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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ftunivnapoliiris:oai:www.iris.unina.it:11588/201587 2024-04-14T08:03:11+00:00 Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue CASTELLANO I DI MARO A CHAMBERY A PARENTE A DI MARTINO M. T PARLATO G MASULLO M RUOCCO, MARIA ROSARIA DE VENDITTIS, EMMANUELE Castellano, I DI MARO, A Ruocco, MARIA ROSARIA Chambery, A Parente, A DI MARTINO M., T Parlato, G Masullo, M DE VENDITTIS, Emmanuele 2006 STAMPA http://hdl.handle.net/11588/201587 https://doi.org/10.1016/j.biochi.2006.04.005 eng eng info:eu-repo/semantics/altIdentifier/pmid/16713057 volume:88 firstpage:1377 lastpage:1389 numberofpages:13 journal:BIOCHIMIE http://hdl.handle.net/11588/201587 doi:10.1016/j.biochi.2006.04.005 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-33750505881 info:eu-repo/semantics/closedAccess Superoxide dismutase Pseudoalteromonas haloplankti psychrophilic enzyme sulfhydryl reactivity covalent modification info:eu-repo/semantics/article 2006 ftunivnapoliiris https://doi.org/10.1016/j.biochi.2006.04.005 2024-03-21T18:56:34Z 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 mitochondrial 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 molecular 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 beta-mercaptoethanol, when this reducing agent is added in the purification procedure. The reactivity of Cys57 leads also to the formation of a disulfide bridge between two PhSOD subunits in specific denaturing conditions. The possible modification of Cys57 by physiological thiols, eventually regulating the PhSOD functioning, is discussed. Article in Journal/Newspaper Antarc* Antarctic IRIS Università degli Studi di Napoli Federico II Antarctic The Antarctic Biochimie 88 10 1377 1389 |
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Open Polar |
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IRIS Università degli Studi di Napoli Federico II |
op_collection_id |
ftunivnapoliiris |
language |
English |
topic |
Superoxide dismutase Pseudoalteromonas haloplankti psychrophilic enzyme sulfhydryl reactivity covalent modification |
spellingShingle |
Superoxide dismutase Pseudoalteromonas haloplankti psychrophilic enzyme sulfhydryl reactivity covalent modification CASTELLANO I DI MARO A CHAMBERY A PARENTE A DI MARTINO M. T PARLATO G MASULLO M RUOCCO, MARIA ROSARIA DE VENDITTIS, EMMANUELE Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue |
topic_facet |
Superoxide dismutase Pseudoalteromonas haloplankti psychrophilic enzyme sulfhydryl reactivity 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 mitochondrial 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 molecular 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 beta-mercaptoethanol, when this reducing agent is added in the purification procedure. The reactivity of Cys57 leads also to the formation of a disulfide bridge between two PhSOD subunits in specific denaturing conditions. The possible modification of Cys57 by physiological thiols, eventually regulating the PhSOD functioning, is discussed. |
author2 |
Castellano, I DI MARO, A Ruocco, MARIA ROSARIA Chambery, A Parente, A DI MARTINO M., T Parlato, G Masullo, M DE VENDITTIS, Emmanuele |
format |
Article in Journal/Newspaper |
author |
CASTELLANO I DI MARO A CHAMBERY A PARENTE A DI MARTINO M. T PARLATO G MASULLO M RUOCCO, MARIA ROSARIA DE VENDITTIS, EMMANUELE |
author_facet |
CASTELLANO I DI MARO A CHAMBERY A PARENTE A DI MARTINO M. T PARLATO G MASULLO M RUOCCO, MARIA ROSARIA DE VENDITTIS, EMMANUELE |
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/11588/201587 https://doi.org/10.1016/j.biochi.2006.04.005 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/16713057 volume:88 firstpage:1377 lastpage:1389 numberofpages:13 journal:BIOCHIMIE http://hdl.handle.net/11588/201587 doi:10.1016/j.biochi.2006.04.005 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-33750505881 |
op_rights |
info:eu-repo/semantics/closedAccess |
op_doi |
https://doi.org/10.1016/j.biochi.2006.04.005 |
container_title |
Biochimie |
container_volume |
88 |
container_issue |
10 |
container_start_page |
1377 |
op_container_end_page |
1389 |
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1796299259848425472 |