Journal of the American Chemical Society 2005-05-04

Site-specific binding of quinones to proteins through thiol addition and addition-elimination reactions.

Wen-Wu Li, Jürgen Heinze, Wolfgang Haehnel

Index: J. Am. Chem. Soc. 127(17) , 6140-1, (2005)

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Abstract

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.