Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Chemical compound
Glutathione disulfide (GSSG) is a disulfide derived from two glutathione molecules.[1]
In living cells, glutathione disulfide is reduced into two molecules of glutathione with reducing equivalents from the coenzyme NADPH. This reaction is catalyzed by the enzyme glutathione reductase.[2]
Antioxidant enzymes, such as glutathione peroxidases and peroxiredoxins, generate glutathione disulfide during the reduction of peroxides such as hydrogen peroxide (H2O2) and organic hydroperoxides (ROOH):[3]
2 GSH + ROOH → GSSG + ROH + H2O
Other enzymes, such as glutaredoxins, generate glutathione disulfide through thiol-disulfide exchange with protein disulfide bonds or other low molecular mass compounds, such as coenzyme A disulfide or dehydroascorbic acid.[4]
2 GSH + R-S-S-R → GSSG + 2 RSH
The GSH:GSSG ratio is therefore an important bioindicator of cellular health, with a higher ratio signifying less oxidative stress in the organism. A lower ratio may even be indicative of neurodegenerative diseases, such as Parkinson's disease (PD) and Alzheimer's disease.[5]
^Meister A, Anderson ME (1983). "Glutathione". Annual Review of Biochemistry. 52: 711–60. doi:10.1146/annurev.bi.52.070183.003431. PMID 6137189.
^Deneke SM, Fanburg BL (1989). "Regulation of cellular glutathione". The American Journal of Physiology. 257 (4 Pt 1): L163–73. doi:10.1152/ajplung.1989.257.4.L163. PMID 2572174.
^Meister A (1988). "Glutathione metabolism and its selective modification". The Journal of Biological Chemistry. 263 (33): 17205–8. doi:10.1016/S0021-9258(19)77815-6. PMID 3053703.
^Holmgren A, Johansson C, Berndt C, Lönn ME, Hudemann C, Lillig CH (December 2005). "Thiol redox control via thioredoxin and glutaredoxin systems". Biochem. Soc. Trans. 33 (Pt 6): 1375–7. doi:10.1042/BST20051375. PMID 16246122.
^Owen, Joshua B.; Butterfield, D. Allan (2010). "Measurement of oxidized/reduced glutathione ratio". In Bross, Peter; Gregersen, Niels (eds.). Protein Misfolding and Cellular Stress in Disease and Aging. Methods in Molecular Biology. Vol. 648. pp. 269–77. doi:10.1007/978-1-60761-756-3_18. ISBN 978-1-60761-755-6. PMID 20700719.
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tissue, more than 90% of the total glutathione pool is in the reduced form (GSH), with the remainder in the disulfide form (GSSG). 80-85% of cellular GSH...
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environment of the cell as viewed through the redox state of the glutathionedisulfide/glutathione couple". Free Radic Biol Med. 30 (11): 1191–212. doi:10...
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the rancidification of oils and fats. In cells, antioxidants such as glutathione, mycothiol, or bacillithiol, and enzyme systems like superoxide dismutase...
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strongly oxidizing member. Using glutathione oxidation as a metric, DsbA is ten times more oxidizing than protein disulfide-isomerase (the eukaryotic equivalent...