Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state
Tetrameric hemoglobins represent the most commonly used model for the description of the basic concepts of protein allostery. The classical stereochemical model assumes a concerted transition of the protein, upon oxygen release, from the relaxed (R) to the tense (T) state. Despite the large amount o...
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Online Access: | http://hdl.handle.net/11588/305204 https://doi.org/10.1021/ja803363p |
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ftunivnapoliiris:oai:www.iris.unina.it:11588/305204 2024-09-09T19:03:53+00:00 Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state L. Vitagliano G. Smulevich B. Howes G. di Prisco C. Verde VERGARA, ALESSANDRO BONOMI, GIOVANNA MERLINO, ANTONELLO MAZZARELLA, LELIO L., Vitagliano Vergara, Alessandro Bonomi, Giovanna Merlino, Antonello G., Smulevich B., Howe G., di Prisco C., Verde Mazzarella, Lelio 2008 STAMPA http://hdl.handle.net/11588/305204 https://doi.org/10.1021/ja803363p eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000258293800037 volume:130 issue:32 firstpage:10527 lastpage:10535 numberofpages:9 journal:JOURNAL OF THE AMERICAN CHEMICAL SOCIETY http://hdl.handle.net/11588/305204 doi:10.1021/ja803363p info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-49449107745 info:eu-repo/semantics/article 2008 ftunivnapoliiris https://doi.org/10.1021/ja803363p 2024-06-17T15:19:24Z Tetrameric hemoglobins represent the most commonly used model for the description of the basic concepts of protein allostery. The classical stereochemical model assumes a concerted transition of the protein, upon oxygen release, from the relaxed (R) to the tense (T) state. Despite the large amount of data accumulated on the end-points of the transition, scarce structural information is available on the intermediate species along the pathway. Here we report a spectroscopic characterization of the autoxidation process of the Trematomus newnesi major Hb component and the atomic resolution structure (1.25 Å) of an intermediate form along the pathway characterized by a different binding and oxidation state of the R and chains. In contrast to the R-heme iron, which binds a CO molecule, the iron displays a pentacoordinated oxidized state, which is rare in tetrameric hemoglobins. Interestingly, the information provided by the present analysis is not limited to the characterization of the peculiar oxidation process of Antarctic fish hemoglobins. Indeed, this structure represents the most detailed snapshot of hemoglobin allosteric transition hitherto achieved. Upon ligand release at the heme, a cascade of structural events is observed. Notably, several structural features of the tertiary structure of the R and chains closely resemble those typically observed in the deoxygenated state. The overall quaternary structure also becomes intermediate between the R and the T state. The analysis of the alterations induced by the ligand release provides a clear picture of the temporal sequence of the events associated with the transition. The implications of the present findings have also been discussed in the wider context of tetrameric Hbs. Article in Journal/Newspaper Antarc* Antarctic IRIS Università degli Studi di Napoli Federico II Antarctic Journal of the American Chemical Society 130 32 10527 10535 |
institution |
Open Polar |
collection |
IRIS Università degli Studi di Napoli Federico II |
op_collection_id |
ftunivnapoliiris |
language |
English |
description |
Tetrameric hemoglobins represent the most commonly used model for the description of the basic concepts of protein allostery. The classical stereochemical model assumes a concerted transition of the protein, upon oxygen release, from the relaxed (R) to the tense (T) state. Despite the large amount of data accumulated on the end-points of the transition, scarce structural information is available on the intermediate species along the pathway. Here we report a spectroscopic characterization of the autoxidation process of the Trematomus newnesi major Hb component and the atomic resolution structure (1.25 Å) of an intermediate form along the pathway characterized by a different binding and oxidation state of the R and chains. In contrast to the R-heme iron, which binds a CO molecule, the iron displays a pentacoordinated oxidized state, which is rare in tetrameric hemoglobins. Interestingly, the information provided by the present analysis is not limited to the characterization of the peculiar oxidation process of Antarctic fish hemoglobins. Indeed, this structure represents the most detailed snapshot of hemoglobin allosteric transition hitherto achieved. Upon ligand release at the heme, a cascade of structural events is observed. Notably, several structural features of the tertiary structure of the R and chains closely resemble those typically observed in the deoxygenated state. The overall quaternary structure also becomes intermediate between the R and the T state. The analysis of the alterations induced by the ligand release provides a clear picture of the temporal sequence of the events associated with the transition. The implications of the present findings have also been discussed in the wider context of tetrameric Hbs. |
author2 |
L., Vitagliano Vergara, Alessandro Bonomi, Giovanna Merlino, Antonello G., Smulevich B., Howe G., di Prisco C., Verde Mazzarella, Lelio |
format |
Article in Journal/Newspaper |
author |
L. Vitagliano G. Smulevich B. Howes G. di Prisco C. Verde VERGARA, ALESSANDRO BONOMI, GIOVANNA MERLINO, ANTONELLO MAZZARELLA, LELIO |
spellingShingle |
L. Vitagliano G. Smulevich B. Howes G. di Prisco C. Verde VERGARA, ALESSANDRO BONOMI, GIOVANNA MERLINO, ANTONELLO MAZZARELLA, LELIO Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state |
author_facet |
L. Vitagliano G. Smulevich B. Howes G. di Prisco C. Verde VERGARA, ALESSANDRO BONOMI, GIOVANNA MERLINO, ANTONELLO MAZZARELLA, LELIO |
author_sort |
L. Vitagliano |
title |
Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state |
title_short |
Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state |
title_full |
Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state |
title_fullStr |
Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state |
title_full_unstemmed |
Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state |
title_sort |
spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state |
publishDate |
2008 |
url |
http://hdl.handle.net/11588/305204 https://doi.org/10.1021/ja803363p |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000258293800037 volume:130 issue:32 firstpage:10527 lastpage:10535 numberofpages:9 journal:JOURNAL OF THE AMERICAN CHEMICAL SOCIETY http://hdl.handle.net/11588/305204 doi:10.1021/ja803363p info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-49449107745 |
op_doi |
https://doi.org/10.1021/ja803363p |
container_title |
Journal of the American Chemical Society |
container_volume |
130 |
container_issue |
32 |
container_start_page |
10527 |
op_container_end_page |
10535 |
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1809817905550852096 |