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 Delta H of oxygenation compared with the majority of mammalian haemoglobins from temperate species (exceptions are represented by some cold-resistant species, such as...
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ftpubmed:oai:pubmedcentral.nih.gov:1224201 2023-05-15T14:54:10+02:00 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 2004-06-15 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1224201 http://www.ncbi.nlm.nih.gov/pubmed/14979874 https://doi.org/10.1042/BJ20031421 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1224201 http://www.ncbi.nlm.nih.gov/pubmed/14979874 http://dx.doi.org/10.1042/BJ20031421 Research Article Text 2004 ftpubmed https://doi.org/10.1042/BJ20031421 2013-08-30T14:14:26Z Haemoglobins from mammals of sub-Arctic and Arctic species, as well as fetal human Hb, are all characterized by a significantly lower Delta H 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 Delta H of oxygenation is mainly due to an increase in the number of the oxygen-linked chloride-binding sites. Text Arctic Ursus arctos PubMed Central (PMC) Arctic Biochemical Journal 380 3 889 896 |
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Research Article |
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Research Article 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. |
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Research Article |
description |
Haemoglobins from mammals of sub-Arctic and Arctic species, as well as fetal human Hb, are all characterized by a significantly lower Delta H 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 Delta H of oxygenation is mainly due to an increase in the number of the oxygen-linked chloride-binding sites. |
format |
Text |
author |
De Rosa, M Cristina Castagnola, Massimo Bertonati, Claudia Galtieri, Antonio Giardina, Bruno |
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. |
publishDate |
2004 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1224201 http://www.ncbi.nlm.nih.gov/pubmed/14979874 https://doi.org/10.1042/BJ20031421 |
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Arctic |
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Arctic |
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Arctic Ursus arctos |
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Arctic Ursus arctos |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1224201 http://www.ncbi.nlm.nih.gov/pubmed/14979874 http://dx.doi.org/10.1042/BJ20031421 |
op_doi |
https://doi.org/10.1042/BJ20031421 |
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Biochemical Journal |
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380 |
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3 |
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889 |
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896 |
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1766325899276320768 |