Ruhr University Bochum, Institute of Biochemistry and Pathobiochemistry, Microbial Biochemistry, Universitätsstrasse 150, 44780 Bochum, Germany.
Ruhr University Bochum, Institute of Biochemistry and Pathobiochemistry, Microbial Biochemistry, Universitätsstrasse 150, 44780 Bochum, Germany.
Curr Opin Chem Biol. 2023 Dec;77:102390. doi: 10.1016/j.cbpa.2023.102390. Epub 2023 Oct 3.
Due to its nucleophilicity, the thiol group of cysteine is chemically very versatile. Hence, cysteine often has important functions in a protein, be it as the active site or, in extracellular proteins, as part of a structural disulfide. Within the cytosol, cysteines are typically reduced. But the nucleophilicity of its thiol group makes it also particularly prone to post-translational oxidative modifications. These modifications often lead to an alteration of the function of the affected protein and are reversible in vivo, e.g. by the thioredoxin and glutaredoxin system. The in vivo-reversible nature of these modifications and their genesis in the presence of localized high oxidant levels led to the paradigm of thiol-based redox regulation, the adaptation, and modulation of the cellular metabolism in response to oxidative stimuli by thiol oxidation in regulative proteins. Consequently, the proteomic study of these oxidative posttranslational modifications of cysteine plays an indispensable role in redox biology.
由于其亲核性，半胱氨酸的巯基在化学上非常多样。因此，半胱氨酸在蛋白质中经常具有重要的功能，无论是作为活性位点，还是在细胞外蛋白质中，作为结构二硫键的一部分。在细胞质中，半胱氨酸通常被还原。但其巯基的亲核性使其特别容易发生翻译后氧化修饰。这些修饰通常会导致受影响蛋白质的功能发生改变，并且在体内是可逆的，例如通过硫氧还蛋白和谷氧还蛋白系统。这些修饰的体内不可逆性及其在局部高氧化剂水平存在下的起源导致了基于巯基的氧化还原调节范例的出现，即通过调节蛋白中的巯基氧化来适应和调节细胞代谢对氧化刺激的反应。因此，对半胱氨酸的这些氧化翻译后修饰的蛋白质组学研究在氧化还原生物学中起着不可或缺的作用。
