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-Structure paper
Title | The distal pocket histidine residue in horse heart myoglobin directs the o-binding mode of nitrite to the heme iron. |
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Journal, issue, pages | J. Am. Chem. Soc., Vol. 131, Page 18119-18128, Year 2009 |
Publish date | May 5, 2009 (structure data deposition date) |
![]() | Yi, J. / Heinecke, J. / Tan, H. / Ford, P.C. / Richter-Addo, G.B. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.9 - 2 Å |
Structure data | ![]() PDB-3hc9: ![]() PDB-3hen: ![]() PDB-3heo: ![]() PDB-3hep: |
Chemicals | ![]() ChemComp-HEM: ![]() ChemComp-PO4: ![]() ChemComp-NA: ![]() ChemComp-HOH: ![]() ChemComp-NO2: |
Source |
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![]() | OXYGEN 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 |