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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Online Access: | http://hdl.handle.net/11591/181562 https://doi.org/10.1016/j.biochi.2006.04.005 |
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ftuncampaniairis:oai:iris.unicampania.it:11591/181562 2024-04-14T08:04:27+00:00 Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue CASTELLANO I DI MARO, Antimo RUOCCO MR CHAMBERY, Angela PARENTE A DI MARTINO MT PARLATO G MASULLO M DE VENDITTIS E. Castellano, I DI MARO, Antimo Ruocco, Mr Chambery, Angela Parente, A DI MARTINO, Mt Parlato, G Masullo, M DE VENDITTIS, E. 2006 http://hdl.handle.net/11591/181562 https://doi.org/10.1016/j.biochi.2006.04.005 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000242460000007 volume:88 issue:10 firstpage:1377 lastpage:1389 numberofpages:13 journal:BIOCHIMIE http://hdl.handle.net/11591/181562 doi:10.1016/j.biochi.2006.04.005 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-33750505881 Covalent modification Pseudoalteromonas haloplankti Psychrophilic enzyme Sulfhydryl reactivity Superoxide dismutase info:eu-repo/semantics/article 2006 ftuncampaniairis https://doi.org/10.1016/j.biochi.2006.04.005 2024-03-21T16:00:02Z 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 β-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. © 2006 Elsevier Masson SAS. All rights reserved. Article in Journal/Newspaper Antarc* Antarctic Università degli Studi della Campania "Luigi Vanvitelli": CINECA IRIS V: Antarctic The Antarctic Biochimie 88 10 1377 1389 |
institution |
Open Polar |
collection |
Università degli Studi della Campania "Luigi Vanvitelli": CINECA IRIS V: |
op_collection_id |
ftuncampaniairis |
language |
English |
topic |
Covalent modification Pseudoalteromonas haloplankti Psychrophilic enzyme Sulfhydryl reactivity Superoxide dismutase |
spellingShingle |
Covalent modification Pseudoalteromonas haloplankti Psychrophilic enzyme Sulfhydryl reactivity Superoxide dismutase CASTELLANO I DI MARO, Antimo RUOCCO MR CHAMBERY, Angela PARENTE A DI MARTINO MT 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 |
Covalent modification Pseudoalteromonas haloplankti Psychrophilic enzyme Sulfhydryl reactivity Superoxide dismutase |
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 β-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. © 2006 Elsevier Masson SAS. All rights reserved. |
author2 |
Castellano, I DI MARO, Antimo Ruocco, Mr Chambery, Angela Parente, A DI MARTINO, Mt Parlato, G Masullo, M DE VENDITTIS, E. |
format |
Article in Journal/Newspaper |
author |
CASTELLANO I DI MARO, Antimo RUOCCO MR CHAMBERY, Angela PARENTE A DI MARTINO MT PARLATO G MASULLO M DE VENDITTIS E. |
author_facet |
CASTELLANO I DI MARO, Antimo RUOCCO MR CHAMBERY, Angela PARENTE A DI MARTINO MT 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/11591/181562 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/wos/WOS:000242460000007 volume:88 issue:10 firstpage:1377 lastpage:1389 numberofpages:13 journal:BIOCHIMIE http://hdl.handle.net/11591/181562 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 |
container_issue |
10 |
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1377 |
op_container_end_page |
1389 |
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1796300977980047360 |