Methionine one-electron oxidation: Coherent contributions from radiolysis, IRMPD spectroscopy, DFT calculations and electrochemistry
Methionine is an essential amino acid, unfortunately prone to oxidation. The mechanism of its oxidation by •OH radicals has been studied for more than 40 years and still remains misunderstood. We have reinvestigated the oxidation of this residue in model peptides, aiming at i) improving the identifi...
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Veröffentlicht in: | Radiation physics and chemistry (Oxford, England : 1993) England : 1993), 2016-11, Vol.128, p.103-111 |
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container_title | Radiation physics and chemistry (Oxford, England : 1993) |
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creator | Scuderi, Debora Bergès, Jacqueline de Oliveira, Pedro Houée-Levin, Chantal |
description | Methionine is an essential amino acid, unfortunately prone to oxidation. The mechanism of its oxidation by •OH radicals has been studied for more than 40 years and still remains misunderstood. We have reinvestigated the oxidation of this residue in model peptides, aiming at i) improving the identification of free radicals by the use of more modern quantum chemistry methods; ii) reinvestigating the one-electron reduction potentials as a function of the position in the sequence; iii) identifying the final compounds, which were still unknown; iv) reinvestigating the intramolecular electron transfer (IET) involving this residue.
•Methionine oxidation has been reinvestigated by time-resolved, electrochemistry and mass spectrometry methods.•The final compounds have been identified.•Methionine oxidation can be repaired by intramolecular electron transfer in peptides. |
doi_str_mv | 10.1016/j.radphyschem.2016.05.007 |
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•Methionine oxidation has been reinvestigated by time-resolved, electrochemistry and mass spectrometry methods.•The final compounds have been identified.•Methionine oxidation can be repaired by intramolecular electron transfer in peptides.</description><identifier>ISSN: 0969-806X</identifier><identifier>EISSN: 1879-0895</identifier><identifier>DOI: 10.1016/j.radphyschem.2016.05.007</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Biochemistry ; Biochemistry, Molecular Biology ; Chemical Sciences ; DFT computations ; Electrochemistry ; IRMPD ; Life Sciences ; Mass spectrometry ; Methionine oxidation ; or physical chemistry ; Pulse radiolysis ; Sulfoxide ; Theoretical and</subject><ispartof>Radiation physics and chemistry (Oxford, England : 1993), 2016-11, Vol.128, p.103-111</ispartof><rights>2016 Elsevier Ltd</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-d4b46cc58d4ebdc4f160b7b991323ffec0bb2353ea411a8525e80b69d9d98a1e3</citedby><cites>FETCH-LOGICAL-c406t-d4b46cc58d4ebdc4f160b7b991323ffec0bb2353ea411a8525e80b69d9d98a1e3</cites><orcidid>0000-0003-3931-8481 ; 0000-0002-4823-4143</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0969806X16301487$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://hal.sorbonne-universite.fr/hal-01320731$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Scuderi, Debora</creatorcontrib><creatorcontrib>Bergès, Jacqueline</creatorcontrib><creatorcontrib>de Oliveira, Pedro</creatorcontrib><creatorcontrib>Houée-Levin, Chantal</creatorcontrib><title>Methionine one-electron oxidation: Coherent contributions from radiolysis, IRMPD spectroscopy, DFT calculations and electrochemistry</title><title>Radiation physics and chemistry (Oxford, England : 1993)</title><description>Methionine is an essential amino acid, unfortunately prone to oxidation. The mechanism of its oxidation by •OH radicals has been studied for more than 40 years and still remains misunderstood. We have reinvestigated the oxidation of this residue in model peptides, aiming at i) improving the identification of free radicals by the use of more modern quantum chemistry methods; ii) reinvestigating the one-electron reduction potentials as a function of the position in the sequence; iii) identifying the final compounds, which were still unknown; iv) reinvestigating the intramolecular electron transfer (IET) involving this residue.
