Structural highlights
Function
[HBA_TREBE] Involved in oxygen transport from gills to the various peripheral tissues. [HBB_TREBE] Involved in oxygen transport from gills to the various peripheral tissues.
Publication Abstract from PubMed
Despite their high physiological relevance, haemoglobin crystal structures with NO bound to haem constitute less than 1% of the total ligated haemoglobins (Hbs) deposited in the Protein Data Bank. The major difficulty in obtaining NO-ligated Hbs is most likely to be related to the oxidative denitrosylation caused by the high reactivity of the nitrosylated species with O(2). Here, using Raman-assisted X-ray crystallography, it is shown that under X-ray exposure (at four different radiation doses) crystals of nitrosylated haemoglobin from Trematomus bernacchii undergo a transition, mainly in the beta chains, that generates a pentacoordinate species owing to photodissociation of the Fe-NO bond. These data provide a physical explanation for the low number of nitrosylated Hb structures available in the literature.
Selective X-ray-induced NO photodissociation in haemoglobin crystals: evidence from a Raman-assisted crystallographic study.,Merlino A, Fuchs MR, Pica A, Balsamo A, Dworkowski FS, Pompidor G, Mazzarella L, Vergara A Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):137-40. doi:, 10.1107/S0907444912042229. Epub 2012 Dec 20. PMID:23275172[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Merlino A, Fuchs MR, Pica A, Balsamo A, Dworkowski FS, Pompidor G, Mazzarella L, Vergara A. Selective X-ray-induced NO photodissociation in haemoglobin crystals: evidence from a Raman-assisted crystallographic study. Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):137-40. doi:, 10.1107/S0907444912042229. Epub 2012 Dec 20. PMID:23275172 doi:http://dx.doi.org/10.1107/S0907444912042229
