<?xml version="1.0" encoding="utf-8"?>
<TEI xmlns="http://www.tei-c.org/ns/1.0" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:hal="http://hal.archives-ouvertes.fr/" xmlns:gml="http://www.opengis.net/gml/3.3/" xmlns:gmlce="http://www.opengis.net/gml/3.3/ce" version="1.1" xsi:schemaLocation="http://www.tei-c.org/ns/1.0 http://api.archives-ouvertes.fr/documents/aofr-sword.xsd">
  <teiHeader>
    <fileDesc>
      <titleStmt>
        <title>HAL TEI export of hal-01453211</title>
      </titleStmt>
      <publicationStmt>
        <distributor>CCSD</distributor>
        <availability status="restricted">
          <licence target="https://creativecommons.org/publicdomain/zero/1.0/">CC0 1.0 - Universal</licence>
        </availability>
        <date when="2026-05-19T02:52:00+02:00"/>
      </publicationStmt>
      <sourceDesc>
        <p part="N">HAL API Platform</p>
      </sourceDesc>
    </fileDesc>
  </teiHeader>
  <text>
    <body>
      <listBibl>
        <biblFull>
          <titleStmt>
            <title xml:lang="en">Methionine sulfoxide reductase: Chemistry, substrate binding, recycling process and oxidase activity</title>
            <author role="aut">
              <persName>
                <forename type="first">Sandrine</forename>
                <surname>Boschi-Muller</surname>
              </persName>
              <email type="md5">03be522d6c9ad2e2b4a772cd6218cc6d</email>
              <email type="domain">univ-lorraine.fr</email>
              <idno type="idhal" notation="string">sandrine-boschi-muller</idno>
              <idno type="idhal" notation="numeric">17907</idno>
              <idno type="halauthorid" notation="string">4633-17907</idno>
              <idno type="IDREF">https://www.idref.fr/160452341</idno>
              <idno type="ORCID">https://orcid.org/0000-0001-8962-4749</idno>
              <idno type="IDREF">https://www.idref.fr/131331957</idno>
              <affiliation ref="#struct-237046"/>
            </author>
            <author role="crp">
              <persName>
                <forename type="first">Guy</forename>
                <surname>Branlant</surname>
              </persName>
              <email type="md5">eddfa3a5fe7f93dbaeeee0b6ac183c1a</email>
              <email type="domain">univ-lorraine.fr</email>
              <idno type="idhal" notation="numeric">1000150</idno>
              <idno type="halauthorid" notation="string">212448-1000150</idno>
              <affiliation ref="#struct-237046"/>
            </author>
            <editor role="depositor">
              <persName>
                <forename>Imopa</forename>
                <surname>UL</surname>
              </persName>
              <email type="md5">6ac87a7d24c67a9b6c0da9ddfdaf629b</email>
              <email type="domain">univ-lorraine.fr</email>
            </editor>
          </titleStmt>
          <editionStmt>
            <edition n="v1" type="current">
              <date type="whenSubmitted">2017-02-02 16:12:49</date>
              <date type="whenModified">2024-06-25 10:16:20</date>
              <date type="whenReleased">2017-02-02 16:12:49</date>
              <date type="whenProduced">2014-12</date>
            </edition>
            <respStmt>
              <resp>contributor</resp>
              <name key="480089">
                <persName>
                  <forename>Imopa</forename>
                  <surname>UL</surname>
                </persName>
                <email type="md5">6ac87a7d24c67a9b6c0da9ddfdaf629b</email>
                <email type="domain">univ-lorraine.fr</email>
              </name>
            </respStmt>
          </editionStmt>
          <publicationStmt>
            <distributor>CCSD</distributor>
            <idno type="halId">hal-01453211</idno>
            <idno type="halUri">https://hal.univ-lorraine.fr/hal-01453211</idno>
            <idno type="halBibtex">boschimuller:hal-01453211</idno>
