From the arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin (Articolo in rivista)

Type
Label
  • From the arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Alternative label
  • Maria Cristina De Rosa; Massimo Castagnola; Claudia Bertonati; Antonio Galtieri; Bruno Giardina (2004)
    From the arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin
    in Biochemical journal (Lond., 1984)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Maria Cristina De Rosa; Massimo Castagnola; Claudia Bertonati; Antonio Galtieri; Bruno Giardina (literal)
Pagina inizio
  • 889 (literal)
Pagina fine
  • 896 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 380 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Biochemistry and Clinical Biochemistry and CNR Institute of Chemistry of Molecular Recognition, Catholic University of Rome, L.go F. Vito 1, 00168 Rome, Italy, Department of Organic and Biological Chemistry, University of Messina, Salita Sperone 31, Villaggio S. Agata, 98166 Messina, Italy (literal)
Titolo
  • From the arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin (literal)
Abstract
  • Haemoglobins from mammals of sub-Arctic and Arctic species, as well as fetal human Hb, are all characterized by a significantly lower deltaH of oxygenation compared with the majority of mammalian haemoglobins from temperate species (exceptions are represented by some cold-resistant species, such as cow, horse and pig). This has been interpreted as an adaptive mechanism of great importance from a physiological point of view. To date, the molecular basis of this thermodynamic characteristic is still not known. In the present study,we showthat binding of extra chloride (with respect to adult human Hb) ions to Hb would significantly contribute to lowering the overall heat of oxygenation, thus providing a molecular basis for the low effect of temperature on the oxygenation-deoxygenation cycle. To this aim, the oxygen binding properties of bovine Hb, bear (Ursus arctos) Hb and horse Hb, which are representative of this series of haemoglobins, have been studied with special regard to the effect of heterotropic ligands, such as organic phosphates (namely 2,3-diphosphoglycerate) and chloride. Functional results are consistent with a mechanism for ligand binding that involves an additional binding site for chloride ion. Analysis of computational chemistry results, obtained by the GRID program, further confirm the hypothesis that the reason for the lower deltaH of oxygenation is mainly due to an increase in the number of the oxygen-linked chloride-binding sites. (literal)
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