Role of tertiary structures on the Root effect in fish hemoglobins
Many fish hemoglobins exhibit a marked dependence of oxygen affinity and cooperativity on proton concentration, called Root effect. Both tertiary and quaternary effects have been evoked to explain the allosteric regulation brought about by protons in fish hemoglobins. However, no general rules have...
Published in: | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics |
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Online Access: | http://hdl.handle.net/11381/2633257 https://doi.org/10.1016/j.bbapap.2013.01.031 |
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ftunivparmairis:oai:air.unipr.it:11381/2633257 2024-04-14T08:04:04+00:00 Role of tertiary structures on the Root effect in fish hemoglobins RONDA, Luca BETTATI, Stefano MOZZARELLI, Andrea Antonello Merlino Cinzia Verde Anna Balsamo Lelio Mazzarella Alessandro Vergara Ronda, Luca Antonello, Merlino Bettati, Stefano Cinzia, Verde Anna, Balsamo Lelio, Mazzarella Mozzarelli, Andrea Alessandro, Vergara 2013 http://hdl.handle.net/11381/2633257 https://doi.org/10.1016/j.bbapap.2013.01.031 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000323191800023 volume:1834 issue:9 firstpage:1885 lastpage:1893 numberofpages:9 journal:BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS http://hdl.handle.net/11381/2633257 doi:10.1016/j.bbapap.2013.01.031 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84884606189 Hemoglobin Root effect X-ray crystallography Oxygen binding Microspectrophotometry info:eu-repo/semantics/article 2013 ftunivparmairis https://doi.org/10.1016/j.bbapap.2013.01.031 2024-03-21T18:35:56Z Many fish hemoglobins exhibit a marked dependence of oxygen affinity and cooperativity on proton concentration, called Root effect. Both tertiary and quaternary effects have been evoked to explain the allosteric regulation brought about by protons in fish hemoglobins. However, no general rules have emerged so far. We carried out a complementary crystallographic and microspectroscopic characterization of ligand binding to crystals of deoxy-hemoglobin from the Antarctic fish Trematomus bernacchii (HbTb) at pH 6.2 and pH 8.4. At low pH ligation has negligible structural effects, correlating with low affinity and absence of cooperativity in oxygen binding. At high pH, ligation causes significant changes at the tertiary structural level, while preserving structural markers of the T state. These changes mainly consist in a marked displacement of the position of the switch region CD corner towards an R-like position. The functional data on T-state crystals validate the relevance of the crystallographic observations, revealing that, differently from mammalian Hbs, in HbTb a significant degree of cooperativity in oxygen binding is due to tertiary conformational changes, in the absence of the T–R quaternary transition. Article in Journal/Newspaper Antarc* Antarctic Archivio della ricerca dell'Università di Parma (CINECA IRIS) Antarctic The Antarctic Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1834 9 1885 1893 |
institution |
Open Polar |
collection |
Archivio della ricerca dell'Università di Parma (CINECA IRIS) |
op_collection_id |
ftunivparmairis |
language |
English |
topic |
Hemoglobin Root effect X-ray crystallography Oxygen binding Microspectrophotometry |
spellingShingle |
Hemoglobin Root effect X-ray crystallography Oxygen binding Microspectrophotometry RONDA, Luca BETTATI, Stefano MOZZARELLI, Andrea Antonello Merlino Cinzia Verde Anna Balsamo Lelio Mazzarella Alessandro Vergara Role of tertiary structures on the Root effect in fish hemoglobins |
topic_facet |
Hemoglobin Root effect X-ray crystallography Oxygen binding Microspectrophotometry |
description |
Many fish hemoglobins exhibit a marked dependence of oxygen affinity and cooperativity on proton concentration, called Root effect. Both tertiary and quaternary effects have been evoked to explain the allosteric regulation brought about by protons in fish hemoglobins. However, no general rules have emerged so far. We carried out a complementary crystallographic and microspectroscopic characterization of ligand binding to crystals of deoxy-hemoglobin from the Antarctic fish Trematomus bernacchii (HbTb) at pH 6.2 and pH 8.4. At low pH ligation has negligible structural effects, correlating with low affinity and absence of cooperativity in oxygen binding. At high pH, ligation causes significant changes at the tertiary structural level, while preserving structural markers of the T state. These changes mainly consist in a marked displacement of the position of the switch region CD corner towards an R-like position. The functional data on T-state crystals validate the relevance of the crystallographic observations, revealing that, differently from mammalian Hbs, in HbTb a significant degree of cooperativity in oxygen binding is due to tertiary conformational changes, in the absence of the T–R quaternary transition. |
author2 |
Ronda, Luca Antonello, Merlino Bettati, Stefano Cinzia, Verde Anna, Balsamo Lelio, Mazzarella Mozzarelli, Andrea Alessandro, Vergara |
format |
Article in Journal/Newspaper |
author |
RONDA, Luca BETTATI, Stefano MOZZARELLI, Andrea Antonello Merlino Cinzia Verde Anna Balsamo Lelio Mazzarella Alessandro Vergara |
author_facet |
RONDA, Luca BETTATI, Stefano MOZZARELLI, Andrea Antonello Merlino Cinzia Verde Anna Balsamo Lelio Mazzarella Alessandro Vergara |
author_sort |
RONDA, Luca |
title |
Role of tertiary structures on the Root effect in fish hemoglobins |
title_short |
Role of tertiary structures on the Root effect in fish hemoglobins |
title_full |
Role of tertiary structures on the Root effect in fish hemoglobins |
title_fullStr |
Role of tertiary structures on the Root effect in fish hemoglobins |
title_full_unstemmed |
Role of tertiary structures on the Root effect in fish hemoglobins |
title_sort |
role of tertiary structures on the root effect in fish hemoglobins |
publishDate |
2013 |
url |
http://hdl.handle.net/11381/2633257 https://doi.org/10.1016/j.bbapap.2013.01.031 |
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:000323191800023 volume:1834 issue:9 firstpage:1885 lastpage:1893 numberofpages:9 journal:BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS http://hdl.handle.net/11381/2633257 doi:10.1016/j.bbapap.2013.01.031 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84884606189 |
op_doi |
https://doi.org/10.1016/j.bbapap.2013.01.031 |
container_title |
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics |
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1834 |
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9 |
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1885 |
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