The heme environment of mouse neuroglobin. Evidence for the presence of two conformations of the heme pocket.

@article{Couture2001TheHE,
  title={The heme environment of mouse neuroglobin. Evidence for the presence of two conformations of the heme pocket.},
  author={Manon Couture and Thorsten Burmester and Thomas Hankeln and Denis L. Rousseau},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 39},
  pages={36377-82}
}
Neuroglobin (Ngb) is a newly discovered oxygen-binding heme protein that is primarily expressed in the brain of humans and other vertebrates. To characterize the structure/function relationships of this new heme protein, we have used resonance Raman spectroscopy to determine the structure of the heme environment in Ngb from mice. In the Fe(2+)CO complex, two conformations of the Fe-CO unit are present, one of which arises from an open conformation of the heme pocket in which the CO is not… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 24 extracted citations

Structure and function of haemoglobins.

Blood cells, molecules & diseases • 2018

Similar Papers

Loading similar papers…