From the Artic 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 DeltaH of oxygenation compared with the majority of mammalian haemoglobins from temperate species (exceptions are represented by some cold-resistant species, such as...
Main Authors: | , , |
---|---|
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Biochemical Society
2004
|
Subjects: | |
Online Access: | http://hdl.handle.net/10807/25597 |
id |
ftunicattolicair:oai:publicatt.unicatt.it:10807/25597 |
---|---|
record_format |
openpolar |
spelling |
ftunicattolicair:oai:publicatt.unicatt.it:10807/25597 2023-12-03T10:17:24+01:00 From the Artic to fetal life: physiological importance and structural basis of an "additional" chloride binding site in haemoglobin Castagnola, Massimo Giardina, Bruno De Rosa, Maria Cristina Castagnola, Massimo Giardina, Bruno De Rosa, Maria Cristina 2004 http://hdl.handle.net/10807/25597 eng eng Biochemical Society country:ITA issue:Ottobre firstpage:889 lastpage:896 numberofpages:8 issueyear:2004 journal:BIOCHEMICAL JOURNAL http://hdl.handle.net/10807/25597 HAEMOGLOBIN Settore BIO/10 - BIOCHIMICA info:eu-repo/semantics/article 2004 ftunicattolicair 2023-11-07T23:34:31Z 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 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 DeltaH of oxygenation is mainly due to an increase in the number of the oxygen-linked chloride-binding sites. Article in Journal/Newspaper Arctic Ursus arctos Università Cattolica del Sacro Cuore: PubliCatt Arctic |
institution |
Open Polar |
collection |
Università Cattolica del Sacro Cuore: PubliCatt |
op_collection_id |
ftunicattolicair |
language |
English |
topic |
HAEMOGLOBIN Settore BIO/10 - BIOCHIMICA |
spellingShingle |
HAEMOGLOBIN Settore BIO/10 - BIOCHIMICA Castagnola, Massimo Giardina, Bruno De Rosa, Maria Cristina From the Artic to fetal life: physiological importance and structural basis of an "additional" chloride binding site in haemoglobin |
topic_facet |
HAEMOGLOBIN Settore BIO/10 - BIOCHIMICA |
description |
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 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 DeltaH of oxygenation is mainly due to an increase in the number of the oxygen-linked chloride-binding sites. |
author2 |
Castagnola, Massimo Giardina, Bruno De Rosa, Maria Cristina |
format |
Article in Journal/Newspaper |
author |
Castagnola, Massimo Giardina, Bruno De Rosa, Maria Cristina |
author_facet |
Castagnola, Massimo Giardina, Bruno De Rosa, Maria Cristina |
author_sort |
Castagnola, Massimo |
title |
From the Artic to fetal life: physiological importance and structural basis of an "additional" chloride binding site in haemoglobin |
title_short |
From the Artic to fetal life: physiological importance and structural basis of an "additional" chloride binding site in haemoglobin |
title_full |
From the Artic to fetal life: physiological importance and structural basis of an "additional" chloride binding site in haemoglobin |
title_fullStr |
From the Artic to fetal life: physiological importance and structural basis of an "additional" chloride binding site in haemoglobin |
title_full_unstemmed |
From the Artic to fetal life: physiological importance and structural basis of an "additional" chloride binding site in haemoglobin |
title_sort |
from the artic to fetal life: physiological importance and structural basis of an "additional" chloride binding site in haemoglobin |
publisher |
Biochemical Society |
publishDate |
2004 |
url |
http://hdl.handle.net/10807/25597 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic Ursus arctos |
genre_facet |
Arctic Ursus arctos |
op_relation |
issue:Ottobre firstpage:889 lastpage:896 numberofpages:8 issueyear:2004 journal:BIOCHEMICAL JOURNAL http://hdl.handle.net/10807/25597 |
_version_ |
1784264360298807296 |