Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides.
Identifieur interne : 000257 ( Main/Exploration ); précédent : 000256; suivant : 000258Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides.
Auteurs : Ashwinie A. Ukuwela [Australie] ; Ashley I. Bush [Australie] ; Anthony G. Wedd [Australie] ; Zhiguang Xiao [Australie]Source :
- Chemical science [ 2041-6520 ] ; 2018.
Abstract
Glutaredoxins (Grxs) are a family of glutathione (GSH)-dependent thiol-disulfide oxidoreductases. They feature GSH-binding sites that directly connect the reversible redox chemistry of protein thiols to the abundant cellular nonprotein thiol pool GSSG/GSH. This work studied the pathways for oxidation of protein dithiols P(SH)2 and reduction of protein disulfides P(SS) catalyzed by Homo sapiens HsGrx1 and Escherichia coli EcGrx1. The metal-binding domain HMA4n(SH)2 was chosen as substrate as it contains a solvent-exposed CysCys motif. Quenching of the reactions with excess iodoacetamide followed by protein speciation analysis via ESI-MS allowed interception and characterization of both substrate and enzyme intermediates. The enzymes shuttle between three catalytically-competent forms (Grx(SH)(S-), Grx(SH)(SSG) and Grx(SS)) and employ conserved parallel monothiol and dithiol mechanisms. Experiments with dithiol and monothiol versions of both Grx enzymes demonstrate which monothiol (plus GSSG or GSH) or dithiol pathways dominate a specific oxidation or reduction reaction. Grxs are shown to be a class of versatile enzymes with diverse catalytic functions that are driven by specific interactions with GSSG/GSH.
DOI: 10.1039/c7sc04416j
PubMed: 29675162
PubMed Central: PMC5885593
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Ukuwela</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry , Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3010 , Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry , Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3010 </wicri:regionArea><wicri:noRegion>Victoria 3010 </wicri:noRegion></affiliation></author><author><name sortKey="Bush, Ashley I" sort="Bush, Ashley I" uniqKey="Bush A" first="Ashley I" last="Bush">Ashley I. Bush</name><affiliation wicri:level="1"><nlm:affiliation>Melbourne Dementia Research Centre , Florey Institute of Neuroscience and Mental Health , The University of Melbourne , Parkville , Victoria 3052 , Australia . Email: zhiguang.xiao@florey.edu.au.</nlm:affiliation><country wicri:rule="url">Australie</country></affiliation></author><author><name sortKey="Wedd, Anthony G" sort="Wedd, Anthony G" uniqKey="Wedd A" first="Anthony G" last="Wedd">Anthony G. Wedd</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry , Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3010 , Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry , Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3010 </wicri:regionArea><wicri:noRegion>Victoria 3010 </wicri:noRegion></affiliation></author><author><name sortKey="Xiao, Zhiguang" sort="Xiao, Zhiguang" uniqKey="Xiao Z" first="Zhiguang" last="Xiao">Zhiguang Xiao</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry , Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3010 , Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry , Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3010 </wicri:regionArea><wicri:noRegion>Victoria 3010 </wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Melbourne Dementia Research Centre , Florey Institute of Neuroscience and Mental Health , The University of Melbourne , Parkville , Victoria 3052 , Australia . Email: zhiguang.xiao@florey.edu.au.</nlm:affiliation><country wicri:rule="url">Australie</country></affiliation></author></analytic><series><title level="j">Chemical science</title><idno type="ISSN">2041-6520</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) are a family of glutathione (GSH)-dependent thiol-disulfide oxidoreductases. They feature GSH-binding sites that directly connect the reversible redox chemistry of protein thiols to the abundant cellular nonprotein thiol pool GSSG/GSH. This work studied the pathways for oxidation of protein dithiols P(SH)<sub>2</sub> and reduction of protein disulfides P(SS) catalyzed by <i>Homo sapiens</i> HsGrx1 and <i>Escherichia coli</i> EcGrx1. The metal-binding domain HMA4n(SH)<sub>2</sub> was chosen as substrate as it contains a solvent-exposed CysCys motif. Quenching of the reactions with excess iodoacetamide followed by protein speciation analysis <i>via</i> ESI-MS allowed interception and characterization of both substrate and enzyme intermediates. The enzymes shuttle between three catalytically-competent forms (Grx(SH)(S<sup>-</sup>), Grx(SH)(SSG) and Grx(SS)) and employ conserved parallel monothiol and dithiol mechanisms. Experiments with dithiol and monothiol versions of both Grx enzymes demonstrate which monothiol (plus GSSG or GSH) or dithiol pathways dominate a specific oxidation or reduction reaction. Grxs are shown to be a class of versatile enzymes with diverse catalytic functions that are driven by specific interactions with GSSG/GSH.