Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins
Oxidation of Hbs leads to the formation of different forms of Fe(III) that are relevant to a range of biochemical and physiological functions. Here we report a combined EPR/x-ray crystallography study performed at acidic pH on six ferric tetrameric Hbs. Five of the Hbs were isolated from the high-An...
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ftpubmed:oai:pubmedcentral.nih.gov:2718161 2023-05-15T13:51:25+02:00 Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins Vergara, Alessandro Franzese, Marisa Merlino, Antonello Bonomi, Giovanna Verde, Cinzia Giordano, Daniela di Prisco, Guido Lee, H. Caroline Peisach, Jack Mazzarella, Lelio 2009-08-05 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2718161 http://www.ncbi.nlm.nih.gov/pubmed/19651045 https://doi.org/10.1016/j.bpj.2009.04.056 en eng The Biophysical Society http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2718161 http://www.ncbi.nlm.nih.gov/pubmed/19651045 http://dx.doi.org/10.1016/j.bpj.2009.04.056 © 2009 by the Biophysical Society. This document may be redistributed and reused, subject to certain conditions (http://www.elsevier.com/wps/find/authorsview.authors/supplementalterms1.0) . Protein Text 2009 ftpubmed https://doi.org/10.1016/j.bpj.2009.04.056 2013-09-02T15:12:56Z Oxidation of Hbs leads to the formation of different forms of Fe(III) that are relevant to a range of biochemical and physiological functions. Here we report a combined EPR/x-ray crystallography study performed at acidic pH on six ferric tetrameric Hbs. Five of the Hbs were isolated from the high-Antarctic notothenioid fishes Trematomus bernacchii, Trematomus newnesi, and Gymnodraco acuticeps, and one was isolated from the sub-Antarctic notothenioid Cottoperca gobio. Our EPR analysis reveals that 1), in all of these Hbs, at acidic pH the aquomet form and two hemichromes coexist; and 2), only in the three Hbs that exhibit the Root effect is a significant amount of the pentacoordinate (5C) high-spin Fe(III) form found. The crystal structure at acidic pH of the ferric form of the Root-effect Hb from T. bernacchii is also reported at 1.7 Å resolution. This structure reveals a 5C state of the heme iron for both the α- and β-chains within a T quaternary structure. Altogether, the spectroscopic and crystallographic results indicate that the Root effect and hemichrome stability at acidic pH are correlated in tetrameric Hbs. Furthermore, Antarctic fish Hbs exhibit higher peroxidase activity than mammalian and temperate fish Hbs, suggesting that a partial hemichrome state in tetrameric Hbs, unlike in monomeric Hbs, does not remove the need for protection from peroxide attack, in contrast to previous results from monomeric Hbs. Text Antarc* Antarctic PubMed Central (PMC) Antarctic Biophysical Journal 97 3 866 874 |
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Protein Vergara, Alessandro Franzese, Marisa Merlino, Antonello Bonomi, Giovanna Verde, Cinzia Giordano, Daniela di Prisco, Guido Lee, H. Caroline Peisach, Jack Mazzarella, Lelio Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins |
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Oxidation of Hbs leads to the formation of different forms of Fe(III) that are relevant to a range of biochemical and physiological functions. Here we report a combined EPR/x-ray crystallography study performed at acidic pH on six ferric tetrameric Hbs. Five of the Hbs were isolated from the high-Antarctic notothenioid fishes Trematomus bernacchii, Trematomus newnesi, and Gymnodraco acuticeps, and one was isolated from the sub-Antarctic notothenioid Cottoperca gobio. Our EPR analysis reveals that 1), in all of these Hbs, at acidic pH the aquomet form and two hemichromes coexist; and 2), only in the three Hbs that exhibit the Root effect is a significant amount of the pentacoordinate (5C) high-spin Fe(III) form found. The crystal structure at acidic pH of the ferric form of the Root-effect Hb from T. bernacchii is also reported at 1.7 Å resolution. This structure reveals a 5C state of the heme iron for both the α- and β-chains within a T quaternary structure. Altogether, the spectroscopic and crystallographic results indicate that the Root effect and hemichrome stability at acidic pH are correlated in tetrameric Hbs. Furthermore, Antarctic fish Hbs exhibit higher peroxidase activity than mammalian and temperate fish Hbs, suggesting that a partial hemichrome state in tetrameric Hbs, unlike in monomeric Hbs, does not remove the need for protection from peroxide attack, in contrast to previous results from monomeric Hbs. |
format |
Text |
author |
Vergara, Alessandro Franzese, Marisa Merlino, Antonello Bonomi, Giovanna Verde, Cinzia Giordano, Daniela di Prisco, Guido Lee, H. Caroline Peisach, Jack Mazzarella, Lelio |
author_facet |
Vergara, Alessandro Franzese, Marisa Merlino, Antonello Bonomi, Giovanna Verde, Cinzia Giordano, Daniela di Prisco, Guido Lee, H. Caroline Peisach, Jack Mazzarella, Lelio |
author_sort |
Vergara, Alessandro |
title |
Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins |
title_short |
Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins |
title_full |
Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins |
title_fullStr |
Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins |
title_full_unstemmed |
Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins |
title_sort |
correlation between hemichrome stability and the root effect in tetrameric hemoglobins |
publisher |
The Biophysical Society |
publishDate |
2009 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2718161 http://www.ncbi.nlm.nih.gov/pubmed/19651045 https://doi.org/10.1016/j.bpj.2009.04.056 |
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Antarctic |
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Antarctic |
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Antarc* Antarctic |
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Antarc* Antarctic |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2718161 http://www.ncbi.nlm.nih.gov/pubmed/19651045 http://dx.doi.org/10.1016/j.bpj.2009.04.056 |
op_rights |
© 2009 by the Biophysical Society. This document may be redistributed and reused, subject to certain conditions (http://www.elsevier.com/wps/find/authorsview.authors/supplementalterms1.0) . |
op_doi |
https://doi.org/10.1016/j.bpj.2009.04.056 |
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Biophysical Journal |
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97 |
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3 |
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866 |
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874 |
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1766255295823085568 |