Dioxygen controls the nitrosylation reactions of a protein-bound [4Fe4S] cluster.
Identifieur interne : 000244 ( Main/Exploration ); précédent : 000243; suivant : 000245Dioxygen controls the nitrosylation reactions of a protein-bound [4Fe4S] cluster.
Auteurs : Daniel B. Grabarczyk [Royaume-Uni] ; Philip A. Ash [Royaume-Uni] ; William K. Myers [Royaume-Uni] ; Erin L. Dodd [Royaume-Uni] ; Kylie A. Vincent [Royaume-Uni]Source :
- Dalton transactions (Cambridge, England : 2003) [ 1477-9234 ] ; 2019.
Abstract
Iron-sulfur clusters are exceptionally tuneable protein cofactors, and as one of their many roles they are involved in biological responses to nitrosative stress. Both iron-sulfur proteins and synthetic model clusters are extremely sensitive to nitrosylation, tending towards rapid multi-step reaction and cluster degradation. Reaction of protein-bound iron-sulfur clusters with nitric oxide can be stopped at partial nitrosylation in vivo, and repair of protein-bound nitrosylated clusters is possible in the cellular environment. We have used a combination of infrared, EPR, and UV-visible spectroscopies to show that a model [4Fe4S] cluster-containing protein, A. ferroxidans high potential iron-sulfur protein (HiPIP), reacts with NO to give a product mixture dominated by Roussin's Black Salt (RBS) and Roussin's Red Ester (RRE) species. We have shown that O2 plays a critical role in controlling the major product of nitrosylation, with RBS-like products favoured under strictly anaerobic conditions and RRE favoured in the presence of trace O2. Moreover, addition of trace O2 to anaerobically nitrosylated samples induces conversion of RBS-like products to RRE. These findings may have implications for mechanisms of iron-sulfur cluster repair following nitrosative stress, suggest a crucial role for trace O2, and provide an important link between nitrosylation chemistry of iron-sulfur proteins and the well-established reactivity of synthetic iron-sulfur clusters.
DOI: 10.1039/c9dt00924h
PubMed: 31497816
Affiliations:
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Grabarczyk</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK. kylie.vincent@chem.ox.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR</wicri:regionArea><orgName type="university">Université d'Oxford</orgName><placeName><settlement type="city">Oxford</settlement><region type="nation">Angleterre</region><region type="région" nuts="1">Oxfordshire</region></placeName></affiliation></author><author><name sortKey="Ash, Philip A" sort="Ash, Philip A" uniqKey="Ash P" first="Philip A" last="Ash">Philip A. Ash</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK. kylie.vincent@chem.ox.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR</wicri:regionArea><orgName type="university">Université d'Oxford</orgName><placeName><settlement type="city">Oxford</settlement><region type="nation">Angleterre</region><region type="région" nuts="1">Oxfordshire</region></placeName></affiliation></author><author><name sortKey="Myers, William K" sort="Myers, William K" uniqKey="Myers W" first="William K" last="Myers">William K. 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Dodd</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK. kylie.vincent@chem.ox.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR</wicri:regionArea><orgName type="university">Université d'Oxford</orgName><placeName><settlement type="city">Oxford</settlement><region type="nation">Angleterre</region><region type="région" nuts="1">Oxfordshire</region></placeName></affiliation></author><author><name sortKey="Vincent, Kylie A" sort="Vincent, Kylie A" uniqKey="Vincent K" first="Kylie A" last="Vincent">Kylie A. Vincent</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK. kylie.vincent@chem.ox.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR</wicri:regionArea><orgName type="university">Université d'Oxford</orgName><placeName><settlement type="city">Oxford</settlement><region type="nation">Angleterre</region><region type="région" nuts="1">Oxfordshire</region></placeName></affiliation></author></analytic><series><title level="j">Dalton transactions (Cambridge, England : 2003)</title><idno type="eISSN">1477-9234</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Iron-sulfur clusters are exceptionally tuneable protein cofactors, and as one of their many roles they are involved in biological responses to nitrosative stress. Both iron-sulfur proteins and synthetic model clusters are extremely sensitive to nitrosylation, tending towards rapid multi-step reaction and cluster degradation. Reaction of protein-bound iron-sulfur clusters with nitric oxide can be stopped at partial nitrosylation in vivo, and repair of protein-bound nitrosylated clusters is possible in the cellular environment. We have used a combination of infrared, EPR, and UV-visible spectroscopies to show that a model [4Fe4S] cluster-containing protein, A. ferroxidans high potential iron-sulfur protein (HiPIP), reacts with NO to give a product mixture dominated by Roussin's Black Salt (RBS) and Roussin's Red Ester (RRE) species. We have shown that O<sub>2</sub> plays a critical role in controlling the major product of nitrosylation, with RBS-like products favoured under strictly anaerobic conditions and RRE favoured in the presence of trace O<sub>2</sub>. Moreover, addition of trace O<sub>2</sub> to anaerobically nitrosylated samples induces conversion of RBS-like products to RRE. These findings may have implications for mechanisms of iron-sulfur cluster repair following nitrosative stress, suggest a crucial role for trace O<sub>2</sub>, and provide an important link between nitrosylation chemistry of iron-sulfur proteins and the well-established reactivity of synthetic iron-sulfur clusters.