Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome
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 altern...
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| Format: | Article |
| Language: | en_US |
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American Chemical Society (ACS)
2013
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| Online Access: | http://hdl.handle.net/1721.1/82110 https://orcid.org/0000-0001-6774-9639 https://orcid.org/0000-0003-0771-9889 |
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| author | Ye, Wenjie Seneviratne, Uthpala I. Chao, Ming-Wei Wogan, Gerald N. Skipper, Paul L. Kodihalli, Ravindra Tannenbaum, Steven Robert |
| author2 | Massachusetts Institute of Technology. Department of Biological Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Biological Engineering Ye, Wenjie Seneviratne, Uthpala I. Chao, Ming-Wei Wogan, Gerald N. Skipper, Paul L. Kodihalli, Ravindra Tannenbaum, Steven Robert |
| author_sort | Ye, Wenjie |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T17:03:19Z |
| format | Article |
| id | mit-1721.1/82110 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T17:03:19Z |
| publishDate | 2013 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/821102022-10-03T10:04:46Z Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome Ye, Wenjie Seneviratne, Uthpala I. Chao, Ming-Wei Wogan, Gerald N. Skipper, Paul L. Kodihalli, Ravindra Tannenbaum, Steven Robert Massachusetts Institute of Technology. Department of Biological Engineering Massachusetts Institute of Technology. Department of Chemistry Ye, Wenjie Seneviratne, Uthpala I. Chao, Ming-Wei Kodihalli, Ravindra Wogan, Gerald N. Tannenbaum, Steven Robert Skipper, Paul L. 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. Agilent Technologies 2013-11-13T18:00:06Z 2013-11-13T18:00:06Z 2012-11 2012-11 Article http://purl.org/eprint/type/JournalArticle 0893-228X 1520-5010 http://hdl.handle.net/1721.1/82110 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 https://orcid.org/0000-0001-6774-9639 https://orcid.org/0000-0003-0771-9889 en_US http://dx.doi.org/10.1021/tx3004517 Chemical Research in Toxicology 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. application/pdf American Chemical Society (ACS) PMC |
| spellingShingle | Ye, Wenjie Seneviratne, Uthpala I. Chao, Ming-Wei Wogan, Gerald N. Skipper, Paul L. Kodihalli, Ravindra Tannenbaum, Steven Robert 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 | http://hdl.handle.net/1721.1/82110 https://orcid.org/0000-0001-6774-9639 https://orcid.org/0000-0003-0771-9889 |
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