Cooperative oxygen binding to scapharca inaequivalvis hemoglobin in the crystal. (Articolo in rivista)

Type
Label
  • Cooperative oxygen binding to scapharca inaequivalvis hemoglobin in the crystal. (Articolo in rivista) (literal)
Anno
  • 1996-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1074/jbc.271.7.3627 (literal)
Alternative label
  • Mozzarelli A, Bettati S, Rivetti C, Rossi GL, Colotti G, Chiancone E. (1996)
    Cooperative oxygen binding to scapharca inaequivalvis hemoglobin in the crystal.
    in The Journal of biological chemistry (Print); AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, BETHESDA (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Mozzarelli A, Bettati S, Rivetti C, Rossi GL, Colotti G, Chiancone E. (literal)
Pagina inizio
  • 3627 (literal)
Pagina fine
  • 3632 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 271 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 6 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 7 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • UNIV PARMA,IST SCI BIOCHIM,I-43100 PARMA,ITALY. UNIV ROMA LA SAPIENZA,DIPARTIMENTO SCI BIOCHIM A ROSSI FANELLI, CNR, CTR STUDIO BIOL MOLEC,I-00185 ROME,ITALY (literal)
Titolo
  • Cooperative oxygen binding to scapharca inaequivalvis hemoglobin in the crystal. (literal)
Abstract
  • Oxygen binding to homodimeric Scapharca inaequivalvis hemoglobin (HbI) crystals has been investigated by single-crystal polarized absorption microspectrophotometry. The saturation curve, characterized by a Hill coefficient n(H) = 1.45 and an oxygen pressure at half saturation p(50) = 4.8 torr, at 15 degrees C, shows that HbI in the crystalline state retains positive cooperativity in ligand binding. This finding will permit the correlation of the oxygen-linked conformational changes in the crystal with the expression of cooperativity. Polarized absorption spectra of deoxy-HbI, oxy-HbI, and oxidized HbI crystals indicate that oxygenation does not induce heme reorientation, whereas oxidation does. Lattice interactions prevent the dissociation of oxidized dimers that occurs in solution and stabilize an equilibrium distribution of pentacoordinate and hexacoordinate high spin species. (literal)
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