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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Thiol-based redox processes
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Thiol-based redox processes

机译：基于硫醇的氧化还原工艺

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摘要

Almost 40 years ago it was discovered that thioredoxin is the physiological hydrogen donor needed for the biosynthesis of desoxyribonucleotides, the building blocks of DNA [1]. Since then, we know that thiol-based redox reactions are indispensible in some of the most fundamental processes of life.Thioredoxins and their closely related cousins glutaredoxins also play an important role in keeping the cysteines of cytoplasmic proteins (and proteins in other reducing cell compartments) in their reduced state. Keeping cysteines reduced is important for maintaining the structure of these proteins, because non-native disulfide bonds can lead to unfolding and inactivation. The presence of these thiol-disulfide oxido-reductases is especially important under conditions of oxidative stress, when reactive species threaten to inactivate vital cellular enzymes by cysteine oxidation.
机译：大约40年前，人们发现硫氧还蛋白是脱氧核糖核苷酸（DNA的组成部分）的生物合成所需的生理氢供体[1]。从那时起，我们知道基于硫醇的氧化还原反应在生命的某些最基本过程中是必不可少的。硫氧还蛋白及其密切相关的表亲谷胱甘肽毒素在保持胞质蛋白（以及其他还原性细胞室蛋白）的半胱氨酸中也起着重要作用。 ）处于还原状态。保持半胱氨酸还原对于维持这些蛋白质的结构很重要，因为非天然的二硫键可能导致解折叠和失活。当活性物质威胁通过半胱氨酸氧化使重要的细胞酶失活时，在氧化应激条件下，这些巯基-二硫键氧化还原酶的存在尤其重要。

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