Document Detail

Transimination of quinone imines: a mechanism for embedding exogenous redox activity into the nucleosome.
MedLine Citation:
PMID:  23194336     Owner:  NLM     Status:  MEDLINE    
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.
Wenjie Ye; Uthpala I Seneviratne; Ming-Wei Chao; Kodihalli C Ravindra; Gerald N Wogan; Steven R Tannenbaum; Paul L Skipper
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-12-03
Journal Detail:
Title:  Chemical research in toxicology     Volume:  25     ISSN:  1520-5010     ISO Abbreviation:  Chem. Res. Toxicol.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-17     Completed Date:  2013-05-16     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  8807448     Medline TA:  Chem Res Toxicol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2627-9     Citation Subset:  IM    
Department of Biological Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States.
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MeSH Terms
CHO Cells
Histones / metabolism*
Imines / metabolism*
Lysine / metabolism
Nucleosomes / metabolism*
Quinones / metabolism*
Grant Support
Reg. No./Substance:
0/Histones; 0/Imines; 0/Nucleosomes; 0/Quinones; 56-87-1/Lysine

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