The α1β1 contact of human hemoglobin plays a key role in stabilizing the bound dioxygen: Further evidence from the iron valency hybrids

European Journal of Biochemistry

Volumn 269, Issue 1, 2002, Pages 202-211

  Yasuda, Jun Pei ^a   Ichikawa, Takayuki ^a   Tsuruga, Mie ^a   Matsuoka, Ariki ^b   Sugawara, Yoshiaki ^c   Shikama, Keiji ^a,d  

^a TOHOKU UNIVERSITY   (Japan)

^b FUKUSHIMA MEDICAL UNIVERSITY   (Japan)

^c Hiroshima Prefectural Womens Univ   (Japan)

^d PHP Laboratory for Molecular Biology   (Japan)

Author keywords

1 1 contact; Acid catalysis; Chain nonequivalence; Hb oxidation; Valency hybrids

Indexed keywords

ACID; FERRIC OXIDE; HEMOGLOBIN A; HISTIDINE; IRON; METHEMOGLOBIN; OXYGEN; OXYHEMOGLOBIN; PROTON; TETRAMER;

ALPHA CHAIN; ARTICLE; AUTOOXIDATION; BETA CHAIN; CATALYSIS; CONTROLLED STUDY; HUMAN; HYBRID; MATHEMATICAL ANALYSIS; MOLECULAR INTERACTION; PH; PRIORITY JOURNAL;

DIMERIZATION; HEMOGLOBINS; HUMANS; HYDROGEN-ION CONCENTRATION; IRON; KINETICS; OXIDATION-REDUCTION; OXYHEMOGLOBINS;

EID: 0036151091     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.0014-2956.2002.02635.x     Document Type: Article

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