Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins
Abstract Recent studies have demonstrated that hemoglobins isolated from Antarctic fish undergo peculiar oxidation processes. Here we show, by combining crystallographic and spectroscopic data, that the oxidation pathway of Trematomus bernacchii hemoglobin (HbTb) is distinct from that observed for t...
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crwiley:10.1002/bip.21206 2024-06-02T07:58:21+00:00 Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins Merlino, Antonello Vitagliano, Luigi Howes, Barry D. Verde, Cinzia di Prisco, Guido Smulevich, Giulietta Sica, Filomena Vergara, Alessandro 2009 http://dx.doi.org/10.1002/bip.21206 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.21206 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.21206 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biopolymers volume 91, issue 12, page 1117-1125 ISSN 0006-3525 1097-0282 journal-article 2009 crwiley https://doi.org/10.1002/bip.21206 2024-05-03T10:41:39Z Abstract Recent studies have demonstrated that hemoglobins isolated from Antarctic fish undergo peculiar oxidation processes. Here we show, by combining crystallographic and spectroscopic data, that the oxidation pathway of Trematomus bernacchii hemoglobin (HbTb) is distinct from that observed for the major component of Trematomus newnesi (Hb1Tn), despite the high sequence identity of the two proteins and structural similarity of their ferrous and fully oxidized states. Resonance Raman analysis of HbTb autoxidation upon air‐exposure reveals the absence of the oxidized pentacoordinated state that was observed for Hb1Tn. The HbTb oxidation pathway is characterized by two ferric species: an aquo hexacoordinated high spin state and a bis‐histidyl hexacoordinated low spin form, which appear in the early stages of the oxidation process. The high resolution structure of an intermediate along the oxidation pathway has been determined at 1.4 Å resolution. The analysis of the electron density of the heme pocket shows, for both the α and the β iron, the coexistence of multiple binding states. In this partially oxidized form, HbTb exhibits significant deviations from the canonical R state both at the local and global level. The analysis of these modifications highlights the structural correlation between key functional regions of the protein. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 1117–1125, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library Antarctic Biopolymers 91 12 1117 1125 |
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Wiley Online Library |
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English |
description |
Abstract Recent studies have demonstrated that hemoglobins isolated from Antarctic fish undergo peculiar oxidation processes. Here we show, by combining crystallographic and spectroscopic data, that the oxidation pathway of Trematomus bernacchii hemoglobin (HbTb) is distinct from that observed for the major component of Trematomus newnesi (Hb1Tn), despite the high sequence identity of the two proteins and structural similarity of their ferrous and fully oxidized states. Resonance Raman analysis of HbTb autoxidation upon air‐exposure reveals the absence of the oxidized pentacoordinated state that was observed for Hb1Tn. The HbTb oxidation pathway is characterized by two ferric species: an aquo hexacoordinated high spin state and a bis‐histidyl hexacoordinated low spin form, which appear in the early stages of the oxidation process. The high resolution structure of an intermediate along the oxidation pathway has been determined at 1.4 Å resolution. The analysis of the electron density of the heme pocket shows, for both the α and the β iron, the coexistence of multiple binding states. In this partially oxidized form, HbTb exhibits significant deviations from the canonical R state both at the local and global level. The analysis of these modifications highlights the structural correlation between key functional regions of the protein. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 1117–1125, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com |
format |
Article in Journal/Newspaper |
author |
Merlino, Antonello Vitagliano, Luigi Howes, Barry D. Verde, Cinzia di Prisco, Guido Smulevich, Giulietta Sica, Filomena Vergara, Alessandro |
spellingShingle |
Merlino, Antonello Vitagliano, Luigi Howes, Barry D. Verde, Cinzia di Prisco, Guido Smulevich, Giulietta Sica, Filomena Vergara, Alessandro Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins |
author_facet |
Merlino, Antonello Vitagliano, Luigi Howes, Barry D. Verde, Cinzia di Prisco, Guido Smulevich, Giulietta Sica, Filomena Vergara, Alessandro |
author_sort |
Merlino, Antonello |
title |
Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins |
title_short |
Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins |
title_full |
Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins |
title_fullStr |
Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins |
title_full_unstemmed |
Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins |
title_sort |
combined crystallographic and spectroscopic analysis of trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of antarctic fish hemoglobins |
publisher |
Wiley |
publishDate |
2009 |
url |
http://dx.doi.org/10.1002/bip.21206 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.21206 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.21206 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Biopolymers volume 91, issue 12, page 1117-1125 ISSN 0006-3525 1097-0282 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/bip.21206 |
container_title |
Biopolymers |
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91 |
container_issue |
12 |
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1117 |
op_container_end_page |
1125 |
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1800741665545125888 |