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Structure paper

TitleThe distal pocket histidine residue in horse heart myoglobin directs the o-binding mode of nitrite to the heme iron.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 131, Page 18119-18128, Year 2009
Publish dateMay 5, 2009 (structure data deposition date)
AuthorsYi, J. / Heinecke, J. / Tan, H. / Ford, P.C. / Richter-Addo, G.B.
External linksJ. Am. Chem. Soc. / PubMed:19924902
MethodsX-ray diffraction
Resolution1.9 - 2 Å
Structure data

PDB-3hc9:
Ferric Horse Heart Myoglobin; H64V mutant
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3hen:
Ferric Horse Heart Myoglobin; H64V/V67R Mutant
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3heo:
Ferric Horse Heart Myoglobin; H64V/V67R mutant, Nitrite Modified
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3hep:
Ferric Horse Heart Myoglobin; H64V Mutant, Nitrite Modified
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-PO4:
PHOSPHATE ION

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-NO2:
NITRITE ION

Source
  • equus caballus (horse)
KeywordsOXYGEN TRANSPORT / horse heart myoglobin / ferric / H64V mutant / Heme / Iron / Metal-binding / Muscle protein / Transport / ferric myoglobin / horse heart / H64V/V67R mutant / ferric myolobin / H64V/V67R / nitrite adduct

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