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TitleMagnesium(II) and zinc(II)-protoporphyrin IX's stabilize the lowest oxygen affinity state of human hemoglobin even more strongly than deoxyheme.
Journal, issue, pagesJ. Mol. Biol., Vol. 292, Page 1121-1136, Year 1999
Publish dateJun 22, 1999 (structure data deposition date)
AuthorsMiyazaki, G. / Morimoto, H. / Yun, K.M. / Park, S.Y. / Nakagawa, A. / Minagawa, H. / Shibayama, N.
External linksJ. Mol. Biol. / PubMed:10512707
MethodsX-ray diffraction
Resolution1.7 Å
Structure data

PDB-1qsh:
MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1qsi:
MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HEG:
PROTOPORPHYRIN IX CONTAINING MG

ChemComp-HOH:
WATER

ChemComp-CMO:
CARBON MONOXIDE

Source
  • homo sapiens (human)
KeywordsOXYGEN STORAGE/TRANSPORT / HEMOGLOBIN; OXYGEN AFFINITY; ALLOSTERIC EFFECT; METAL SUBSTITUTION; TRIGGER MECHANISM / OXYGEN STORAGE-TRANSPORT COMPLEX / HEMOGLOBIN; OXYGEN AFFINITY; ALLOSTERIC EFFECT; METAL SUBSTITUTION; TRIGGER MECHANISM; ALPHA CO LIGANDED

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