Quinone- and nitroreductase reactions of Thermotoga maritima thioredoxin reductase.
Identifieur interne : 000516 ( Main/Exploration ); précédent : 000515; suivant : 000517Quinone- and nitroreductase reactions of Thermotoga maritima thioredoxin reductase.
Auteurs : Benjaminas Valiauga [Lituanie] ; Nicolas Rouhier [France] ; Jean-Pierre Jacquot [France] ; Narimantas Nas [Lituanie]Source :
- Acta biochimica Polonica [ 1734-154X ] ; 2015.
Descripteurs français
- KwdFr :
- Catalyse (MeSH), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Flavine adénine dinucléotide (métabolisme), Glutarédoxines (métabolisme), NAD (métabolisme), Nitroréductases (métabolisme), Protéines bactériennes (composition chimique), Protéines bactériennes (métabolisme), Quinones (métabolisme), Sites de fixation (MeSH), Spécificité du substrat (MeSH), Thermodynamique (MeSH), Thermotoga maritima (enzymologie), Thioredoxin-disulfide reductase (composition chimique), Thioredoxin-disulfide reductase (métabolisme).
- MESH :
- composition chimique : Protéines bactériennes, Thioredoxin-disulfide reductase.
- enzymologie : Thermotoga maritima.
- métabolisme : Flavine adénine dinucléotide, Glutarédoxines, NAD, Nitroréductases, Protéines bactériennes, Quinones, Thioredoxin-disulfide reductase.
- Catalyse, Cinétique, Concentration en ions d'hydrogène, Sites de fixation, Spécificité du substrat, Thermodynamique.
English descriptors
- KwdEn :
- Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Binding Sites (MeSH), Catalysis (MeSH), Flavin-Adenine Dinucleotide (metabolism), Glutaredoxins (metabolism), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), NAD (metabolism), Nitroreductases (metabolism), Quinones (metabolism), Substrate Specificity (MeSH), Thermodynamics (MeSH), Thermotoga maritima (enzymology), Thioredoxin-Disulfide Reductase (chemistry), Thioredoxin-Disulfide Reductase (metabolism).
- MESH :
- chemical , chemistry : Bacterial Proteins, Thioredoxin-Disulfide Reductase.
- chemical , metabolism : Bacterial Proteins, Flavin-Adenine Dinucleotide, Glutaredoxins, NAD, Nitroreductases, Quinones, Thioredoxin-Disulfide Reductase.
- enzymology : Thermotoga maritima.
- Binding Sites, Catalysis, Hydrogen-Ion Concentration, Kinetics, Substrate Specificity, Thermodynamics.
Abstract
The Thermotoga maritima NADH:thioredoxin reductase (TmTR) contains FAD and a catalytic disulfide in the active center, and uses a relatively poorly studied physiological oxidant Grx-1-type glutaredoxin. In order to further assess the redox properties of TmTR, we used series of quinoidal and nitroaromatic oxidants with a wide range of single-electron reduction potentials (E(1)7, -0.49-0.09 V). We found that TmTR catalyzed the mixed single- and two-electron reduction of quinones and nitroaromatic compounds, which was much faster than the reduction of Grx-1. The reactivity of both groups of oxidants increased with an increase in their E(1)7, thus pointing to the absence of their structural specificity. The maximal rates of quinone reduction in the steady-state reactions were lower than the maximal rates of reduction of FAD by NADH, obtained in presteady-state experiments. The mixed-type reaction inhibition by NAD(+) was consistent with its competition for a NADH binding site in the oxidized enzyme form, and also with the reoxidation of the reduced enzyme form. The inhibition data yielded a value of the standard potential for TmTR of -0.31±0.03 V at pH 7.0, which may correspond to the FAD/FADH2 redox couple. Overall, the mechanism of quinone- and nitroreductase reactions of T. maritima TR was similar to the previously described mechanism of Arabidopsis thaliana TR, and points to their prooxidant and possibly cytotoxic role.
DOI: 10.18388/abp.2015_1003
PubMed: 26098718
Affiliations:
Links toward previous steps (curation, corpus...)
