Modifications of the Aerobic Respiratory Chain of Paracoccus Denitrificans in Response to Superoxide Oxidative Stress.
Identifieur interne : 000227 ( Main/Exploration ); précédent : 000226; suivant : 000228Modifications of the Aerobic Respiratory Chain of Paracoccus Denitrificans in Response to Superoxide Oxidative Stress.
Auteurs : Vojt Ch Sedlá Ek [République tchèque] ; Igor Ku Era [République tchèque]Source :
- Microorganisms [ 2076-2607 ] ; 2019.
Abstract
Paracoccus denitrificans is a strictly respiring bacterium with a core respiratory chain similar to that of mammalian mitochondria. As such, it continuously produces and has to cope with superoxide and other reactive oxygen species. In this work, the effects of artificially imposed superoxide stress on electron transport were examined. Exposure of aerobically growing cells to paraquat resulted in decreased activities of NADH dehydrogenase, succinate dehydrogenase, and N,N,N',N'-tetramethyl-p-phenylenediamine (TMPD) oxidase. Concomitantly, the total NAD(H) pool size in cells was approximately halved, but the NADH/NAD+ ratio increased twofold, thus partly compensating for inactivation losses of the dehydrogenase. The inactivation of respiratory dehydrogenases, but not of TMPD oxidase, also took place upon treatment of the membrane fraction with xanthine/xanthine oxidase. The decrease in dehydrogenase activities could be fully rescued by anaerobic incubation of membranes in a mixture containing 2-mercaptoethanol, sulfide and ferrous iron, which suggests iron-sulfur clusters as targets for superoxide. By using cyanide titration, a stress-sensitive contribution to the total TMPD oxidase activity was identified and attributed to the cbb3-type terminal oxidase. This response (measured by both enzymatic activity and mRNA level) was abolished in a mutant defective for the FnrP transcription factor. Therefore, our results provide evidence of oxidative stress perception by FnrP.
DOI: 10.3390/microorganisms7120640
PubMed: 31816877
PubMed Central: PMC6955949
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Modifications of the Aerobic Respiratory Chain of Paracoccus Denitrificans in Response to Superoxide Oxidative Stress.</title><author><name sortKey="Sedla Ek, Vojt Ch" sort="Sedla Ek, Vojt Ch" uniqKey="Sedla Ek V" first="Vojt Ch" last="Sedlá Ek">Vojt Ch Sedlá Ek</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno, Czech Republic.</nlm:affiliation><country xml:lang="fr">République tchèque</country><wicri:regionArea>Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno</wicri:regionArea><placeName><settlement type="city">Brno</settlement><region>Moravie</region></placeName></affiliation></author><author><name sortKey="Ku Era, Igor" sort="Ku Era, Igor" uniqKey="Ku Era I" first="Igor" last="Ku Era">Igor Ku Era</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno, Czech Republic.</nlm:affiliation><country xml:lang="fr">République tchèque</country><wicri:regionArea>Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno</wicri:regionArea><placeName><settlement type="city">Brno</settlement><region>Moravie</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2019">2019</date><idno type="RBID">pubmed:31816877</idno><idno type="pmid">31816877</idno><idno type="doi">10.3390/microorganisms7120640</idno><idno type="pmc">PMC6955949</idno><idno type="wicri:Area/Main/Corpus">000178</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000178</idno><idno type="wicri:Area/Main/Curation">000178</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000178</idno><idno type="wicri:Area/Main/Exploration">000178</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Modifications of the Aerobic Respiratory Chain of Paracoccus Denitrificans in Response to Superoxide Oxidative Stress.</title><author><name sortKey="Sedla Ek, Vojt Ch" sort="Sedla Ek, Vojt Ch" uniqKey="Sedla Ek V" first="Vojt Ch" last="Sedlá Ek">Vojt Ch Sedlá Ek</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno, Czech Republic.</nlm:affiliation><country xml:lang="fr">République tchèque</country><wicri:regionArea>Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno</wicri:regionArea><placeName><settlement type="city">Brno</settlement><region>Moravie</region></placeName></affiliation></author><author><name sortKey="Ku Era, Igor" sort="Ku Era, Igor" uniqKey="Ku Era I" first="Igor" last="Ku Era">Igor Ku Era</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno, Czech Republic.