Protein cysteine oxidation in redox signaling: Caveats on sulfenic acid detection and quantification
Protein cysteine oxidation in redox signaling: Caveats on sulfenic acid detection and quantification
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DOI：
10.1016/j.abb.2016.09.013
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发表时间：
2017-03-01
影响因子：
3.9
通讯作者：
Ursini, Fulvio
中科院分区：
文献类型：
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作者：
Forman, Henry Jay;Davies, Michael J.;Ursini, Fulvio
H2O2 调节的关键信号蛋白半胱氨酸的氧化被认为涉及次磺酸 (RSOH) 的形成。 RSOH 随后可能与邻近的酰胺形成磺酰胺 (RSNHR')，或与另一种蛋白质半胱氨酸或谷胱甘肽形成混合二硫键 (RSSR')。先前的研究声称 RSOH 可以作为加合物被检测到（例如，与 5,5-二甲基环己烷-1,3-二酮；双甲酮）。这里讨论的动力学数据表明很少有蛋白质可以在生理信号条件下形成 RSOH。我们还提供了实验证据，表明（1）双甲酮与硫基酰胺反应迅速，比与次磺酸反应更快，（2）二硫化物可以与酰胺可逆地反应形成硫基酰胺。由于一些蛋白质作为次磺酰胺比作为谷胱甘肽化物质更稳定，因此前者可能解释了一些先前被鉴定为“亚磺基”的物质——通过次磺酸产生的可逆氧化硫醇蛋白的细胞补体。 (C) 2016 Elsevier Inc. 保留所有权利。
Oxidation of critical signaling protein cysteines regulated by H2O2 has been considered to involve sulfenic acid (RSOH) formation. RSOH may subsequently form either a sulfenyl amide (RSNHR') with a neighboring amide, or a mixed disulfide (RSSR') with another protein cysteine or glutathione. Previous studies have claimed that RSOH can be detected as an adduct (e.g., with 5,5-dimethylcyclohexane-1,3-dione; dimedone). Here, kinetic data are discussed which indicate that few proteins can form RSOH under physiological signaling conditions. We also present experimental evidence that indicates that (1) dimedone reacts rapidly with sulfenyl amides, and more rapidly than with sulfenic acids, and (2) that disulfides can react reversibly with amides to form sulfenyl amides. As some proteins are more stable as the sulfenyl amide than as a glutathionylated species, the former may account for some of the species previously identified as the "sulfenome" - the cellular complement of reversibly-oxidized thiol proteins generated via sulfenic acids. (C) 2016 Elsevier Inc. All rights reserved.