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and INRA, Interactions Arbres-Microorganismes, UMR1136, F-54280 Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Universite de Lorraine, Interactions Arbres-Microorganismes, UMR1136, F-54500 Vandoeuvre-les-Nancy, France; and INRA, Interactions Arbres-Microorganismes, UMR1136, F-54280 Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><affiliation wicri:level="4"><nlm:affiliation>Universite de Lorraine, Interactions Arbres-Microorganismes, UMR1136, F-54500 Vandoeuvre-les-Nancy, France; and INRA, Interactions Arbres-Microorganismes, UMR1136, F-54280 Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Universite de Lorraine, Interactions Arbres-Microorganismes, UMR1136, F-54500 Vandoeuvre-les-Nancy, France; and INRA, Interactions Arbres-Microorganismes, UMR1136, F-54280 Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey=" Nas, Narimantas" sort=" Nas, Narimantas" uniqKey=" Nas N" first="Narimantas" last=" Nas">Narimantas Nas</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Biochemistry of Vilnius University, LT-08662 Vilnius, Lithuania.</nlm:affiliation><country xml:lang="fr">Lituanie</country><wicri:regionArea>Institute of Biochemistry of Vilnius University, LT-08662 Vilnius</wicri:regionArea><wicri:noRegion>LT-08662 Vilnius</wicri:noRegion></affiliation></author></analytic><series><title level="j">Acta biochimica Polonica</title><idno type="eISSN">1734-154X</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (metabolism)</term><term>Binding Sites (MeSH)</term><term>Catalysis (MeSH)</term><term>Flavin-Adenine Dinucleotide (metabolism)</term><term>Glutaredoxins (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Kinetics (MeSH)</term><term>NAD (metabolism)</term><term>Nitroreductases (metabolism)</term><term>Quinones (metabolism)</term><term>Substrate Specificity (MeSH)</term><term>Thermodynamics (MeSH)</term><term>Thermotoga maritima (enzymology)</term><term>Thioredoxin-Disulfide Reductase (chemistry)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse (MeSH)</term><term>Cinétique (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Flavine adénine dinucléotide (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>NAD (métabolisme)</term><term>Nitroréductases (métabolisme)</term><term>Protéines bactériennes (composition chimique)</term><term>Protéines bactériennes (métabolisme)</term><term>Quinones (métabolisme)</term><term>Sites de fixation (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Thermodynamique (MeSH)</term><term>Thermotoga maritima (enzymologie)</term><term>Thioredoxin-disulfide reductase (composition chimique)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Flavin-Adenine Dinucleotide</term><term>Glutaredoxins</term><term>NAD</term><term>Nitroreductases</term><term>Quinones</term><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines bactériennes</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Thermotoga maritima</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Thermotoga maritima</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Flavine adénine dinucléotide</term><term>Glutarédoxines</term><term>NAD</term><term>Nitroréductases</term><term>Protéines bactériennes</term><term>Quinones</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Catalysis</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Substrate Specificity</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Sites de fixation</term><term>Spécificité du substrat</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Thermotoga maritima NADH:thioredoxin reductase (TmTR) contains FAD and a catalytic disulfide in the active center, and uses a relatively poorly studied physiological oxidant Grx-1-type glutaredoxin. In order to further assess the redox properties of TmTR, we used series of quinoidal and nitroaromatic oxidants with a wide range of single-electron reduction potentials (E(1)7, -0.49-0.09 V). We found that TmTR catalyzed the mixed single- and two-electron reduction of quinones and nitroaromatic compounds, which was much faster than the reduction of Grx-1. The reactivity of both groups of oxidants increased with an increase in their E(1)7, thus pointing to the absence of their structural specificity. The maximal rates of quinone reduction in the steady-state reactions were lower than the maximal rates of reduction of FAD by NADH, obtained in presteady-state experiments. The mixed-type reaction inhibition by NAD(+) was consistent with its competition for a NADH binding site in the oxidized enzyme form, and also with the reoxidation of the reduced enzyme form. The inhibition data yielded a value of the standard potential for TmTR of -0.31±0.03 V at pH 7.0, which may correspond to the FAD/FADH2 redox couple. Overall, the mechanism of quinone- and nitroreductase reactions of T. maritima TR was similar to the previously described mechanism of Arabidopsis thaliana TR, and points to their prooxidant and possibly cytotoxic role. