Protonation of histidine 55 affects the oxygen access to heme in the alpha chain of the hemoglobin from the Antarctic fish Trematomus bernacchii.
The Root effect describes the drastic drop of oxygen affinity and loss of cooperativity at acidic pH expressed in the hemoglobins (Hb) of certain fish. The comparison between the deoxy structures of the Root effect Hb from the Antarctic fish Trematomus bernacchii (HbTb) at different pHs (pH = 6.2 an...
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Online Access: | http://hdl.handle.net/11588/404502 https://doi.org/10.1002/iub.436 http://onlinelibrary.wiley.com/doi/10.1002/iub.436/abstract |
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ftunivnapoliiris:oai:www.iris.unina.it:11588/404502 2024-09-09T19:08:19+00:00 Protonation of histidine 55 affects the oxygen access to heme in the alpha chain of the hemoglobin from the Antarctic fish Trematomus bernacchii. Boechi L. Martì M. A. Estrin D. A. VERGARA, ALESSANDRO SICA, FILOMENA MAZZARELLA, LELIO MERLINO, ANTONELLO Boechi, L. Martì, M. A. Vergara, Alessandro Sica, Filomena Mazzarella, Lelio Estrin, D. A. Merlino, Antonello 2011 http://hdl.handle.net/11588/404502 https://doi.org/10.1002/iub.436 http://onlinelibrary.wiley.com/doi/10.1002/iub.436/abstract eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000288860900007 volume:63 issue:3 firstpage:175 lastpage:182 numberofpages:8 journal:IUBMB LIFE http://hdl.handle.net/11588/404502 doi:10.1002/iub.436 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-79953251135 http://onlinelibrary.wiley.com/doi/10.1002/iub.436/abstract * Trematomus bernacchii * hemoglobin * implicit ligand sampling * molecular dynamics simulations * pH * oxygen binding info:eu-repo/semantics/article 2011 ftunivnapoliiris https://doi.org/10.1002/iub.436 2024-06-17T15:19:26Z The Root effect describes the drastic drop of oxygen affinity and loss of cooperativity at acidic pH expressed in the hemoglobins (Hb) of certain fish. The comparison between the deoxy structures of the Root effect Hb from the Antarctic fish Trematomus bernacchii (HbTb) at different pHs (pH = 6.2 and pH = 8.4) shows that the most significant differences are localized at the CDα region, where a salt bridge between Asp48 and His55 breaks during the low-to-high pH transition. In order to shed light on the relationship between pH, CDα loop structure and dynamics, and oxygen access to the active site in the alpha chain of HbTb, different computer simulation techniques were performed. Our results highlight the importance of the protonation of His55 in regulating oxygen access, underscoring its pivotal role in the structural and functional properties of HbTb. These data provide further support to the hypothesis that this residue might contribute to the release of Root protons in HbTb and underline the fact that an efficient transport of molecular oxygen in Hbs relies on a subtle balance of tertiary structure and protein conformational flexibility. Article in Journal/Newspaper Antarc* Antarctic IRIS Università degli Studi di Napoli Federico II Antarctic The Antarctic IUBMB Life 63 3 175 182 |
institution |
Open Polar |
collection |
IRIS Università degli Studi di Napoli Federico II |
op_collection_id |
ftunivnapoliiris |
language |
English |
topic |
* Trematomus bernacchii * hemoglobin * implicit ligand sampling * molecular dynamics simulations * pH * oxygen binding |
spellingShingle |
* Trematomus bernacchii * hemoglobin * implicit ligand sampling * molecular dynamics simulations * pH * oxygen binding Boechi L. Martì M. A. Estrin D. A. VERGARA, ALESSANDRO SICA, FILOMENA MAZZARELLA, LELIO MERLINO, ANTONELLO Protonation of histidine 55 affects the oxygen access to heme in the alpha chain of the hemoglobin from the Antarctic fish Trematomus bernacchii. |
topic_facet |
* Trematomus bernacchii * hemoglobin * implicit ligand sampling * molecular dynamics simulations * pH * oxygen binding |
description |
The Root effect describes the drastic drop of oxygen affinity and loss of cooperativity at acidic pH expressed in the hemoglobins (Hb) of certain fish. The comparison between the deoxy structures of the Root effect Hb from the Antarctic fish Trematomus bernacchii (HbTb) at different pHs (pH = 6.2 and pH = 8.4) shows that the most significant differences are localized at the CDα region, where a salt bridge between Asp48 and His55 breaks during the low-to-high pH transition. In order to shed light on the relationship between pH, CDα loop structure and dynamics, and oxygen access to the active site in the alpha chain of HbTb, different computer simulation techniques were performed. Our results highlight the importance of the protonation of His55 in regulating oxygen access, underscoring its pivotal role in the structural and functional properties of HbTb. These data provide further support to the hypothesis that this residue might contribute to the release of Root protons in HbTb and underline the fact that an efficient transport of molecular oxygen in Hbs relies on a subtle balance of tertiary structure and protein conformational flexibility. |
author2 |
Boechi, L. Martì, M. A. Vergara, Alessandro Sica, Filomena Mazzarella, Lelio Estrin, D. A. Merlino, Antonello |
format |
Article in Journal/Newspaper |
author |
Boechi L. Martì M. A. Estrin D. A. VERGARA, ALESSANDRO SICA, FILOMENA MAZZARELLA, LELIO MERLINO, ANTONELLO |
author_facet |
Boechi L. Martì M. A. Estrin D. A. VERGARA, ALESSANDRO SICA, FILOMENA MAZZARELLA, LELIO MERLINO, ANTONELLO |
author_sort |
Boechi L. |
title |
Protonation of histidine 55 affects the oxygen access to heme in the alpha chain of the hemoglobin from the Antarctic fish Trematomus bernacchii. |
title_short |
Protonation of histidine 55 affects the oxygen access to heme in the alpha chain of the hemoglobin from the Antarctic fish Trematomus bernacchii. |
title_full |
Protonation of histidine 55 affects the oxygen access to heme in the alpha chain of the hemoglobin from the Antarctic fish Trematomus bernacchii. |
title_fullStr |
Protonation of histidine 55 affects the oxygen access to heme in the alpha chain of the hemoglobin from the Antarctic fish Trematomus bernacchii. |
title_full_unstemmed |
Protonation of histidine 55 affects the oxygen access to heme in the alpha chain of the hemoglobin from the Antarctic fish Trematomus bernacchii. |
title_sort |
protonation of histidine 55 affects the oxygen access to heme in the alpha chain of the hemoglobin from the antarctic fish trematomus bernacchii. |
publishDate |
2011 |
url |
http://hdl.handle.net/11588/404502 https://doi.org/10.1002/iub.436 http://onlinelibrary.wiley.com/doi/10.1002/iub.436/abstract |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000288860900007 volume:63 issue:3 firstpage:175 lastpage:182 numberofpages:8 journal:IUBMB LIFE http://hdl.handle.net/11588/404502 doi:10.1002/iub.436 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-79953251135 http://onlinelibrary.wiley.com/doi/10.1002/iub.436/abstract |
op_doi |
https://doi.org/10.1002/iub.436 |
container_title |
IUBMB Life |
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63 |
container_issue |
3 |
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175 |
op_container_end_page |
182 |
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1809822549763162112 |