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Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome

[Image: see text] 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 l...

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Autores principales: Ye, Wenjie, Seneviratne, Uthpala I., Chao, Ming-Wei, Ravindra, Kodihalli C., Wogan, Gerald N., Tannenbaum, Steven R., Skipper, Paul L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2012
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3525013/
https://www.ncbi.nlm.nih.gov/pubmed/23194336
http://dx.doi.org/10.1021/tx3004517
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author Ye, Wenjie
Seneviratne, Uthpala I.
Chao, Ming-Wei
Ravindra, Kodihalli C.
Wogan, Gerald N.
Tannenbaum, Steven R.
Skipper, Paul L.
author_facet Ye, Wenjie
Seneviratne, Uthpala I.
Chao, Ming-Wei
Ravindra, Kodihalli C.
Wogan, Gerald N.
Tannenbaum, Steven R.
Skipper, Paul L.
author_sort Ye, Wenjie
collection PubMed
description [Image: see text] 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.
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spelling pubmed-35250132012-12-18 Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome Ye, Wenjie Seneviratne, Uthpala I. Chao, Ming-Wei Ravindra, Kodihalli C. Wogan, Gerald N. Tannenbaum, Steven R. Skipper, Paul L. Chem Res Toxicol [Image: see text] 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. American Chemical Society 2012-11-29 2012-12-17 /pmc/articles/PMC3525013/ /pubmed/23194336 http://dx.doi.org/10.1021/tx3004517 Text en Copyright © 2012 American Chemical Society http://pubs.acs.org This is an open-access article distributed under the ACS AuthorChoice Terms & Conditions. Any use of this article, must conform to the terms of that license which are available at http://pubs.acs.org.
spellingShingle Ye, Wenjie
Seneviratne, Uthpala I.
Chao, Ming-Wei
Ravindra, Kodihalli C.
Wogan, Gerald N.
Tannenbaum, Steven R.
Skipper, Paul L.
Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome
title Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome
title_full Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome
title_fullStr Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome
title_full_unstemmed Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome
title_short Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome
title_sort transimination of quinone imines: a mechanism for embedding exogenous redox activity into the nucleosome
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3525013/
https://www.ncbi.nlm.nih.gov/pubmed/23194336
http://dx.doi.org/10.1021/tx3004517
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