Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome
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Ye_2012-Transimination of quinone.pdf
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Author(s)
Ye, Wenjie
Seneviratne, Uthpala I.
Chao, Ming-Wei
Wogan, Gerald N.
Skipper, Paul L.
Kodihalli, Ravindra
Tannenbaum, Steven Robert
Date Issued
November 2012
Journal
Chemical Research in Toxicology
Publisher
American Chemical Society (ACS)
Citation
Ye, Wenjie, Uthpala I. Seneviratne, Ming-Wei Chao, Kodihalli C. Ravindra, Gerald N. Wogan, Steven R. Tannenbaum, and Paul L. Skipper. “Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome.” Chemical Research in Toxicology 25, no. 12 (December 17, 2012): 2627-2629. © 2012 American Chemical Society
Version
Final published version
Abstract
Aminophenols can redox cycle through the corresponding quinone imines to generate ROS. The electrophilic quinone imine intermediate can react with protein thiols as a mechanism of immobilization in vivo. Here, we describe the previously unkown transimination of a quinone imine by lysine as an alternative anchoring mechanism. The redox properties of the condensation product remain largely unchanged because the only structural change to the redox nucleus is the addition of an alkyl substituent to the imine nitrogen. Transimination enables targeting of histone proteins since histones are lysine-rich but nearly devoid of cysteines. Consequently, quinone imines can be embedded in the nucleosome and may be expected to produce ROS in maximal proximity to the genome.
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
Massachusetts Institute of Technology. Department of Chemistry
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1021/tx3004517
