From the Arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin

Haemoglobins from mammals of sub-Arctic and Arctic species, as well as fetal human Hb, are all characterized by a significantly lower ΔH of oxygenation compared with the majority of mammalian haemoglobins from temperate species (exceptions are represented by some cold-resistant species, such as cow,...

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Published in:Biochemical Journal
Main Authors: DE ROSA, M. Cristina, CASTAGNOLA, Massimo, BERTONATI, Claudia, GALTIERI, Antonio, GIARDINA, Bruno
Format: Article in Journal/Newspaper
Language:English
Published: Portland Press Ltd. 2004
Subjects:
Online Access:http://dx.doi.org/10.1042/bj20031421
https://portlandpress.com/biochemj/article-pdf/380/3/889/715022/bj3800889.pdf
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spelling crportlandpress:10.1042/bj20031421 2024-09-15T18:40:15+00:00 From the Arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin DE ROSA, M. Cristina CASTAGNOLA, Massimo BERTONATI, Claudia GALTIERI, Antonio GIARDINA, Bruno 2004 http://dx.doi.org/10.1042/bj20031421 https://portlandpress.com/biochemj/article-pdf/380/3/889/715022/bj3800889.pdf en eng Portland Press Ltd. Biochemical Journal volume 380, issue 3, page 889-896 ISSN 0264-6021 1470-8728 journal-article 2004 crportlandpress https://doi.org/10.1042/bj20031421 2024-08-01T04:17:37Z Haemoglobins from mammals of sub-Arctic and Arctic species, as well as fetal human Hb, are all characterized by a significantly lower ΔH 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 show that 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 ΔH of oxygenation is mainly due to an increase in the number of the oxygen-linked chloride-binding sites. Article in Journal/Newspaper Ursus arctos Portland Press Biochemical Journal 380 3 889 896
institution Open Polar
collection Portland Press
op_collection_id crportlandpress
language English
description Haemoglobins from mammals of sub-Arctic and Arctic species, as well as fetal human Hb, are all characterized by a significantly lower ΔH 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 show that 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 ΔH of oxygenation is mainly due to an increase in the number of the oxygen-linked chloride-binding sites.
format Article in Journal/Newspaper
author DE ROSA, M. Cristina
CASTAGNOLA, Massimo
BERTONATI, Claudia
GALTIERI, Antonio
GIARDINA, Bruno
spellingShingle DE ROSA, M. Cristina
CASTAGNOLA, Massimo
BERTONATI, Claudia
GALTIERI, Antonio
GIARDINA, Bruno
From the Arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin
author_facet DE ROSA, M. Cristina
CASTAGNOLA, Massimo
BERTONATI, Claudia
GALTIERI, Antonio
GIARDINA, Bruno
author_sort DE ROSA, M. Cristina
title From the Arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin
title_short From the Arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin
title_full From the Arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin
title_fullStr From the Arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin
title_full_unstemmed From the Arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin
title_sort from the arctic to fetal life: physiological importance and structural basis of an additional chloride-binding site in haemoglobin
publisher Portland Press Ltd.
publishDate 2004
url http://dx.doi.org/10.1042/bj20031421
https://portlandpress.com/biochemj/article-pdf/380/3/889/715022/bj3800889.pdf
genre Ursus arctos
genre_facet Ursus arctos
op_source Biochemical Journal
volume 380, issue 3, page 889-896
ISSN 0264-6021 1470-8728
op_doi https://doi.org/10.1042/bj20031421
container_title Biochemical Journal
container_volume 380
container_issue 3
container_start_page 889
op_container_end_page 896
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