Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins.
All tetrameric hemoglobins from Antarctic fish, including that from Trematomus bernacchii, HbTb form in the ferric state, promptly and distinctively from all the other tetrameric hemoglobins, a mixture of aquo-met at the α subunits and bis-histidyl adduct (hemichrome) at the β subunits. The role of...
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ftunivnapoliiris:oai:www.iris.unina.it:11588/463458 2024-09-09T19:10:08+00:00 Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins. Balsamo A Sannino F Mazzarella L MERLINO, ANTONELLO PARRILLI, ERMENEGILDA TUTINO, MARIA LUISA VERGARA, ALESSANDRO Balsamo, A Sannino, F Merlino, Antonello Parrilli, Ermenegilda Tutino, MARIA LUISA Mazzarella, L Vergara, Alessandro 2012 http://hdl.handle.net/11588/463458 https://doi.org/10.1016/j.biochi.2011.12.013 http://www.sciencedirect.com/science/article/pii/S0300908411004688 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000302045900005 volume:94 issue:4 firstpage:953 lastpage:960 numberofpages:8 journal:BIOCHIMIE http://hdl.handle.net/11588/463458 doi:10.1016/j.biochi.2011.12.013 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84857459275 http://www.sciencedirect.com/science/article/pii/S0300908411004688 Heme bis-Histidyl coordination β4 hemoglobin Expression Molecular dynamics info:eu-repo/semantics/article 2012 ftunivnapoliiris https://doi.org/10.1016/j.biochi.2011.12.013 2024-06-17T15:19:28Z All tetrameric hemoglobins from Antarctic fish, including that from Trematomus bernacchii, HbTb form in the ferric state, promptly and distinctively from all the other tetrameric hemoglobins, a mixture of aquo-met at the α subunits and bis-histidyl adduct (hemichrome) at the β subunits. The role of the tertiary and quaternary structure in the hemichrome formation is unknown. Here we report the cloning, expression, purification, spectroscopic and computational characterization of the β-chain of HbTb (β-HbTb). Similarly to the human β-chains, β-HbTb self-assembles to form the homotetramer β(4)-HbTb; however, the latter quantitatively forms reversible ferric and ferrous bis-histidyl adducts, which are only partially present in the human tetramer (β(4)-HbA). A molecular dynamics study of the isolated β subunit of the two Hbs indicates that the ability to form hemichrome is an intrinsic feature of the chain; moreover, the greater propensity of β-HbTb to form the bis-histidyl adduct is probably linked to the higher flexibility of the CD loop region. On the bases of these experimental and computational results on the isolated chain, the influence of the quaternary structure on the stability of the endogenous ferrous and ferric hexa-coordination is also discussed. Article in Journal/Newspaper Antarc* Antarctic IRIS Università degli Studi di Napoli Federico II Antarctic Biochimie 94 4 953 960 |
institution |
Open Polar |
collection |
IRIS Università degli Studi di Napoli Federico II |
op_collection_id |
ftunivnapoliiris |
language |
English |
topic |
Heme bis-Histidyl coordination β4 hemoglobin Expression Molecular dynamics |
spellingShingle |
Heme bis-Histidyl coordination β4 hemoglobin Expression Molecular dynamics Balsamo A Sannino F Mazzarella L MERLINO, ANTONELLO PARRILLI, ERMENEGILDA TUTINO, MARIA LUISA VERGARA, ALESSANDRO Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins. |
topic_facet |
Heme bis-Histidyl coordination β4 hemoglobin Expression Molecular dynamics |
description |
All tetrameric hemoglobins from Antarctic fish, including that from Trematomus bernacchii, HbTb form in the ferric state, promptly and distinctively from all the other tetrameric hemoglobins, a mixture of aquo-met at the α subunits and bis-histidyl adduct (hemichrome) at the β subunits. The role of the tertiary and quaternary structure in the hemichrome formation is unknown. Here we report the cloning, expression, purification, spectroscopic and computational characterization of the β-chain of HbTb (β-HbTb). Similarly to the human β-chains, β-HbTb self-assembles to form the homotetramer β(4)-HbTb; however, the latter quantitatively forms reversible ferric and ferrous bis-histidyl adducts, which are only partially present in the human tetramer (β(4)-HbA). A molecular dynamics study of the isolated β subunit of the two Hbs indicates that the ability to form hemichrome is an intrinsic feature of the chain; moreover, the greater propensity of β-HbTb to form the bis-histidyl adduct is probably linked to the higher flexibility of the CD loop region. On the bases of these experimental and computational results on the isolated chain, the influence of the quaternary structure on the stability of the endogenous ferrous and ferric hexa-coordination is also discussed. |
author2 |
Balsamo, A Sannino, F Merlino, Antonello Parrilli, Ermenegilda Tutino, MARIA LUISA Mazzarella, L Vergara, Alessandro |
format |
Article in Journal/Newspaper |
author |
Balsamo A Sannino F Mazzarella L MERLINO, ANTONELLO PARRILLI, ERMENEGILDA TUTINO, MARIA LUISA VERGARA, ALESSANDRO |
author_facet |
Balsamo A Sannino F Mazzarella L MERLINO, ANTONELLO PARRILLI, ERMENEGILDA TUTINO, MARIA LUISA VERGARA, ALESSANDRO |
author_sort |
Balsamo A |
title |
Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins. |
title_short |
Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins. |
title_full |
Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins. |
title_fullStr |
Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins. |
title_full_unstemmed |
Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins. |
title_sort |
role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins. |
publishDate |
2012 |
url |
http://hdl.handle.net/11588/463458 https://doi.org/10.1016/j.biochi.2011.12.013 http://www.sciencedirect.com/science/article/pii/S0300908411004688 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000302045900005 volume:94 issue:4 firstpage:953 lastpage:960 numberofpages:8 journal:BIOCHIMIE http://hdl.handle.net/11588/463458 doi:10.1016/j.biochi.2011.12.013 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84857459275 http://www.sciencedirect.com/science/article/pii/S0300908411004688 |
op_doi |
https://doi.org/10.1016/j.biochi.2011.12.013 |
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Biochimie |
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94 |
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4 |
container_start_page |
953 |
op_container_end_page |
960 |
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