title: Redox control by dithiol-disulfide exchange in plants: II. The cytosolic and mitochondrial systems.
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.
authors.affiliation: Unité Mixte de Recherches 1136 INRA UHP (Interaction Arbres Microorganismes), Université Henri Poincaré BP 239, 54506 Vandoeuvre Cedex, France. nrouhier@scbiol.uhp-nancy.fr
authors.forename: Nicolas
authors.initials: N
authors.lastname: Rouhier
authors.forename: Eric
authors.initials: E
authors.lastname: Gelhaye
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Jacquot
mesh_terms: D003600:Cytosol / Q000378:metabolism*; D004220:Disulfides / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D008954:Models, Biological; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D010944:Plants / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000378:metabolism*; D013879:Thioredoxins / Q000378:metabolism
chemical_list: D004220:Disulfides; D013438:Sulfhydryl Compounds; D013879:Thioredoxins; D009249:NADP