Oxidation reactions glutathione

Guengerich FP, Geiger LE, Hogy LL, et al. 1981. In vitro metabolism of acrylonitrile to 2-cyanoethylene oxide, reaction with glutathione, and irreversible binding to proteins and nucleic acids. Cancer Res 41 4925-4933. 

Peroxides, including hydrogen peroxide (H2O2), can damage cells by causing unwanted oxidation reactions. The tripeptide glutathione (GSH) is able to participate in a cellular protection mechanism via its ability to form disulfide bridges. 

Ellison DH, Salmon GA, Wilkinson F (1972) Nanosecond pulse radiolysis of methanolic and aqueous solutions of readily oxidizable solutes. Proc R Soc Lond A 328 23-36 Erben-Russ M, Bors W, Saran M (1987) Reactions of linoleic acid peroxyl radicals with phenolic antioxidants a pulse radiolysis study. Int J Radiat Biol 52 393-412 Eriksen TE, Fransson G (1988) Radical-induced oxidation of glutathione in alkaline aqueous solution. Radiat Phys Chem 32 163-167... 

Enzyme-based biosensors are very suitable for the antioxidant status evaluation, since they show excellent selectivity for biological substances and can directly determine and/or monitor antioxidant compounds in a complex media such as biological or vegetable samples without needing a prior separation step. During the course of the catalytic reaction on the electroactive substrates, the current produced at an applied potential is related to the concentration of a specific biomarker, for which the biosensor is selective. HRP-based biosensors for antioxidant status evaluation have been applied in the detection of superoxide radical [119], nitric oxide [120], glutathione [119, 121], uric acid [122, 123], and phenolic compounds [124—126],... 

Reoxidation of pro-a chains of types I and II procollagen into triple helical procollagen was studied using various concentrations of reduced (GSH) and oxidized (GSSG) glutathione as an oxidizing system in the reaction mixture. Pure protein disulfide-isomerase (PDI 5ng) was used in the reaction. 

The immediate product of the oxidative reaction, the monodehydroascorbate radical (Eq. [1]), is a fairly reactive and unstable species which, in the presence of a suitable reductase system, is reduced back to ascorbate. Monodehydroascorbate reductases have been identified and purified in a few cases (Ushimara et al., 1997 Dalton et al., 1992 Shigeoka et al., 1987 Borraccino et al., 1986 Hossain et al., 1984) and cDNA sequences have been published for the pea (Murthy and Zilinskas, 1994) and cucumber enzymes (Sano et al., 1995). A bacterial expression system is also available for the cucumber enzyme (Sano et al., 1995). In the absence of a suitably efficient reductase system, the monodehydroascorbate radicals disproportionate to dehydroascorbate and ascorbate in this case, ascorbate is regenerated using a glutathione-dependent dehydroascorbate reductase enzyme (Foyer and Mullineaux, 1998 and references therein). Under non-... 

The overall reaction is oxidation of glutathione at the expense of hydrogen peroxide, organic hydroperoxides, and fatty acid hydroperoxides, respectively, according to the following reaction ... 

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