The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin.

@article{Hamdane2003TheRS,
  title={The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin.},
  author={Djemel Hamdane and Laurent Kiger and Sylvia Dewilde and Brian N. Green and Alessandra Pesce and Julien Uzan and Thorsten Burmester and Thomas Hankeln and Martino Bolognesi and L. Moens and M C Michael C Marden},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 51},
  pages={51713-21}
}
Neuroglobin and cytoglobin reversibly bind oxygen in competition with the distal histidine, and the observed oxygen affinity therefore depends on the properties of both ligands. In the absence of an external ligand, the iron atom of these globins is hexacoordinated. There are three cysteine residues in human neuroglobin; those at positions CD7 and D5 are sufficiently close to form an internal disulfide bond. Both cysteine residues in cytoglobin, although localized in other positions than in… CONTINUE READING

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Neuroglobin, Dependence of Oxygen Affinity on Disulfide Bond 51721 by gest on D ecem er 26

  • L. J. Matthias, P. T. Yam, +5 authors P. J. Hogg
  • Nat. Immunol
  • 2002
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