Liu Zhichao, Rouhier Nicolas, Couturier Jérémy
Université de Lorraine, INRAE, IAM, F-54000 Nancy, France.
Institut Universitaire de France, F-75000 Paris, France.
Antioxidants (Basel). 2025 Jan 16;14(1):101. doi: 10.3390/antiox14010101.
The oxidative modification of specific cysteine residues to persulfides is thought to be the main way by which hydrogen sulfide (HS) exerts its biological and signaling functions. Therefore, protein persulfidation represents an important thiol-switching mechanism as other reversible redox post-translational modifications. Considering their reductase activity but also their connections with proteins that generate HS and its related molecules, the glutaredoxin (GRX) and thioredoxin (TRX)-reducing systems have potential dual roles in both protein persulfidation and depersulfidation. In this review, we will first focus on recent advances describing the physiological pathways leading to protein persulfidation before discussing the dual roles of the physiological TRX and glutathione/GRX-reducing systems in protein persulfidation/depersulfidation.
特定半胱氨酸残基氧化修饰为过硫化物被认为是硫化氢（H₂S）发挥其生物学和信号传导功能的主要方式。因此，蛋白质过硫化作为一种重要的硫醇开关机制，与其他可逆的氧化还原翻译后修饰类似。考虑到谷氧还蛋白（GRX）和硫氧还蛋白（TRX）还原系统的还原酶活性以及它们与产生H₂S及其相关分子的蛋白质的联系，它们在蛋白质过硫化和去硫化过程中可能具有双重作用。在这篇综述中，我们将首先关注描述导致蛋白质过硫化的生理途径的最新进展，然后再讨论生理性TRX和谷胱甘肽/GRX还原系统在蛋白质过硫化/去硫化中的双重作用。
