过氧化物酶对还原型谷胱甘肽的单电子和双电子氧化作用。
One- and two-electron oxidation of reduced glutathione by peroxidases.
作者信息
Mason R P
出版信息
Adv Exp Med Biol. 1986;197:493-503. doi: 10.1007/978-1-4684-5134-4_47.
The oxidation of glutathione by horseradish peroxidase or lactoperoxidase forms a thiyl free radical, as demonstrated with the spin-trapping ESR technique. Reactions of this thiyl free radical result in oxygen consumption, which is inhibited by the radical trap 5,5-dimethyl-1-pyrroline-N-oxide. In contrast to L-cysteine oxidation, glutathione oxidation is highly hydrogen peroxide-dependent. The oxidation of glutathione by glutathione peroxidase forms GSSG without forming a thiyl radical intermediate except in the presence of the thiyl radical-generating horseradish peroxidase.
如自旋捕获电子顺磁共振技术所证实，辣根过氧化物酶或乳过氧化物酶使谷胱甘肽氧化会形成一个硫自由基。该硫自由基的反应会导致耗氧，而这种耗氧会被自由基捕获剂5,5-二甲基-1-吡咯啉-N-氧化物抑制。与L-半胱氨酸氧化不同，谷胱甘肽氧化高度依赖过氧化氢。谷胱甘肽过氧化物酶使谷胱甘肽氧化会形成氧化型谷胱甘肽，除了在存在能产生硫自由基的辣根过氧化物酶的情况下，不会形成硫自由基中间体。
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