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The ratio of reduced glutathione to oxidized glutathione within cells is a measure of cellular oxidative stress [17] [10] where increased GSSG-to-GSH ratio is indicative of greater oxidative stress. In the reduced state, the thiol group of cysteinyl residue is a source of one reducing equivalent. Glutathione disulfide (GSSG) is thereby generated.
Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the GSR gene.Glutathione reductase (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide to the sulfhydryl form glutathione (), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell.
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 .
The NADPH maintains the supply of reduced glutathione in the cells that is used to mop up free radicals that cause oxidative damage. The pathway also stimulates catalase, an antioxidant enzyme. [20] The G6PD / NADPH pathway is the only source of reduced glutathione in red blood cells (erythrocytes). The role of red cells as oxygen carriers puts ...
The glutathione binding site, or "G-site", is located in the thioredoxin-like domain of both cytosolic and mitochondrial GSTs. The region containing the greatest amount of variability between the assorted classes is that of helix α2 , where one of three different amino acid residues interacts with the glycine residue of glutathione.
In contrast to thioredoxins, which are reduced by thioredoxin reductase, no oxidoreductase exists that specifically reduces glutaredoxins. Instead, glutaredoxins are reduced by the oxidation of glutathione. Reduced glutathione is then regenerated by glutathione reductase. Together these components compose the glutathione system. [6]
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