Magnesium(II) and zinc(II)-protoporphyrin IX's stabilize the lowest oxygen affinity state of human hemoglobin even more strongly than deoxyheme

Journal of Molecular Biology

Volumn 292, Issue 5, 1999, Pages 1121-1136

  Miyazaki, Gentaro ^a   Morimoto, Hideki ^a   Yun, Kyung Mook ^a   Park, Sam Yong ^b   Nakagawa, Atushi ^a   Minagawa, Hirotaka ^c   Shibayama, Naoya ^d  

^a OSAKA UNIVERSITY   (Japan)

^b RIKEN HARIMA INSTITUTE   (Japan)

^c NEC CORPORATION   (Japan)

^d JICHI MEDICAL UNIVERSITY   (Japan)

Author keywords

Allosteric effect; Hemoglobin; Metal substitution; Oxygen affinity; Trigger mechanism

Indexed keywords

DEOXYHEMOGLOBIN; HEMOGLOBIN; HYBRID PROTEIN; MAGNESIUM ION; PHYTIC ACID; PROTEIN SUBUNIT; PROTOPORPHYRIN; ZINC ION;

ALLOSTERISM; ARTICLE; CONTROLLED STUDY; EQUILIBRIUM CONSTANT; HUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

EID: 0033536620     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3124     Document Type: Article

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