•Methionine oxidation has been reinvestigated by time-resolved, electrochemistry and mass spectrometry methods.•The final compounds have been identified.•Methionine oxidation can be repaired by intramolecular electron transfer in peptides.</description><subject>Biochemistry</subject><subject>Biochemistry, Molecular Biology</subject><subject>Chemical Sciences</subject><subject>DFT computations</subject><subject>Electrochemistry</subject><subject>IRMPD</subject><subject>Life Sciences</subject><subject>Mass spectrometry</subject><subject>Methionine oxidation</subject><subject>or physical chemistry</subject><subject>Pulse radiolysis</subject><subject>Sulfoxide</subject><subject>Theoretical and</subject><issn>0969-806X</issn><issn>1879-0895</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNqNUE1LxDAUDKLg-vEf4lGw9WX77U3Wj11YUWQFbyFNXmmWbrMkdbF3f7ipXcSjvMODycy8zBBywSBkwNLrdWiF2ta9kzVuwqmHQkhCgOyATFieFQHkRXJIJlCkRZBD-n5MTpxbg2fkSTQhX0_Y1dq0ukVqWgywQdlZ01LzqZXo_MsNnZkaLbYdlabtrC4_BtjRypoN9de1aXqn3RVdvD693FG3_XFw0mz7K3r3sKJSNPKjEaNKtIrujwxf1q6z_Rk5qkTj8Hy_T8nbw_1qNg-Wz4-L2e0ykDGkXaDiMk6lTHIVY6lkXLEUyqwsChZNo6pCCWU5jZIIRcyYyJNpgjmUaaH85IJhdEouR99aNHxr9UbYnhuh-fx2yQcMvBNkEdsxzy1GrvRZnMXqV8CAD9XzNf9TPR-q55BwX6zXzkYt-jA7jZY7qbGVqLT1ybky-h8u3xIyluQ</recordid><startdate>20161101</startdate><enddate>20161101</enddate><creator>Scuderi, Debora</creator><creator>Bergès, Jacqueline</creator><creator>de Oliveira, Pedro</creator><creator>Houée-Levin, Chantal</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>AAYXX</scope><scope>CITATION</scope><scope>1XC</scope><scope>VOOES</scope><orcidid>https://orcid.org/0000-0003-3931-8481</orcidid><orcidid>https://orcid.org/0000-0002-4823-4143</orcidid></search><sort><creationdate>20161101</creationdate><title>Methionine one-electron oxidation: Coherent contributions from radiolysis, IRMPD spectroscopy, DFT calculations and electrochemistry</title><author>Scuderi, Debora ; Bergès, Jacqueline ; de Oliveira, Pedro ; Houée-Levin, Chantal</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c406t-d4b46cc58d4ebdc4f160b7b991323ffec0bb2353ea411a8525e80b69d9d98a1e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Biochemistry</topic><topic>Biochemistry, Molecular Biology</topic><topic>Chemical Sciences</topic><topic>DFT computations</topic><topic>Electrochemistry</topic><topic>IRMPD</topic><topic>Life Sciences</topic><topic>Mass spectrometry</topic><topic>Methionine oxidation</topic><topic>or physical chemistry</topic><topic>Pulse radiolysis</topic><topic>Sulfoxide</topic><topic>Theoretical and</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Scuderi, Debora</creatorcontrib><creatorcontrib>Bergès, Jacqueline</creatorcontrib><creatorcontrib>de Oliveira, Pedro</creatorcontrib><creatorcontrib>Houée-Levin, Chantal</creatorcontrib><collection>CrossRef</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><jtitle>Radiation physics and chemistry (Oxford, England : 1993)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Scuderi, Debora</au><au>Bergès, Jacqueline</au><au>de Oliveira, Pedro</au><au>Houée-Levin, Chantal</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Methionine one-electron oxidation: Coherent contributions from radiolysis, IRMPD spectroscopy, DFT calculations and electrochemistry</atitle><jtitle>Radiation physics and chemistry (Oxford, England : 1993)</jtitle><date>2016-11-01</date><risdate>2016</risdate><volume>128</volume><spage>103</spage><epage>111</epage><pages>103-111</pages><issn>0969-806X</issn><eissn>1879-0895</eissn><abstract>Methionine is an essential amino acid, unfortunately prone to oxidation. The mechanism of its oxidation by •OH radicals has been studied for more than 40 years and still remains misunderstood. We have reinvestigated the oxidation of this residue in model peptides, aiming at i) improving the identification of free radicals by the use of more modern quantum chemistry methods; ii) reinvestigating the one-electron reduction potentials as a function of the position in the sequence; iii) identifying the final compounds, which were still unknown; iv) reinvestigating the intramolecular electron transfer (IET) involving this residue.
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source | Elsevier ScienceDirect Journals |
subjects | Biochemistry Biochemistry, Molecular Biology Chemical Sciences DFT computations Electrochemistry IRMPD Life Sciences Mass spectrometry Methionine oxidation or physical chemistry Pulse radiolysis Sulfoxide Theoretical and |
title | Methionine one-electron oxidation: Coherent contributions from radiolysis, IRMPD spectroscopy, DFT calculations and electrochemistry |
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