Glutathione disulfide

Glutathione disulfide
Names
Systematic IUPAC name
(2S,2′S)-5,5′-(Disulfanediylbis{(2R)-3-[(carboxymethyl)amino]-3-oxopropane-1,2-diyl})bis(2-amino-5-oxopentanoic acid)
Identifiers
3D model (JSmol)
Abbreviations GSSG
ChEMBL
ChemSpider
ECHA InfoCard 100.043.777 Edit this at Wikidata
KEGG
UNII
  • InChI=1S/C20H32N6O12S2/c21-9(19(35)36)1-3-13(27)25-11(17(33)23-5-15(29)30)7-39-40-8-12(18(34)24-6-16(31)32)26-14(28)4-2-10(22)20(37)38/h9-12H,1-8,21-22H2,(H,23,33)(H,24,34)(H,25,27)(H,26,28)(H,29,30)(H,31,32)(H,35,36)(H,37,38)/t9-,10-,11-,12-/m0/s1 ☒N
    Key: YPZRWBKMTBYPTK-BJDJZHNGSA-N ☒N
  • InChI=1/C20H32N6O12S2/c21-9(19(35)36)1-3-13(27)25-11(17(33)23-5-15(29)30)7-39-40-8-12(18(34)24-6-16(31)32)26-14(28)4-2-10(22)20(37)38/h9-12H,1-8,21-22H2,(H,23,33)(H,24,34)(H,25,27)(H,26,28)(H,29,30)(H,31,32)(H,35,36)(H,37,38)/t9-,10-,11-,12-/m0/s1
    Key: YPZRWBKMTBYPTK-BJDJZHNGBD
  • C(CC(=O)N[C@@H](CSSC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=O)O)N)C(=O)NCC(=O)O)[C@@H](C(=O)O)N
Properties
C20H32N6O12S2
Molar mass 612.63 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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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]

  1. ^ Meister A, Anderson ME (1983). "Glutathione". Annual Review of Biochemistry. 52: 711–60. doi:10.1146/annurev.bi.52.070183.003431. PMID 6137189.
  2. ^ 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. Archived from the original on 2020-06-10. Retrieved 2017-03-20.
  3. ^ 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. Archived from the original on 2020-06-10. Retrieved 2017-03-20.
  4. ^ 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.
  5. ^ 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.