            <idno type="halRefHtml">&lt;i&gt;Bioorganic Chemistry&lt;/i&gt;, 2014, 57, pp.222-230. &lt;a target="_blank" href="https://dx.doi.org/10.1016/j.bioorg.2014.07.002"&gt;&amp;#x27E8;10.1016/j.bioorg.2014.07.002&amp;#x27E9;&lt;/a&gt;</idno>
            <idno type="halRef">Bioorganic Chemistry, 2014, 57, pp.222-230. &amp;#x27E8;10.1016/j.bioorg.2014.07.002&amp;#x27E9;</idno>
            <availability status="restricted"/>
          </publicationStmt>
          <seriesStmt>
            <idno type="stamp" n="CNRS">CNRS - Centre national de la recherche scientifique</idno>
            <idno type="stamp" n="UNIV-LORRAINE">Université de Lorraine</idno>
            <idno type="stamp" n="IMOPA-UL">IMoPA - Ingénierie Moléculaire, Cellulaire et Physiopathologie</idno>
            <idno type="stamp" n="BMS-UL">Pôle scientifique Biologie, Médecine, Santé de l'Université de Lorraine</idno>
            <idno type="stamp" n="IMOPA-EQ3">Enzymologie Moléculaire &amp; Structurale (EMS)</idno>
          </seriesStmt>
          <notesStmt>
            <note type="audience" n="2">International</note>
            <note type="popular" n="0">No</note>
            <note type="peer" n="1">Yes</note>
          </notesStmt>
          <sourceDesc>
            <biblStruct>
              <analytic>
                <title xml:lang="en">Methionine sulfoxide reductase: Chemistry, substrate binding, recycling process and oxidase activity</title>
                <author role="aut">
                  <persName>
                    <forename type="first">Sandrine</forename>
                    <surname>Boschi-Muller</surname>
                  </persName>
                  <email type="md5">03be522d6c9ad2e2b4a772cd6218cc6d</email>
                  <email type="domain">univ-lorraine.fr</email>
                  <idno type="idhal" notation="string">sandrine-boschi-muller</idno>
                  <idno type="idhal" notation="numeric">17907</idno>
                  <idno type="halauthorid" notation="string">4633-17907</idno>
                  <idno type="IDREF">https://www.idref.fr/160452341</idno>
                  <idno type="ORCID">https://orcid.org/0000-0001-8962-4749</idno>
                  <idno type="IDREF">https://www.idref.fr/131331957</idno>
                  <affiliation ref="#struct-237046"/>
                </author>
                <author role="crp">
                  <persName>
                    <forename type="first">Guy</forename>
                    <surname>Branlant</surname>
                  </persName>
                  <email type="md5">eddfa3a5fe7f93dbaeeee0b6ac183c1a</email>
                  <email type="domain">univ-lorraine.fr</email>
                  <idno type="idhal" notation="numeric">1000150</idno>
                  <idno type="halauthorid" notation="string">212448-1000150</idno>
                  <affiliation ref="#struct-237046"/>
                </author>
              </analytic>
              <monogr>
                <idno type="halJournalId" status="VALID">11203</idno>
                <idno type="issn">0045-2068</idno>
                <idno type="eissn">1090-2120</idno>
                <title level="j">Bioorganic Chemistry</title>
                <imprint>
                  <publisher>Elsevier</publisher>
                  <biblScope unit="volume">57</biblScope>
                  <biblScope unit="pp">222-230</biblScope>
                  <date type="datePub">2014-12</date>
                </imprint>
              </monogr>
              <idno type="doi">10.1016/j.bioorg.2014.07.002</idno>
            </biblStruct>
          </sourceDesc>
          <profileDesc>
            <langUsage>
              <language ident="en">English</language>
            </langUsage>
            <textClass>
              <classCode scheme="halDomain" n="sdv.bbm.bc">Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM]</classCode>
              <classCode scheme="halDomain" n="sdv.mhep">Life Sciences [q-bio]/Human health and pathology</classCode>
              <classCode scheme="halTypology" n="ART">Journal articles</classCode>
