Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes
Abstract 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 Antarcti...
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crwiley:10.1110/ps.04861504 2024-06-02T07:57:16+00:00 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 http://dx.doi.org/10.1110/ps.04861504 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.04861504 https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.04861504 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Protein Science volume 13, issue 10, page 2766-2781 ISSN 0961-8368 1469-896X journal-article 2004 crwiley https://doi.org/10.1110/ps.04861504 2024-05-03T12:06:15Z Abstract 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. Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library Antarctic The Antarctic Protein Science 13 10 2766 2781 |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Abstract 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 |
Article in Journal/Newspaper |
author |
Verde, Cinzia Howes, Barry D. De Rosa, M. Cristina Raiola, Luca Smulevich, Giulietta Williams, Richard Giardina, Bruno Parisi, Elio Di Prisco, Guido |
spellingShingle |
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 |
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 |
Wiley |
publishDate |
2004 |
url |
http://dx.doi.org/10.1110/ps.04861504 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.04861504 https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.04861504 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Protein Science volume 13, issue 10, page 2766-2781 ISSN 0961-8368 1469-896X |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
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 |
_version_ |
1800740397172916224 |