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Updated: May 18, 2026

Rapid Quantification of Oxidized and Reduced Forms of Glutathione Using Ortho -phthalaldehyde in Cultured Mammalian Cells In Vitro
Published on: June 28, 2024
Glutathione- and glutaredoxin-dependent reduction of methionine sulfoxide reductase A
Jérémy Couturier1, Florence Vignols, Jean-Pierre Jacquot
1UMR1136 Université de Lorraine-INRA, Interactions Arbres-Microorganismes, IFR 110, Faculté des Sciences, 54500 Vandoeuvre, France. Jeremy.Couturier@scbiol.uhp-nancy.fr
Abstract:
A natural fusion occurring between two tandemly repeated glutaredoxin (Grx) modules and a methionine sulfoxide reductase A (MsrA) has been detected in Gracilaria gracilis. Using an in vivo yeast complementation assay and in vitro activity measurements, we demonstrated that this fusion enzyme was able to reduce methionine sulfoxide into methionine using glutathione as a reductant. Consistently, a poplar cytosolic MsrA can be regenerated in vitro by glutaredoxins with an efficiency comparable to that of thioredoxins, but using a different mechanism. We hypothesize that the glutathione/glutaredoxin system could constitute an evolutionary conserved alternative regeneration system for MsrA.
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