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TitleAn order-disorder transition plays a role in switching off the root effect in fish hemoglobins.
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 32568-32575, Year 2010
Publish dateJun 10, 2010 (structure data deposition date)
AuthorsVergara, A. / Vitagliano, L. / Merlino, A. / Sica, F. / Marino, K. / Verde, C. / di Prisco, G. / Mazzarella, L.
External linksJ. Biol. Chem. / PubMed:20610398
MethodsX-ray diffraction
Resolution2.01 - 2.2 Å
Structure data

PDB-3nfe:
The crystal structure of hemoglobin I from trematomus newnesi in deoxygenated state
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

PDB-3ng6:
The crystal structure of hemoglobin I from Trematomus newnesi in deoxygenated state obtained through an oxidation/reduction cycle in which potassium hexacyanoferrate and sodium dithionite were alternatively added
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HOH:
WATER

Source
  • trematomus newnesi (dusky notothen)
KeywordsOXYGEN TRANSPORT / root effect / fish hemoglobin / antarctic fish

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