Treffon Patrick, Vierling Elizabeth
Department of Biochemistry & Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA.
Antioxidants (Basel). 2022 Jul 21;11(7):1411. doi: 10.3390/antiox11071411.
Protein cysteines (Cys) undergo a multitude of different reactive oxygen species (ROS), reactive sulfur species (RSS), and/or reactive nitrogen species (RNS)-derived modifications. -nitrosation (also referred to as nitrosylation), the addition of a nitric oxide (NO) group to reactive Cys thiols, can alter protein stability and activity and can result in changes of protein subcellular localization. Although it is clear that this nitrosative posttranslational modification (PTM) regulates multiple signal transduction pathways in plants, the enzymatic systems that catalyze the reverse -denitrosation reaction are poorly understood. This review provides an overview of the biochemistry and regulation of nitro-oxidative modifications of protein Cys residues with a focus on NO production and -nitrosation. In addition, the importance and recent advances in defining enzymatic systems proposed to be involved in regulating -denitrosation are addressed, specifically cytosolic thioredoxins (TRX) and the newly identified aldo-keto reductases (AKR).
蛋白质半胱氨酸（Cys）会经历多种不同的源自活性氧（ROS）、活性硫（RSS）和/或活性氮（RNS）的修饰。亚硝基化（也称为亚硝基化作用），即向反应性半胱氨酸硫醇添加一氧化氮（NO）基团，可改变蛋白质的稳定性和活性，并可能导致蛋白质亚细胞定位的变化。尽管很明显这种亚硝化翻译后修饰（PTM）在植物中调节多种信号转导途径，但对催化反向脱亚硝基化反应的酶系统了解甚少。本综述概述了蛋白质半胱氨酸残基亚硝基氧化修饰的生物化学和调控，重点是NO的产生和亚硝基化。此外，还讨论了在确定参与调节脱亚硝基化的酶系统方面的重要性和最新进展，特别是胞质硫氧还蛋白（TRX）和新鉴定的醛酮还原酶（AKR）。