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">31497816</PMID><DateCompleted><Year>2019</Year><Month>09</Month><Day>27</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>27</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1477-9234</ISSN><JournalIssue CitedMedium="Internet"><Volume>48</Volume><Issue>37</Issue><PubDate><Year>2019</Year><Month>Oct</Month><Day>07</Day></PubDate></JournalIssue><Title>Dalton transactions (Cambridge, England : 2003)</Title><ISOAbbreviation>Dalton Trans</ISOAbbreviation></Journal><ArticleTitle>Dioxygen controls the nitrosylation reactions of a protein-bound [4Fe4S] cluster.</ArticleTitle><Pagination><MedlinePgn>13960-13970</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1039/c9dt00924h</ELocationID><Abstract><AbstractText>Iron-sulfur clusters are exceptionally tuneable protein cofactors, and as one of their many roles they are involved in biological responses to nitrosative stress. Both iron-sulfur proteins and synthetic model clusters are extremely sensitive to nitrosylation, tending towards rapid multi-step reaction and cluster degradation. Reaction of protein-bound iron-sulfur clusters with nitric oxide can be stopped at partial nitrosylation in vivo, and repair of protein-bound nitrosylated clusters is possible in the cellular environment. We have used a combination of infrared, EPR, and UV-visible spectroscopies to show that a model [4Fe4S] cluster-containing protein, A. ferroxidans high potential iron-sulfur protein (HiPIP), reacts with NO to give a product mixture dominated by Roussin's Black Salt (RBS) and Roussin's Red Ester (RRE) species. We have shown that O<sub>2</sub> plays a critical role in controlling the major product of nitrosylation, with RBS-like products favoured under strictly anaerobic conditions and RRE favoured in the presence of trace O<sub>2</sub>. Moreover, addition of trace O<sub>2</sub> to anaerobically nitrosylated samples induces conversion of RBS-like products to RRE. These findings may have implications for mechanisms of iron-sulfur cluster repair following nitrosative stress, suggest a crucial role for trace O<sub>2</sub>, and provide an important link between nitrosylation chemistry of iron-sulfur proteins and the well-established reactivity of synthetic iron-sulfur clusters.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Grabarczyk</LastName><ForeName>Daniel B</ForeName><Initials>DB</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-0216-7085</Identifier><AffiliationInfo><Affiliation>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK. kylie.vincent@chem.ox.ac.uk.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ash</LastName><ForeName>Philip A</ForeName><Initials>PA</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-5264-464X</Identifier><AffiliationInfo><Affiliation>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK. kylie.vincent@chem.ox.ac.uk.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Myers</LastName><ForeName>William K</ForeName><Initials>WK</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-5935-9112</Identifier><AffiliationInfo><Affiliation>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK. kylie.vincent@chem.ox.ac.uk.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dodd</LastName><ForeName>Erin L</ForeName><Initials>EL</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-9870-2398</Identifier><AffiliationInfo><Affiliation>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK. kylie.vincent@chem.ox.ac.uk.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vincent</LastName><ForeName>Kylie A</ForeName><Initials>KA</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-6444-9382</Identifier><AffiliationInfo><Affiliation>Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK. kylie.vincent@chem.ox.ac.uk.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>09</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Dalton Trans</MedlineTA><NlmUniqueID>101176026</NlmUniqueID><ISSNLinking>1477-9226</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>9</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>9</Month><Day>10</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>9</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31497816</ArticleId><ArticleId IdType="doi">10.1039/c9dt00924h</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Oxfordshire</li></region><settlement><li>Oxford</li></settlement><orgName><li>Université d'Oxford</li></orgName></list><tree><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Grabarczyk, Daniel B" sort="Grabarczyk, Daniel B" uniqKey="Grabarczyk D" first="Daniel B" last="Grabarczyk">Daniel B. Grabarczyk</name></region><name sortKey="Ash, Philip A" sort="Ash, Philip A" uniqKey="Ash P" first="Philip A" last="Ash">Philip A. Ash</name><name sortKey="Dodd, Erin L" sort="Dodd, Erin L" uniqKey="Dodd E" first="Erin L" last="Dodd">Erin L. Dodd</name><name sortKey="Myers, William K" sort="Myers, William K" uniqKey="Myers W" first="William K" last="Myers">William K. Myers</name><name sortKey="Vincent, Kylie A" sort="Vincent, Kylie A" uniqKey="Vincent K" first="Kylie A" last="Vincent">Kylie A. Vincent</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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