Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes
The suborder Notothenioidei dominates the Antarctic ichthyofauna. The non-Antarctic monotypic family Pseudaphritidae is one of the most primitive families. The characterization of the oxygen-transport system of euryhaline Pseudaphritis urvillii is herewith reported. Similar to most Antarctic notothe...
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fthighwire:oai:open-archive.highwire.org:protsci:ps.04861504v1 2023-05-15T13:59:10+02:00 Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes Verde, Cinzia Howes, Barry D. De Rosa, M. Cristina Raiola, Luca Smulevich, Giulietta Williams, Richard Giardina, Bruno Parisi, Elio Di Prisco, Guido 2004-08-31 10:47:35.0 text/html http://www.proteinscience.org/cgi/content/short/ps.04861504v1 https://doi.org/10.1110/ps.04861504 en eng Cold Spring Harbor Laboratory Press http://www.proteinscience.org/cgi/content/short/ps.04861504v1 http://dx.doi.org/10.1110/ps.04861504 Copyright (C) 2004, Cold Spring Harbor Laboratory Press ARTICLES TEXT 2004 fthighwire https://doi.org/10.1110/ps.04861504 2007-06-25T04:05:14Z The suborder Notothenioidei dominates the Antarctic ichthyofauna. The non-Antarctic monotypic family Pseudaphritidae is one of the most primitive families. The characterization of the oxygen-transport system of euryhaline Pseudaphritis urvillii is herewith reported. Similar to most Antarctic notothenioids, this temperate species has a single major hemoglobin (Hb 1, over 95% of the total). Hb 1 has strong Bohr and Root effects. It shows two very uncommon features in oxygen binding: At high pH values, the oxygen affinity is exceptionally high compared to other notothenioids, and subunit cooperativity is modulated by pH in an unusual way, namely the curve of the Hill coefficient is bell-shaped, with values approaching 1 at both extremes of pH. Molecular modeling, electronic absorption and resonance Raman spectra have been used to characterize the heme environment of Hb 1 in an attempt to explain these features, particularly in view of some potentially important nonconservative replacements found in the primary structure. Compared to human HbA, no major changes were found in the structure of the proximal cavity of the α-chain of Hb 1, although an altered distal histidyl and heme position was identified in the models of the β-chain, possibly facilitated by a more open heme pocket due to reduced steric constraints on the vinyl substituent groups. This conformation may lead to the hemichrome form identified by spectroscopy in the Met state, which likely fulfils a potentially important physiological role. Text Antarc* Antarctic HighWire Press (Stanford University) Antarctic The Antarctic Protein Science 13 10 2766 2781 |
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English |
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ARTICLES Verde, Cinzia Howes, Barry D. De Rosa, M. Cristina Raiola, Luca Smulevich, Giulietta Williams, Richard Giardina, Bruno Parisi, Elio Di Prisco, Guido Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes |
topic_facet |
ARTICLES |
description |
The suborder Notothenioidei dominates the Antarctic ichthyofauna. The non-Antarctic monotypic family Pseudaphritidae is one of the most primitive families. The characterization of the oxygen-transport system of euryhaline Pseudaphritis urvillii is herewith reported. Similar to most Antarctic notothenioids, this temperate species has a single major hemoglobin (Hb 1, over 95% of the total). Hb 1 has strong Bohr and Root effects. It shows two very uncommon features in oxygen binding: At high pH values, the oxygen affinity is exceptionally high compared to other notothenioids, and subunit cooperativity is modulated by pH in an unusual way, namely the curve of the Hill coefficient is bell-shaped, with values approaching 1 at both extremes of pH. Molecular modeling, electronic absorption and resonance Raman spectra have been used to characterize the heme environment of Hb 1 in an attempt to explain these features, particularly in view of some potentially important nonconservative replacements found in the primary structure. Compared to human HbA, no major changes were found in the structure of the proximal cavity of the α-chain of Hb 1, although an altered distal histidyl and heme position was identified in the models of the β-chain, possibly facilitated by a more open heme pocket due to reduced steric constraints on the vinyl substituent groups. This conformation may lead to the hemichrome form identified by spectroscopy in the Met state, which likely fulfils a potentially important physiological role. |
format |
Text |
author |
Verde, Cinzia Howes, Barry D. De Rosa, M. Cristina Raiola, Luca Smulevich, Giulietta Williams, Richard Giardina, Bruno Parisi, Elio Di Prisco, Guido |
author_facet |
Verde, Cinzia Howes, Barry D. De Rosa, M. Cristina Raiola, Luca Smulevich, Giulietta Williams, Richard Giardina, Bruno Parisi, Elio Di Prisco, Guido |
author_sort |
Verde, Cinzia |
title |
Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes |
title_short |
Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes |
title_full |
Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes |
title_fullStr |
Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes |
title_full_unstemmed |
Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes |
title_sort |
structure and function of the gondwanian hemoglobin of pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes |
publisher |
Cold Spring Harbor Laboratory Press |
publishDate |
2004 |
url |
http://www.proteinscience.org/cgi/content/short/ps.04861504v1 https://doi.org/10.1110/ps.04861504 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
http://www.proteinscience.org/cgi/content/short/ps.04861504v1 http://dx.doi.org/10.1110/ps.04861504 |
op_rights |
Copyright (C) 2004, Cold Spring Harbor Laboratory Press |
op_doi |
https://doi.org/10.1110/ps.04861504 |
container_title |
Protein Science |
container_volume |
13 |
container_issue |
10 |
container_start_page |
2766 |
op_container_end_page |
2781 |
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1766267611990982656 |