One- and two-electron oxidation of reduced glutathione by peroxidases.
نویسندگان
چکیده
منابع مشابه
Glutathione peroxidases as oncotargets
Oxidative stress is a disturbance in the equilibrium among free radicals, reactive oxygen species, and endogenous antioxidant defense mechanisms. Oxidative stress is a result of imbalance between the production of reactive oxygen and the biological system's ability to detoxify the reactive intermediates or to repair the resulting damage. Mounting evidence has implicated oxidative stress in vari...
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With the glutathione system that leads to rapid regeneration of reduced lysozyme (Saxena, V. P., and Wetlaufer, D. B. (1971) Biochemistry 9, 5015), reduced pancreatic ribonuclease (RNase) regenerated activity in high yield (greater than 90%) but at a considerably lower rate (t1/2 approximately 75 min). Systematic examination of the effects upon regeneration of the concentrations and ratios of r...
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Glutathione (GSH) was oxidized to GSSG in the presence of H2O2, tyrosine, and peroxidase. During the GSH oxidation catalyzed by lactoperoxidase, O2 was consumed and the formation of glutathione free radical was confirmed by ESR of its 5,5'-dimethyl-1-pyrroline-N-oxide adduct. When lactoperoxidase was replaced by thyroid peroxidase in the reaction system, the consumption of O2 and the formation ...
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Photosensitized one-electron oxidation of DNA has attracted much interest because it causes oxidative damage which leads to mutation, and because it is involved in the basic mechanism of photodynamic therapy. In the present article, we describe the mechanistic study of photosensitized DNA damage, especially addressing the kinetics of hole transfer by adenine(A)-hopping and its effect on the DNA...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1986
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)35988-4