Triiodide reduction by cellobiose:quinone oxidoreductase of Phanerochaete chrysosporium.
Identifieur interne : 000E97 ( Main/Exploration ); précédent : 000E96; suivant : 000E98Triiodide reduction by cellobiose:quinone oxidoreductase of Phanerochaete chrysosporium.
Auteurs : W J Bao [États-Unis] ; V. RenganathanSource :
- FEBS letters [ 0014-5793 ] ; 1991.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Cellobiose, Flavines, Iodures.
- enzymologie : Basidiomycota.
- métabolisme : Carbohydrate dehydrogenases.
- Catalyse, Myeloperoxidase, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Cellobiose, Flavins, Iodides.
- chemical , metabolism : Carbohydrate Dehydrogenases.
- enzymology : Basidiomycota.
- Catalysis, Oxidation-Reduction, Peroxidase.
Abstract
Cellobiose:quinone oxidoreductase (CBQase) in the presence of cellobiose inhibits peroxidase-catalyzed oxidation of iodide to triiodide (I3). This inhibition is due to the two-electron reduction of I3- by CBQase. The apparent Km of I3- for this reaction is 120 microM and the specific activity is 57 mumol.min-1.mg-1. A proposed mechanism for I3- reduction by CBQase involves initial reduction of the flavin moiety by cellobiose to produce a dihydroflavin. This is followed by the substitution of one of the iodine atoms of I3- at the C(4a)-position of dihydroflavin to generate C(4a)-iododihydroflavin and two iodide ions. The C(4a)-iododihydroflavin eliminates HI to regenerate the oxidized CBQase.
DOI: 10.1016/0014-5793(91)80242-u
PubMed: 1847342
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Renganathan</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991</date><idno type="RBID">pubmed:1847342</idno><idno type="pmid">1847342</idno><idno type="doi">10.1016/0014-5793(91)80242-u</idno><idno type="wicri:Area/Main/Corpus">000F26</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000F26</idno><idno type="wicri:Area/Main/Curation">000F26</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000F26</idno><idno type="wicri:Area/Main/Exploration">000F26</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Triiodide reduction by cellobiose:quinone oxidoreductase of Phanerochaete chrysosporium.</title><author><name sortKey="Bao, W J" sort="Bao, W J" uniqKey="Bao W" first="W J" last="Bao">W J Bao</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemical and Biological Sciences, Oregon Graduate Institute of Science and Technology, Beaverton, OR 97006-1999.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Oregon</region></placeName><wicri:cityArea>Department of Chemical and Biological Sciences, Oregon Graduate Institute of Science and Technology, Beaverton</wicri:cityArea></affiliation></author><author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Carbohydrate Dehydrogenases (metabolism)</term><term>Catalysis (MeSH)</term><term>Cellobiose (chemistry)</term><term>Flavins (chemistry)</term><term>Iodides (chemistry)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidase (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (enzymologie)</term><term>Carbohydrate dehydrogenases (métabolisme)</term><term>Catalyse (MeSH)</term><term>Cellobiose (composition chimique)</term><term>Flavines (composition chimique)</term><term>Iodures (composition chimique)</term><term>Myeloperoxidase (MeSH)</term><term>Oxydoréduction (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cellobiose</term><term>Flavins</term><term>Iodides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbohydrate Dehydrogenases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellobiose</term><term>Flavines</term><term>Iodures</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carbohydrate dehydrogenases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>Oxidation-Reduction</term><term>Peroxidase</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Myeloperoxidase</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cellobiose:quinone oxidoreductase (CBQase) in the presence of cellobiose inhibits peroxidase-catalyzed oxidation of iodide to triiodide (I3). This inhibition is due to the two-electron reduction of I3- by CBQase. The apparent Km of I3- for this reaction is 120 microM and the specific activity is 57 mumol.min-1.mg-1. A proposed mechanism for I3- reduction by CBQase involves initial reduction of the flavin moiety by cellobiose to produce a dihydroflavin. This is followed by the substitution of one of the iodine atoms of I3- at the C(4a)-position of dihydroflavin to generate C(4a)-iododihydroflavin and two iodide ions. The C(4a)-iododihydroflavin eliminates HI to regenerate the oxidized CBQase.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1847342</PMID><DateCompleted><Year>1991</Year><Month>03</Month><Day>27</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>279</Volume><Issue>1</Issue><PubDate><Year>1991</Year><Month>Feb</Month><Day>11</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Triiodide reduction by cellobiose:quinone oxidoreductase of Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>30-2</MedlinePgn></Pagination><Abstract><AbstractText>Cellobiose:quinone oxidoreductase (CBQase) in the presence of cellobiose inhibits peroxidase-catalyzed oxidation of iodide to triiodide (I3). This inhibition is due to the two-electron reduction of I3- by CBQase. The apparent Km of I3- for this reaction is 120 microM and the specific activity is 57 mumol.min-1.mg-1. A proposed mechanism for I3- reduction by CBQase involves initial reduction of the flavin moiety by cellobiose to produce a dihydroflavin. This is followed by the substitution of one of the iodine atoms of I3- at the C(4a)-position of dihydroflavin to generate C(4a)-iododihydroflavin and two iodide ions. The C(4a)-iododihydroflavin eliminates HI to regenerate the oxidized CBQase.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bao</LastName><ForeName>W J</ForeName><Initials>WJ</Initials><AffiliationInfo><Affiliation>Department of Chemical and Biological Sciences, Oregon Graduate Institute of Science and Technology, Beaverton, OR 97006-1999.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Renganathan</LastName><ForeName>V</ForeName><Initials>V</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005415">Flavins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007454">Iodides</NameOfSubstance></Chemical><Chemical><RegistryNumber>16462-44-5</RegistryNumber><NameOfSubstance UI="D002475">Cellobiose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D002237">Carbohydrate Dehydrogenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.99.18</RegistryNumber><NameOfSubstance UI="C019859">cellobiose-quinone oxidoreductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.7</RegistryNumber><NameOfSubstance UI="D009195">Peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002475" MajorTopicYN="N">Cellobiose</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005415" MajorTopicYN="N">Flavins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007454" MajorTopicYN="N">Iodides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009195" MajorTopicYN="N">Peroxidase</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>2</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>2</Month><Day>11</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>2</Month><Day>11</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1847342</ArticleId><ArticleId IdType="doi">10.1016/0014-5793(91)80242-u</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Oregon</li></region></list><tree><noCountry><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></noCountry><country name="États-Unis"><region name="Oregon"><name sortKey="Bao, W J" sort="Bao, W J" uniqKey="Bao W" first="W J" last="Bao">W J Bao</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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