Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis
The myoglobin of the polychaete annelid Ophelia bicornis was isolated, purified to homogeneity and characterized. The primary structure, obtained from cDNA and protein sequencing, consists of 139 amino acid residues. The alignment with other globin sequences showed that O. bicornis myoglobin misses...
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Portland Press Ltd.
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crportlandpress:10.1042/bj20050267 2024-06-09T07:49:47+00:00 Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis Sanna, M. Teresa Manconi, Barbara Castagnola, Massimo Giardina, Bruno Masia, Daniela Messana, Irene Olianas, Alessandra Patamia, Maria Petruzzelli, Raffaele Pellegrini, Mariagiuseppina 2005 http://dx.doi.org/10.1042/bj20050267 https://portlandpress.com/biochemj/article-pdf/389/2/497/720625/bj3890497.pdf en eng Portland Press Ltd. Biochemical Journal volume 389, issue 2, page 497-505 ISSN 0264-6021 1470-8728 journal-article 2005 crportlandpress https://doi.org/10.1042/bj20050267 2024-05-16T14:10:30Z The myoglobin of the polychaete annelid Ophelia bicornis was isolated, purified to homogeneity and characterized. The primary structure, obtained from cDNA and protein sequencing, consists of 139 amino acid residues. The alignment with other globin sequences showed that O. bicornis myoglobin misses the pre-A helix and the first six residues of the A helix. The presence of a PheB10-GlnE7 haem distal residue pair is in agreement with the measured oxygen affinity (P50=0.85 mmHg; 1 mmHg=0.133 kPa) and the only slightly higher autoxidation rate constant (0.28 h−1) with respect to that of the sperm whale myoglobin mutant E7 His→Gln (0.21 h−1) and to elephant myoglobin (0.1 h−1). Oxygen-binding co-operativity was found to be absent under all the examined experimental conditions. The resistance of O. bicornis myoglobin towards autoxidation seems to confirm the important role of part of the A helix in the stability of the globin. The higher pKa of the acid–alkaline ferric transition of O. bicornis with respect to Asian elephant myoglobin, as well as the higher absorbance ratio of its ferric form to the oxy form measured in the Soret region (γmet/γoxy) with respect to that of the African elephant myoglobin, suggested a stronger interaction between the distal glutamine and the water molecule at the sixth co-ordinate position. Article in Journal/Newspaper Sperm whale Portland Press Biochemical Journal 389 2 497 505 |
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Portland Press |
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English |
description |
The myoglobin of the polychaete annelid Ophelia bicornis was isolated, purified to homogeneity and characterized. The primary structure, obtained from cDNA and protein sequencing, consists of 139 amino acid residues. The alignment with other globin sequences showed that O. bicornis myoglobin misses the pre-A helix and the first six residues of the A helix. The presence of a PheB10-GlnE7 haem distal residue pair is in agreement with the measured oxygen affinity (P50=0.85 mmHg; 1 mmHg=0.133 kPa) and the only slightly higher autoxidation rate constant (0.28 h−1) with respect to that of the sperm whale myoglobin mutant E7 His→Gln (0.21 h−1) and to elephant myoglobin (0.1 h−1). Oxygen-binding co-operativity was found to be absent under all the examined experimental conditions. The resistance of O. bicornis myoglobin towards autoxidation seems to confirm the important role of part of the A helix in the stability of the globin. The higher pKa of the acid–alkaline ferric transition of O. bicornis with respect to Asian elephant myoglobin, as well as the higher absorbance ratio of its ferric form to the oxy form measured in the Soret region (γmet/γoxy) with respect to that of the African elephant myoglobin, suggested a stronger interaction between the distal glutamine and the water molecule at the sixth co-ordinate position. |
format |
Article in Journal/Newspaper |
author |
Sanna, M. Teresa Manconi, Barbara Castagnola, Massimo Giardina, Bruno Masia, Daniela Messana, Irene Olianas, Alessandra Patamia, Maria Petruzzelli, Raffaele Pellegrini, Mariagiuseppina |
spellingShingle |
Sanna, M. Teresa Manconi, Barbara Castagnola, Massimo Giardina, Bruno Masia, Daniela Messana, Irene Olianas, Alessandra Patamia, Maria Petruzzelli, Raffaele Pellegrini, Mariagiuseppina Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis |
author_facet |
Sanna, M. Teresa Manconi, Barbara Castagnola, Massimo Giardina, Bruno Masia, Daniela Messana, Irene Olianas, Alessandra Patamia, Maria Petruzzelli, Raffaele Pellegrini, Mariagiuseppina |
author_sort |
Sanna, M. Teresa |
title |
Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis |
title_short |
Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis |
title_full |
Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis |
title_fullStr |
Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis |
title_full_unstemmed |
Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis |
title_sort |
functional and structural characterization of the myoglobin from the polychaete ophelia bicornis |
publisher |
Portland Press Ltd. |
publishDate |
2005 |
url |
http://dx.doi.org/10.1042/bj20050267 https://portlandpress.com/biochemj/article-pdf/389/2/497/720625/bj3890497.pdf |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Biochemical Journal volume 389, issue 2, page 497-505 ISSN 0264-6021 1470-8728 |
op_doi |
https://doi.org/10.1042/bj20050267 |
container_title |
Biochemical Journal |
container_volume |
389 |
container_issue |
2 |
container_start_page |
497 |
op_container_end_page |
505 |
_version_ |
1801382600056504320 |