Adaptation to extreme environments: structure-function relationships in Emperor penguin haemoglobin
The functional properties of the single haemoglobin (Hb) of Emperor penguin (Aptenodytes forsteri) have been investigated at different temperatures as a function of proton and organic phosphate concentration. The complete amino acid sequence has been established. Comparison with that of human HbA sh...
Published in: | Journal of Molecular Biology |
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Language: | English |
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1994
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Online Access: | http://hdl.handle.net/2108/54671 https://doi.org/10.1006/jmbi.1994.1259 |
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ftunivromatorver:oai:art.torvergata.it:2108/54671 2024-05-19T07:32:46+00:00 Adaptation to extreme environments: structure-function relationships in Emperor penguin haemoglobin Tamburrini, M di Prisco, G Giardina, B. CONDO', SAVERIO GIOVANNI Tamburrini, M Condo', Sg di Prisco, G Giardina, B 1994-04-15 http://hdl.handle.net/2108/54671 https://doi.org/10.1006/jmbi.1994.1259 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:A1994NF66000007 volume:237 issue:5 firstpage:615 lastpage:621 journal:JOURNAL OF MOLECULAR BIOLOGY http://hdl.handle.net/2108/54671 doi:10.1006/jmbi.1994.1259 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0028284553 Animal Thermodynamic Oxyhemoglobin Hydrogen-Ion Concentration Inositol Temperature Amino Acid Sequence Protein Binding Structure-Activity Relationship Oxygen Hemoglobin Sequence Alignment Sequence Analysi Molecular Sequence Data Birds Settore BIO/10 - BIOCHIMICA info:eu-repo/semantics/article 1994 ftunivromatorver https://doi.org/10.1006/jmbi.1994.1259 2024-04-30T23:58:45Z The functional properties of the single haemoglobin (Hb) of Emperor penguin (Aptenodytes forsteri) have been investigated at different temperatures as a function of proton and organic phosphate concentration. The complete amino acid sequence has been established. Comparison with that of human HbA shows 12 substitutions in the contact regions of alpha beta dimers. In addition to overall similarities shared with most of the avian Hbs previously described, this Hb shows significant differences, which could be related to the peculiar behaviour of this penguin. In particular we may consider that: (1) the shape of the Bohr effect curve seems well adapted for gas exchange during very prolonged dives, preserving penguin Hb from a sudden and not controlled stripping of oxygen; (2) the very minor enthalpy change observed at lower pH could be an example of molecular adaptation, through which oxygen delivery becomes essentially insensitive to exposure to the extremely low temperatures of the environment. Moreover, the small alkaline Bohr effect has been found to be only chloride-linked, since the pH dependence of the oxygen affinity is totally abolished in the absence of this ion. These functional characteristics are discussed on the basis of the primary structure of alpha and beta-chains. Article in Journal/Newspaper Aptenodytes forsteri Universitá degli Studi di Roma "Tor Vergata": ART - Archivio Istituzionale della Ricerca Journal of Molecular Biology 237 5 615 621 |
institution |
Open Polar |
collection |
Universitá degli Studi di Roma "Tor Vergata": ART - Archivio Istituzionale della Ricerca |
op_collection_id |
ftunivromatorver |
language |
English |
topic |
Animal Thermodynamic Oxyhemoglobin Hydrogen-Ion Concentration Inositol Temperature Amino Acid Sequence Protein Binding Structure-Activity Relationship Oxygen Hemoglobin Sequence Alignment Sequence Analysi Molecular Sequence Data Birds Settore BIO/10 - BIOCHIMICA |
spellingShingle |
Animal Thermodynamic Oxyhemoglobin Hydrogen-Ion Concentration Inositol Temperature Amino Acid Sequence Protein Binding Structure-Activity Relationship Oxygen Hemoglobin Sequence Alignment Sequence Analysi Molecular Sequence Data Birds Settore BIO/10 - BIOCHIMICA Tamburrini, M di Prisco, G Giardina, B. CONDO', SAVERIO GIOVANNI Adaptation to extreme environments: structure-function relationships in Emperor penguin haemoglobin |
topic_facet |
Animal Thermodynamic Oxyhemoglobin Hydrogen-Ion Concentration Inositol Temperature Amino Acid Sequence Protein Binding Structure-Activity Relationship Oxygen Hemoglobin Sequence Alignment Sequence Analysi Molecular Sequence Data Birds Settore BIO/10 - BIOCHIMICA |
description |
The functional properties of the single haemoglobin (Hb) of Emperor penguin (Aptenodytes forsteri) have been investigated at different temperatures as a function of proton and organic phosphate concentration. The complete amino acid sequence has been established. Comparison with that of human HbA shows 12 substitutions in the contact regions of alpha beta dimers. In addition to overall similarities shared with most of the avian Hbs previously described, this Hb shows significant differences, which could be related to the peculiar behaviour of this penguin. In particular we may consider that: (1) the shape of the Bohr effect curve seems well adapted for gas exchange during very prolonged dives, preserving penguin Hb from a sudden and not controlled stripping of oxygen; (2) the very minor enthalpy change observed at lower pH could be an example of molecular adaptation, through which oxygen delivery becomes essentially insensitive to exposure to the extremely low temperatures of the environment. Moreover, the small alkaline Bohr effect has been found to be only chloride-linked, since the pH dependence of the oxygen affinity is totally abolished in the absence of this ion. These functional characteristics are discussed on the basis of the primary structure of alpha and beta-chains. |
author2 |
Tamburrini, M Condo', Sg di Prisco, G Giardina, B |
format |
Article in Journal/Newspaper |
author |
Tamburrini, M di Prisco, G Giardina, B. CONDO', SAVERIO GIOVANNI |
author_facet |
Tamburrini, M di Prisco, G Giardina, B. CONDO', SAVERIO GIOVANNI |
author_sort |
Tamburrini, M |
title |
Adaptation to extreme environments: structure-function relationships in Emperor penguin haemoglobin |
title_short |
Adaptation to extreme environments: structure-function relationships in Emperor penguin haemoglobin |
title_full |
Adaptation to extreme environments: structure-function relationships in Emperor penguin haemoglobin |
title_fullStr |
Adaptation to extreme environments: structure-function relationships in Emperor penguin haemoglobin |
title_full_unstemmed |
Adaptation to extreme environments: structure-function relationships in Emperor penguin haemoglobin |
title_sort |
adaptation to extreme environments: structure-function relationships in emperor penguin haemoglobin |
publishDate |
1994 |
url |
http://hdl.handle.net/2108/54671 https://doi.org/10.1006/jmbi.1994.1259 |
genre |
Aptenodytes forsteri |
genre_facet |
Aptenodytes forsteri |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:A1994NF66000007 volume:237 issue:5 firstpage:615 lastpage:621 journal:JOURNAL OF MOLECULAR BIOLOGY http://hdl.handle.net/2108/54671 doi:10.1006/jmbi.1994.1259 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0028284553 |
op_doi |
https://doi.org/10.1006/jmbi.1994.1259 |
container_title |
Journal of Molecular Biology |
container_volume |
237 |
container_issue |
5 |
container_start_page |
615 |
op_container_end_page |
621 |
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1799470947295559680 |