Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue
A psychrophilic superoxide dismutase (SOD) has been characterized from the Antarctic eubacterium Pseudoalteromonas haloplanktis (Ph). PhSOD is a homodimeric iron-containing enzyme and displays a high specific activity, even at low temperature. The enzyme is inhibited by sodium azide and inactivated...
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ftuninapoliparth:oai:ricerca.uniparthenope.it:11367/26394 2024-04-21T07:48:14+00:00 Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue CASTELLANO, I. DI MARO, A. RUOCCO, M. R. CHAMBERY, A. PARENTE, A. DI MARTINO, M. T. PARLATO, G. MASULLO, M. DE VENDITTIS, E. Castellano, I. DI MARO, A. Ruocco, M. R. Chambery, A. Parente, A. DI MARTINO, M. T. Parlato, G. Masullo, M. DE VENDITTIS, E. 2006 http://hdl.handle.net/11367/26394 https://doi.org/10.1016/j.biochi.2006.04.005 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000242460000007 volume:88 firstpage:1377 lastpage:1389 numberofpages:13 journal:BIOCHIMIE http://hdl.handle.net/11367/26394 doi:10.1016/j.biochi.2006.04.005 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-33750505881 Superoxide dismutase Pseudoalteromonas haloplanktis Psychrophilic enzyme Covalent modification info:eu-repo/semantics/article 2006 ftuninapoliparth https://doi.org/10.1016/j.biochi.2006.04.005 2024-03-28T01:11:47Z A psychrophilic superoxide dismutase (SOD) has been characterized from the Antarctic eubacterium Pseudoalteromonas haloplanktis (Ph). PhSOD is a homodimeric iron-containing enzyme and displays a high specific activity, even at low temperature. The enzyme is inhibited by sodium azide and inactivated by hydrogen peroxide; it is also very sensitive to peroxynitrite, a physiological inactivator of the human mitochon- drial Mn-SOD. Even though PhSOD is isolated from a cold-adapted micro-organism, its heat stability is well above the maximum growth temperature of P. haloplanktis, a feature common to other Fe- and Mn-SODs. The primary structure of PhSOD was determined by a combination of mass spectrometry and automated Edman degradation. The polypeptide chain is made of 192 amino acid residues, corresponding to a mole- cular mass of 21251 Da. The alignment with other Fe- and Mn-SODs showed a high amino acid identity with Fe-SOD from Vibrio cholerae (79%) and Escherichia coli (70%). A significant similarity is also shared with human mitochondrial Mn-SOD. PhSOD has the unique and highly reactive Cys57 residue, located in a variable region of the protein. The three-dimensional model of the PhSOD monomer indicates that Cys57 is included in a region, whose structural organization apparently discriminates between dimeric and tetrameric SODs. This residue forms a disulfide adduct with β-mercaptoethanol, when this reducing agent is added in the purification procedure. The reactivity of Cys57 leads also to the for- mation of a disulfide bridge between two PhSOD subunits in specific denaturing conditions. The possible modification of Cys57 by physiolo- gical thiols, eventually regulating the PhSOD functioning, is discussed. Article in Journal/Newspaper Antarc* Antarctic Università degli Studi di Napoli "Parthenope": CINECA IRIS Biochimie 88 10 1377 1389 |
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Open Polar |
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Università degli Studi di Napoli "Parthenope": CINECA IRIS |
op_collection_id |
ftuninapoliparth |
language |
English |
topic |
Superoxide dismutase Pseudoalteromonas haloplanktis Psychrophilic enzyme Covalent modification |
spellingShingle |
Superoxide dismutase Pseudoalteromonas haloplanktis Psychrophilic enzyme Covalent modification CASTELLANO, I. DI MARO, A. RUOCCO, M. R. CHAMBERY, A. PARENTE, A. DI MARTINO, M. T. PARLATO, G. MASULLO, M. DE VENDITTIS, E. Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue |
topic_facet |
Superoxide dismutase Pseudoalteromonas haloplanktis Psychrophilic enzyme Covalent modification |
description |
A psychrophilic superoxide dismutase (SOD) has been characterized from the Antarctic eubacterium Pseudoalteromonas haloplanktis (Ph). PhSOD is a homodimeric iron-containing enzyme and displays a high specific activity, even at low temperature. The enzyme is inhibited by sodium azide and inactivated by hydrogen peroxide; it is also very sensitive to peroxynitrite, a physiological inactivator of the human mitochon- drial Mn-SOD. Even though PhSOD is isolated from a cold-adapted micro-organism, its heat stability is well above the maximum growth temperature of P. haloplanktis, a feature common to other Fe- and Mn-SODs. The primary structure of PhSOD was determined by a combination of mass spectrometry and automated Edman degradation. The polypeptide chain is made of 192 amino acid residues, corresponding to a mole- cular mass of 21251 Da. The alignment with other Fe- and Mn-SODs showed a high amino acid identity with Fe-SOD from Vibrio cholerae (79%) and Escherichia coli (70%). A significant similarity is also shared with human mitochondrial Mn-SOD. PhSOD has the unique and highly reactive Cys57 residue, located in a variable region of the protein. The three-dimensional model of the PhSOD monomer indicates that Cys57 is included in a region, whose structural organization apparently discriminates between dimeric and tetrameric SODs. This residue forms a disulfide adduct with β-mercaptoethanol, when this reducing agent is added in the purification procedure. The reactivity of Cys57 leads also to the for- mation of a disulfide bridge between two PhSOD subunits in specific denaturing conditions. The possible modification of Cys57 by physiolo- gical thiols, eventually regulating the PhSOD functioning, is discussed. |
author2 |
Castellano, I. DI MARO, A. Ruocco, M. R. Chambery, A. Parente, A. DI MARTINO, M. T. Parlato, G. Masullo, M. DE VENDITTIS, E. |
format |
Article in Journal/Newspaper |
author |
CASTELLANO, I. DI MARO, A. RUOCCO, M. R. CHAMBERY, A. PARENTE, A. DI MARTINO, M. T. PARLATO, G. MASULLO, M. DE VENDITTIS, E. |
author_facet |
CASTELLANO, I. DI MARO, A. RUOCCO, M. R. CHAMBERY, A. PARENTE, A. DI MARTINO, M. T. PARLATO, G. MASULLO, M. DE VENDITTIS, E. |
author_sort |
CASTELLANO, I. |
title |
Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue |
title_short |
Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue |
title_full |
Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue |
title_fullStr |
Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue |
title_full_unstemmed |
Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue |
title_sort |
psychrophilic superoxide dismutase from pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue |
publishDate |
2006 |
url |
http://hdl.handle.net/11367/26394 https://doi.org/10.1016/j.biochi.2006.04.005 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000242460000007 volume:88 firstpage:1377 lastpage:1389 numberofpages:13 journal:BIOCHIMIE http://hdl.handle.net/11367/26394 doi:10.1016/j.biochi.2006.04.005 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-33750505881 |
op_doi |
https://doi.org/10.1016/j.biochi.2006.04.005 |
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Biochimie |
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88 |
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10 |
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1377 |
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1389 |
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1796948529621499904 |