Molecular Biomarkers, The Biodesign Institute at Arizona State University, Tempe, Arizona 85287, USA.
Biochemistry. 2010 Sep 7;49(35):7748-55. doi: 10.1021/bi1008694.
As a posttranslational protein modification, cysteine sulfenic acid (Cys-SOH) is well established as an oxidative stress-induced mediator of enzyme function and redox signaling. Data presented herein show that protein Cys-SOH forms spontaneously in air-exposed aqueous solutions of unfolded (disulfide-reduced) protein in the absence of added oxidizing reagents, mediating the oxidative disulfide bond formation process key to in vitro, nonenzymatic protein folding. Molecular oxygen (O(2)) and trace metals [e.g., copper(II)] are shown to be important reagents in the oxidative refolding process. Cys-SOH is also shown to play a role in spontaneous disulfide-based dimerization of peptide molecules containing free cysteine residues. In total, the data presented expose a chemically ubiquitous role for Cys-SOH in solutions of free cysteine-containing protein exposed to air.
作为一种翻译后蛋白质修饰，半胱氨酸亚磺酸（Cys-SOH）已被广泛确认为氧化应激诱导的酶功能和氧化还原信号的介质。本文提供的数据表明，在没有添加氧化试剂的情况下，未折叠（二硫键还原）蛋白质在空气中暴露于水溶液中会自发形成蛋白质 Cys-SOH，介导氧化二硫键形成过程，这是体外非酶促蛋白质折叠的关键。结果表明，分子氧（O（2））和痕量金属[例如，铜（II）]是氧化重折叠过程中的重要试剂。Cys-SOH 还在含有游离半胱氨酸残基的肽分子的自发基于二硫键的二聚化中发挥作用。总的来说，这些数据揭示了 Cys-SOH 在含有游离半胱氨酸的蛋白质溶液中暴露于空气中的普遍化学作用。