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26098718</PMID><DateCompleted><Year>2016</Year><Month>04</Month><Day>28</Day></DateCompleted><DateRevised><Year>2015</Year><Month>06</Month><Day>29</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1734-154X</ISSN><JournalIssue CitedMedium="Internet"><Volume>62</Volume><Issue>2</Issue><PubDate><Year>2015</Year></PubDate></JournalIssue><Title>Acta biochimica Polonica</Title><ISOAbbreviation>Acta Biochim Pol</ISOAbbreviation></Journal><ArticleTitle>Quinone- and nitroreductase reactions of Thermotoga maritima thioredoxin reductase.</ArticleTitle><Pagination><MedlinePgn>303-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.18388/abp.2015_1003</ELocationID><Abstract><AbstractText>The Thermotoga maritima NADH:thioredoxin reductase (TmTR) contains FAD and a catalytic disulfide in the active center, and uses a relatively poorly studied physiological oxidant Grx-1-type glutaredoxin. In order to further assess the redox properties of TmTR, we used series of quinoidal and nitroaromatic oxidants with a wide range of single-electron reduction potentials (E(1)7, -0.49-0.09 V). We found that TmTR catalyzed the mixed single- and two-electron reduction of quinones and nitroaromatic compounds, which was much faster than the reduction of Grx-1. The reactivity of both groups of oxidants increased with an increase in their E(1)7, thus pointing to the absence of their structural specificity. The maximal rates of quinone reduction in the steady-state reactions were lower than the maximal rates of reduction of FAD by NADH, obtained in presteady-state experiments. The mixed-type reaction inhibition by NAD(+) was consistent with its competition for a NADH binding site in the oxidized enzyme form, and also with the reoxidation of the reduced enzyme form. The inhibition data yielded a value of the standard potential for TmTR of -0.31±0.03 V at pH 7.0, which may correspond to the FAD/FADH2 redox couple. Overall, the mechanism of quinone- and nitroreductase reactions of T. maritima TR was similar to the previously described mechanism of Arabidopsis thaliana TR, and points to their prooxidant and possibly cytotoxic role. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Valiauga</LastName><ForeName>Benjaminas</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry of Vilnius University, LT-08662 Vilnius, Lithuania.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Universite de Lorraine, Interactions Arbres-Microorganismes, UMR1136, F-54500 Vandoeuvre-les-Nancy, France; and INRA, Interactions Arbres-Microorganismes, UMR1136, F-54280 Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials><AffiliationInfo><Affiliation>Universite de Lorraine, Interactions Arbres-Microorganismes, UMR1136, F-54500 Vandoeuvre-les-Nancy, France; and INRA, Interactions Arbres-Microorganismes, UMR1136, F-54280 Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Čėnas</LastName><ForeName>Narimantas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry of Vilnius University, LT-08662 Vilnius, Lithuania.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>06</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>Poland</Country><MedlineTA>Acta Biochim Pol</MedlineTA><NlmUniqueID>14520300R</NlmUniqueID><ISSNLinking>0001-527X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011809">Quinones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0U46U6E8UK</RegistryNumber><NameOfSubstance UI="D009243">NAD</NameOfSubstance></Chemical><Chemical><RegistryNumber>146-14-5</RegistryNumber><NameOfSubstance UI="D005182">Flavin-Adenine Dinucleotide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.7.-</RegistryNumber><NameOfSubstance UI="D009601">Nitroreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005182" MajorTopicYN="N">Flavin-Adenine Dinucleotide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009243" MajorTopicYN="N">NAD</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009601" MajorTopicYN="N">Nitroreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011809" MajorTopicYN="N">Quinones</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020124" MajorTopicYN="N">Thermotoga maritima</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>03</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>04</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>04</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>6</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>6</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>4</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26098718</ArticleId><ArticleId IdType="pii">2015_1003</ArticleId><ArticleId IdType="doi">10.18388/abp.2015_1003</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li><li>Lituanie</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Champenoux</li></settlement><orgName><li>Université de Lorraine</li></orgName></list><tree><country name="Lituanie"><noRegion><name sortKey="Valiauga, Benjaminas" sort="Valiauga, Benjaminas" uniqKey="Valiauga B" first="Benjaminas" last="Valiauga">Benjaminas Valiauga</name></noRegion><name sortKey=" Nas, Narimantas" sort=" Nas, Narimantas" uniqKey=" Nas N" first="Narimantas" last=" Nas">Narimantas Nas</name></country><country name="France"><region name="Grand Est"><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></region><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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