</nlm:affiliation><country xml:lang="fr">République tchèque</country><wicri:regionArea>Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno</wicri:regionArea><placeName><settlement type="city">Brno</settlement><region>Moravie</region></placeName></affiliation></author></analytic><series><title level="j">Microorganisms</title><idno type="ISSN">2076-2607</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"><i>Paracoccus denitrificans</i> is a strictly respiring bacterium with a core respiratory chain similar to that of mammalian mitochondria. As such, it continuously produces and has to cope with superoxide and other reactive oxygen species. In this work, the effects of artificially imposed superoxide stress on electron transport were examined. Exposure of aerobically growing cells to paraquat resulted in decreased activities of NADH dehydrogenase, succinate dehydrogenase, and <i>N</i>,<i>N</i>,<i>N</i>',<i>N</i>'-tetramethyl-p-phenylenediamine (TMPD) oxidase. Concomitantly, the total NAD(H) pool size in cells was approximately halved, but the NADH/NAD<sup>+</sup> ratio increased twofold, thus partly compensating for inactivation losses of the dehydrogenase. The inactivation of respiratory dehydrogenases, but not of TMPD oxidase, also took place upon treatment of the membrane fraction with xanthine/xanthine oxidase. The decrease in dehydrogenase activities could be fully rescued by anaerobic incubation of membranes in a mixture containing 2-mercaptoethanol, sulfide and ferrous iron, which suggests iron-sulfur clusters as targets for superoxide. By using cyanide titration, a stress-sensitive contribution to the total TMPD oxidase activity was identified and attributed to the <i>cbb</i><sub>3</sub>-type terminal oxidase. This response (measured by both enzymatic activity and mRNA level) was abolished in a mutant defective for the FnrP transcription factor. Therefore, our results provide evidence of oxidative stress perception by FnrP.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">31816877</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>28</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Print">2076-2607</ISSN><JournalIssue CitedMedium="Print"><Volume>7</Volume><Issue>12</Issue><PubDate><Year>2019</Year><Month>Dec</Month><Day>03</Day></PubDate></JournalIssue><Title>Microorganisms</Title><ISOAbbreviation>Microorganisms</ISOAbbreviation></Journal><ArticleTitle>Modifications of the Aerobic Respiratory Chain of Paracoccus Denitrificans in Response to Superoxide Oxidative Stress.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E640</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/microorganisms7120640</ELocationID><Abstract><AbstractText><i>Paracoccus denitrificans</i> is a strictly respiring bacterium with a core respiratory chain similar to that of mammalian mitochondria. As such, it continuously produces and has to cope with superoxide and other reactive oxygen species. In this work, the effects of artificially imposed superoxide stress on electron transport were examined. Exposure of aerobically growing cells to paraquat resulted in decreased activities of NADH dehydrogenase, succinate dehydrogenase, and <i>N</i>,<i>N</i>,<i>N</i>',<i>N</i>'-tetramethyl-p-phenylenediamine (TMPD) oxidase. Concomitantly, the total NAD(H) pool size in cells was approximately halved, but the NADH/NAD<sup>+</sup> ratio increased twofold, thus partly compensating for inactivation losses of the dehydrogenase. The inactivation of respiratory dehydrogenases, but not of TMPD oxidase, also took place upon treatment of the membrane fraction with xanthine/xanthine oxidase. The decrease in dehydrogenase activities could be fully rescued by anaerobic incubation of membranes in a mixture containing 2-mercaptoethanol, sulfide and ferrous iron, which suggests iron-sulfur clusters as targets for superoxide. By using cyanide titration, a stress-sensitive contribution to the total TMPD oxidase activity was identified and attributed to the <i>cbb</i><sub>3</sub>-type terminal oxidase. This response (measured by both enzymatic activity and mRNA level) was abolished in a mutant defective for the FnrP transcription factor. Therefore, our results provide evidence of oxidative stress perception by FnrP.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sedláček</LastName><ForeName>Vojtěch</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno, Czech Republic.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kučera</LastName><ForeName>Igor</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno, Czech Republic.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GA16-18476S</GrantID><Agency>Grantová Agentura České Republiky</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>12</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Microorganisms</MedlineTA><NlmUniqueID>101625893</NlmUniqueID><ISSNLinking>2076-2607</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">FnrP transcription factor</Keyword><Keyword MajorTopicYN="N">NADH dehydrogenase</Keyword><Keyword MajorTopicYN="N">iron–sulfur cluster</Keyword><Keyword MajorTopicYN="N">succinate dehydrogenase</Keyword><Keyword MajorTopicYN="N">superoxide</Keyword><Keyword MajorTopicYN="N">terminal oxidase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>11</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>11</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>11</Month><Day>29</Day></PubMedPubDate><PubMedPubDate 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