Abstract
Glutaredoxins (Grxs) are small oxidoreductases of the thioredoxin family of proteins regulating the thiol redox state of several proteins. Thereby, Grxs are key elements in redox signaling. Redox signaling via protein thiols depends on reversible oxidative modifications induced mainly by reactive oxygen/nitrogen species and glutathione (GSH) in form of its oxidized disulfide or S-nitroso-glutathione. Grxs contribute to redox signaling by the catalysis of glutathionylation, de-glutathionylation, as well as reduction of disulfide bridges via two distinct enzymatic mechanisms. The dithiol mechanism utilizes both active site cysteines to reduce disulfides, whereas the monothiol mechanism utilizes only the N-terminal active site cysteine for the reduction of GSH mixed disulfides. The sphere of action of Grxs continues to grow with the recent identification of novel targets. Because of limited methodological tools, the identification of new substrates for oxidoreductases in general is one of the biggest challenges in this research area. With this review, we provide a condensed summary of the current knowledge of thiol/disulfide exchange reactions catalyzed by Grxs regarding the mechanistic, structural, and functional aspects. The latter will be of high importance for future research directions, gaining novel insights into redox signaling in general, and the role of Grxs in particular.
Published Version
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