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">29675162</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">2041-6520</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>5</Issue><PubDate><Year>2018</Year><Month>Feb</Month><Day>07</Day></PubDate></JournalIssue><Title>Chemical science</Title><ISOAbbreviation>Chem Sci</ISOAbbreviation></Journal><ArticleTitle>Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides.</ArticleTitle><Pagination><MedlinePgn>1173-1183</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1039/c7sc04416j</ELocationID><Abstract><AbstractText>Glutaredoxins (Grxs) are a family of glutathione (GSH)-dependent thiol-disulfide oxidoreductases. They feature GSH-binding sites that directly connect the reversible redox chemistry of protein thiols to the abundant cellular nonprotein thiol pool GSSG/GSH. This work studied the pathways for oxidation of protein dithiols P(SH)<sub>2</sub> and reduction of protein disulfides P(SS) catalyzed by <i>Homo sapiens</i> HsGrx1 and <i>Escherichia coli</i> EcGrx1. The metal-binding domain HMA4n(SH)<sub>2</sub> was chosen as substrate as it contains a solvent-exposed CysCys motif. Quenching of the reactions with excess iodoacetamide followed by protein speciation analysis <i>via</i> ESI-MS allowed interception and characterization of both substrate and enzyme intermediates. The enzymes shuttle between three catalytically-competent forms (Grx(SH)(S<sup>-</sup>), Grx(SH)(SSG) and Grx(SS)) and employ conserved parallel monothiol and dithiol mechanisms. Experiments with dithiol and monothiol versions of both Grx enzymes demonstrate which monothiol (plus GSSG or GSH) or dithiol pathways dominate a specific oxidation or reduction reaction. Grxs are shown to be a class of versatile enzymes with diverse catalytic functions that are driven by specific interactions with GSSG/GSH.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ukuwela</LastName><ForeName>Ashwinie A</ForeName><Initials>AA</Initials><Identifier Source="ORCID">0000-0002-9974-1436</Identifier><AffiliationInfo><Affiliation>School of Chemistry , Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3010 , Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bush</LastName><ForeName>Ashley I</ForeName><Initials>AI</Initials><Identifier Source="ORCID">0000-0001-8259-9069</Identifier><AffiliationInfo><Affiliation>Melbourne Dementia Research Centre , Florey Institute of Neuroscience and Mental Health , The University of Melbourne , Parkville , Victoria 3052 , Australia . Email: zhiguang.xiao@florey.edu.au.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wedd</LastName><ForeName>Anthony G</ForeName><Initials>AG</Initials><AffiliationInfo><Affiliation>School of Chemistry , Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3010 , Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Xiao</LastName><ForeName>Zhiguang</ForeName><Initials>Z</Initials><Identifier Source="ORCID">0000-0001-6908-8897</Identifier><AffiliationInfo><Affiliation>School of Chemistry , Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3010 , Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Melbourne Dementia Research Centre , Florey Institute of Neuroscience and Mental Health , The University of Melbourne , Parkville , Victoria 3052 , Australia . 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Ukuwela</name></noRegion><name sortKey="Bush, Ashley I" sort="Bush, Ashley I" uniqKey="Bush A" first="Ashley I" last="Bush">Ashley I. Bush</name><name sortKey="Wedd, Anthony G" sort="Wedd, Anthony G" uniqKey="Wedd A" first="Anthony G" last="Wedd">Anthony G. Wedd</name><name sortKey="Xiao, Zhiguang" sort="Xiao, Zhiguang" uniqKey="Xiao Z" first="Zhiguang" last="Xiao">Zhiguang Xiao</name><name sortKey="Xiao, Zhiguang" sort="Xiao, Zhiguang" uniqKey="Xiao Z" first="Zhiguang" last="Xiao">Zhiguang Xiao</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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