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Updated: Aug 7, 2026

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
Redox control by dithiol-disulfide exchange in plants: II. The cytosolic and mitochondrial systems
Nicolas Rouhier1, Eric Gelhaye, Jean-Pierre Jacquot
1Unité Mixte de Recherches 1136 INRA UHP (Interaction Arbres Microorganismes), Université Henri Poincaré BP 239, 54506 Vandoeuvre Cedex, France. nrouhier@scbiol.uhp-nancy.fr
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.
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