              <classCode scheme="halOldTypology" n="ART">Journal articles</classCode>
              <classCode scheme="halTreeTypology" n="ART">Journal articles</classCode>
            </textClass>
            <abstract xml:lang="en">
              <p>Three classes of methionine sulfoxide reductases are known: MsrA and MsrB which are implicated stereo-selectively in the repair of protein oxidized on their methionine residues; and fRMsr, discovered more recently, which binds and reduces selectively free L-Met-R-O. It is now well established that the chemical mechanism of the reductase step passes through formation of a sulfenic acid intermediate. The oxidized catalytic cysteine can then be recycled by either Trx when a recycling cysteine is operative or a reductant like glutathione in the absence of recycling cysteine which is the case for 30% of the MsrBs. Recently, it was shown that a subclass of MsrAs with two recycling cysteines displays an oxidase activity. This reverse activity needs the accumulation of the sulfenic acid intermediate. The present review focuses on recent insights into the catalytic mechanism of action of the Msrs based on kinetic studies, theoretical chemistry investigations and new structural data. Major attention is placed on how the sulfenic acid intermediate can be formed and the oxidized catalytic cysteine returns back to its reduced form. (C) 2014 Elsevier Inc. All rights reserved.</p>
            </abstract>
          </profileDesc>
        </biblFull>
      </listBibl>
    </body>
    <back>
      <listOrg type="structures">
        <org type="laboratory" xml:id="struct-237046" status="OLD">
          <idno type="IdRef">180727281</idno>
          <idno type="ISNI">0000000417589034</idno>
          <idno type="RNSR">201320578R</idno>
          <idno type="IdUnivLorraine">[UL]RNG--</idno>
          <idno type="ROR">https://ror.org/04yc2e502</idno>
          <orgName>Ingénierie Moléculaire et Physiopathologie Articulaire</orgName>
          <orgName type="acronym">IMoPA</orgName>
          <date type="start">2013-01-01</date>
          <date type="end">2023-12-31</date>
          <desc>
            <address>
              <addrLine>Université de Lorraine, Faculté de Médicine, 9 avenue de la Forêt de Haye, BP 184, 54505 Vandoeuvre-les-Nancy Cedex</addrLine>
              <country key="FR"/>
            </address>
            <ref type="url">http://www.imopa.cnrs.fr/</ref>
          </desc>
          <listRelation>
            <relation active="#struct-413289" type="direct"/>
            <relation name="UMR7365" active="#struct-441569" type="direct"/>
          </listRelation>
        </org>
        <org type="institution" xml:id="struct-413289" status="VALID">
          <idno type="IdRef">157040569</idno>
          <idno type="IdUnivLorraine">[UL]100--</idno>
          <idno type="ROR">https://ror.org/04vfs2w97</idno>
          <orgName>Université de Lorraine</orgName>
          <orgName type="acronym">UL</orgName>
          <date type="start">2012-01-01</date>
          <desc>
            <address>
              <addrLine>34 cours Léopold - CS 25233 - 54052 Nancy cedex</addrLine>
              <country key="FR"/>
            </address>
            <ref type="url">http://www.univ-lorraine.fr/</ref>
          </desc>
        </org>
        <org type="regroupinstitution" xml:id="struct-441569" status="VALID">
          <idno type="IdRef">02636817X</idno>
          <idno type="ISNI">0000000122597504</idno>
          <idno type="ROR">https://ror.org/02feahw73</idno>
          <orgName>Centre National de la Recherche Scientifique</orgName>
          <orgName type="acronym">CNRS</orgName>
          <date type="start">1939-10-19</date>
          <desc>
            <address>
              <country key="FR"/>
            </address>
            <ref type="url">https://www.cnrs.fr/</ref>
          </desc>
        </org>
      </listOrg>
    </back>
  </text>
</TEI>