Redox control by dithiol-disulfide exchange in plants: II. The cytosolic and mitochondrial systems.
Identifieur interne : 000F75 ( Main/Exploration ); précédent : 000F74; suivant : 000F76Redox control by dithiol-disulfide exchange in plants: II. The cytosolic and mitochondrial systems.
Auteurs : Nicolas Rouhier [France] ; Eric Gelhaye ; Jean-Pierre JacquotSource :
- Annals of the New York Academy of Sciences [ 0077-8923 ] ; 2002.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Cytosol, Disulfures, Mitochondries, NADP, Plantes, Thiols, Thiorédoxines.
- Modèles biologiques, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Disulfides, NADP, Sulfhydryl Compounds, Thioredoxins.
- metabolism : Cytosol, Mitochondria, Plants.
- Models, Biological, Oxidation-Reduction.
Abstract
This paper describes the existence of two pathways efficient in the reduction of disulfide bridges on selected proteins and mitochondria of photosynthetic organisms. The first is constituted by NADPH, the flavoenzyme NADPH thioredoxin reductase, and thioredoxin; and the second by NADPH, glutathione reductase, glutathione, and glutaredoxin. Molecular details concerning the proteins participating in these redox regulatory cascades are provided, and their molecular targets and functions are described.
DOI: 10.1111/j.1749-6632.2002.tb04693.x
PubMed: 12485921
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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The first is constituted by NADPH, the flavoenzyme NADPH thioredoxin reductase, and thioredoxin; and the second by NADPH, glutathione reductase, glutathione, and glutaredoxin. Molecular details concerning the proteins participating in these redox regulatory cascades are provided, and their molecular targets and functions are described.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12485921</PMID><DateCompleted><Year>2003</Year><Month>02</Month><Day>13</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0077-8923</ISSN><JournalIssue CitedMedium="Print"><Volume>973</Volume><PubDate><Year>2002</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Annals of the New York Academy of Sciences</Title><ISOAbbreviation>Ann N Y Acad Sci</ISOAbbreviation></Journal><ArticleTitle>Redox control by dithiol-disulfide exchange in plants: II. The cytosolic and mitochondrial systems.</ArticleTitle><Pagination><MedlinePgn>520-8</MedlinePgn></Pagination><Abstract><AbstractText>This paper describes the existence of two pathways efficient in the reduction of disulfide bridges on selected proteins and mitochondria of photosynthetic organisms. The first is constituted by NADPH, the flavoenzyme NADPH thioredoxin reductase, and thioredoxin; and the second by NADPH, glutathione reductase, glutathione, and glutaredoxin. 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