Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System

By A. Fernandes, A. Holmgren. Antioxidants and Redox Signaling, 2004

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Redox-based regulation of signal transduction: principles, pitfalls, and promises. (2008, background): “Trx catalyze the reversible reduction of disulfides, resulting in a reduced pool of dithiol target protein, and a disulfide in the active form of Trx which is then reduced by thioredoxin reductase, using electrons from NADPH.”
Redox homeostasis in plants under abiotic stress: role of electron carriers, energy metabolism mediators and proteinaceous thiols (2015, background): “Glutaredoxins act as redox enzymes to catalyze the reduction of disulfides by using reduced glutathione (GSH) as a cofactor (Holmgren, 1988, 1989; Holmgren and Gleason, 1988).”
Posttranslational Protein Modification in Archaea (2005, background): “Acting as strong reductants in various cellular processes (120, 348), both the thioredoxin system, involving two thioredoxins and thioredoxin reductase, and the glutaredoxin system, including three glutaredoxins and glutathione reductase, maintain intracellular disulfide bonds in the reduced state t”
Comprehending crystalline β-carotene accumulation by comparing engineered cell models and the natural carotenoid-rich system of citrus (2011, neutral): “Glutaredoxins (Grxs) are thiol-disulphide oxidoreductases present in most prokaryotic and eukaryotic organisms (Fernandes and Holmgren, 2004).”