Cysteine residues in proteins are subject to diverse redox chemistry. Oxidation of cysteine to S-nitrosocysteine, cysteine sulfenic and sulfinic acids, disulfides and persulfides are a few prominent examples of these oxidative post-translational modifications. In living organisms, these modifications often play key roles in cell signalling and protein function, but a full account of this biochemistry is far from complete. It is therefore an important goal in chemical biology to identify what proteins are subjected to these modifications and understand their physiological function. This review provides an overview of these modifications, how they can be detected and quantified using chemical probes, and how this information provides insight into their role in biology. This survey also highlights future opportunities in the study of cysteine redox chemistry, the challenges that await chemists and biologists in this area of study, and how meeting such challenges might reveal valuable information for biomedical science.

中文翻译：

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半胱氨酸氧化作图的化学方法

蛋白质中的半胱氨酸残基经受多种氧化还原化学作用。半胱氨酸氧化成硫-亚硝基半胱氨酸，半胱氨酸亚磺酸和亚磺酸，二硫化物和过硫化物是这些氧化后翻译修饰的一些突出实例。在活生物体中，这些修饰通常在细胞信号传导和蛋白质功能中起关键作用，但是对这种生物化学的完整描述远未完成。因此，化学生物学的一个重要目标是确定哪些蛋白质会受到这些修饰并了解其生理功能。这篇综述概述了这些修饰，如何使用化学探针对它们进行检测和定量，以及这些信息如何洞察其在生物学中的作用。这项调查还重点介绍了半胱氨酸氧化还原化学研究的未来机遇，以及该领域研究人员所面临的挑战，