Biochemical properties of poplar thioredoxin z.
Identifieur interne : 002F86 ( Main/Exploration ); précédent : 002F85; suivant : 002F87Biochemical properties of poplar thioredoxin z.
Auteurs : Kamel Chibani [France] ; Lionel Tarrago ; Peter Schürmann ; Jean-Pierre Jacquot ; Nicolas RouhierSource :
- FEBS letters [ 1873-3468 ] ; 2011.
Descripteurs français
- KwdFr :
- Antioxydants (métabolisme), Ferrosulfoprotéines (métabolisme), Oxidoreductases (métabolisme), Plastes (métabolisme), Populus (cytologie), Populus (enzymologie), Populus (métabolisme), Protéines végétales (métabolisme), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (métabolisme), Transport d'électrons (MeSH).
- MESH :
- cytologie : Populus.
- enzymologie : Populus.
- métabolisme : Antioxydants, Ferrosulfoprotéines, Oxidoreductases, Plastes, Populus, Protéines végétales, Thioredoxin-disulfide reductase, Thiorédoxines.
- Transport d'électrons.
English descriptors
- KwdEn :
- Antioxidants (metabolism), Electron Transport (MeSH), Iron-Sulfur Proteins (metabolism), Oxidoreductases (metabolism), Plant Proteins (metabolism), Plastids (metabolism), Populus (cytology), Populus (enzymology), Populus (metabolism), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (metabolism).
- MESH :
- chemical , metabolism : Antioxidants, Iron-Sulfur Proteins, Oxidoreductases, Plant Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- cytology : Populus.
- enzymology : Populus.
- metabolism : Plastids, Populus.
- Electron Transport.
Abstract
Trx-z is a chloroplastic thioredoxin, exhibiting a usual WCGPC active site, but whose biochemical properties are unknown. We demonstrate here that Trx-z supports the activity of several plastidial antioxidant enzymes, such as thiol-peroxidases and methionine sulfoxide reductases, using electrons provided by ferredoxin-thioredoxin reductase. Its disulfide reductase activity requires the presence of both active site cysteines forming a catalytic disulfide bridge with a midpoint redox potential of -251 mV at pH7. These in vitro biochemical data suggest that, besides its decisive role in the regulation of plastidial transcription, Trx-z might also be involved in stress response.
DOI: 10.1016/j.febslet.2011.03.006
PubMed: 21385584
Affiliations:
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(metabolism)</term><term>Plastids (metabolism)</term><term>Populus (cytology)</term><term>Populus (enzymology)</term><term>Populus (metabolism)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antioxydants (métabolisme)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Oxidoreductases (métabolisme)</term><term>Plastes (métabolisme)</term><term>Populus (cytologie)</term><term>Populus (enzymologie)</term><term>Populus (métabolisme)</term><term>Protéines végétales (métabolisme)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term><term>Thiorédoxines (métabolisme)</term><term>Transport d'électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antioxidants</term><term>Iron-Sulfur Proteins</term><term>Oxidoreductases</term><term>Plant Proteins</term><term>Thioredoxin-Disulfide 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We demonstrate here that Trx-z supports the activity of several plastidial antioxidant enzymes, such as thiol-peroxidases and methionine sulfoxide reductases, using electrons provided by ferredoxin-thioredoxin reductase. Its disulfide reductase activity requires the presence of both active site cysteines forming a catalytic disulfide bridge with a midpoint redox potential of -251 mV at pH7. These in vitro biochemical data suggest that, besides its decisive role in the regulation of plastidial transcription, Trx-z might also be involved in stress response.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21385584</PMID><DateCompleted><Year>2011</Year><Month>05</Month><Day>26</Day></DateCompleted><DateRevised><Year>2011</Year><Month>04</Month><Day>04</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3468</ISSN><JournalIssue CitedMedium="Internet"><Volume>585</Volume><Issue>7</Issue><PubDate><Year>2011</Year><Month>Apr</Month><Day>06</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Biochemical properties of poplar thioredoxin z.</ArticleTitle><Pagination><MedlinePgn>1077-81</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.febslet.2011.03.006</ELocationID><Abstract><AbstractText>Trx-z is a chloroplastic thioredoxin, exhibiting a usual WCGPC active site, but whose biochemical properties are unknown. We demonstrate here that Trx-z supports the activity of several plastidial antioxidant enzymes, such as thiol-peroxidases and methionine sulfoxide reductases, using electrons provided by ferredoxin-thioredoxin reductase. Its disulfide reductase activity requires the presence of both active site cysteines forming a catalytic disulfide bridge with a midpoint redox potential of -251 mV at pH7. These in vitro biochemical data suggest that, besides its decisive role in the regulation of plastidial transcription, Trx-z might also be involved in stress response.</AbstractText><CopyrightInformation>Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. 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