Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins
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...
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Online Access: | http://hdl.handle.net/11588/351617 https://doi.org/10.1002/bip.21206 |
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ftunivnapoliiris:oai:www.iris.unina.it:11588/351617 2024-09-09T19:06:59+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 SICA, FILOMENA VERGARA, ALESSANDRO L. Vitagliano B. Howes C. Verde G. di Prisco G. Smulevich Merlino, Antonello L., Vitagliano B., Howe C., Verde G., di Prisco G., Smulevich Sica, Filomena Vergara, Alessandro 2009 ELETTRONICO http://hdl.handle.net/11588/351617 https://doi.org/10.1002/bip.21206 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000270961600015 volume:91 issue:12 firstpage:1117 lastpage:1125 numberofpages:9 journal:BIOPOLYMERS http://hdl.handle.net/11588/351617 doi:10.1002/bip.21206 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-71749103092 Raman crystallography hemoglobin info:eu-repo/semantics/article 2009 ftunivnapoliiris https://doi.org/10.1002/bip.21206 2024-06-17T15:19:25Z 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. Article in Journal/Newspaper Antarc* Antarctic IRIS Università degli Studi di Napoli Federico II Antarctic Biopolymers 91 12 1117 1125 |
institution |
Open Polar |
collection |
IRIS Università degli Studi di Napoli Federico II |
op_collection_id |
ftunivnapoliiris |
language |
English |
topic |
Raman crystallography hemoglobin |
spellingShingle |
Raman crystallography hemoglobin MERLINO, ANTONELLO SICA, FILOMENA VERGARA, ALESSANDRO L. Vitagliano B. Howes C. Verde G. di Prisco G. Smulevich Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins |
topic_facet |
Raman crystallography hemoglobin |
description |
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. |
author2 |
Merlino, Antonello L., Vitagliano B., Howe C., Verde G., di Prisco G., Smulevich Sica, Filomena Vergara, Alessandro |
format |
Article in Journal/Newspaper |
author |
MERLINO, ANTONELLO SICA, FILOMENA VERGARA, ALESSANDRO L. Vitagliano B. Howes C. Verde G. di Prisco G. Smulevich |
author_facet |
MERLINO, ANTONELLO SICA, FILOMENA VERGARA, ALESSANDRO L. Vitagliano B. Howes C. Verde G. di Prisco G. Smulevich |
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 |
publishDate |
2009 |
url |
http://hdl.handle.net/11588/351617 https://doi.org/10.1002/bip.21206 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000270961600015 volume:91 issue:12 firstpage:1117 lastpage:1125 numberofpages:9 journal:BIOPOLYMERS http://hdl.handle.net/11588/351617 doi:10.1002/bip.21206 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-71749103092 |
op_doi |
https://doi.org/10.1002/bip.21206 |
container_title |
Biopolymers |
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91 |
container_issue |
12 |
container_start_page |
1117 |
op_container_end_page |
1125 |
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1809821033005318144 |