein ligands to iron detected in the crystal structure of the Desulfovibrio gigas hydrogenase (Volbeda, A., Garcin, E., Piras, C., De Lacey, A… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 26 extracted citations

Studies on hydrogenase

Proceedings of the Japan Academy. Series B, Physical and biological sciences • 2013

Similar Papers

Loading similar papers…