Redox control by dithiol-disulfide exchange in plants: II. The cytosolic and mitochondrial systems.
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.
Rouhier
Nicolas
N
Unité Mixte de Recherches 1136 INRA UHP (Interaction Arbres Microorganismes), Université Henri Poincaré BP 239, 54506 Vandoeuvre Cedex, France. nrouhier@scbiol.uhp-nancy.fr
Gelhaye
Eric
E
Jacquot
Jean-Pierre
JP
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
D004220:Disulfides; D013438:Sulfhydryl Compounds; D013879:Thioredoxins; D009249:NADP