Site-Specific Binding of Quinones to Proteins through Thiol Addition and Addition-Elimination Reactions

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• 作者：Wen-Wu Li ; Jü ; rgen Heinze ; and Wolfgang Haehnel
• 刊名：Journal of the American Chemical Society
• 出版年：2005
• 出版时间：May 4, 2005
• 年：2005
• 卷：127
• 期：17
• 页码：6140 - 6141
• 全文大小：79K
• 年卷期：v.127,no.17(May 4, 2005)
• ISSN：1520-5126

文摘

Ubiquinone-0, menaquinone-0, and 2,3,5-trimethyl-1,4-benzoquinone were site-specifically bound to free cysteine of proteins (yeast iso-1 cytochrome c as a model protein) through thioether bond formation. Model thioether quinone conjugates showed unexpected reactivity to cysteine of proteins as their parent quinones by thiol addition-elimination reaction. Cyclic voltammetry studies of the model compounds showed only minor differences in their redox potentials as compared to their parent quinones. Thioether ligation provides a general, simple, and fast method to construct model quinone protein systems. In addition, these studies also contribute to the understanding of biological activities, toxicity, and anti-cancer mechanism of quinones and thioether quinone adducts.