Reductions catalyzed by a quinone and peroxidases from Phanerochaete chrysosporium.
Identifieur interne : 001D30 ( Main/Exploration ); précédent : 001D29; suivant : 001D31Reductions catalyzed by a quinone and peroxidases from Phanerochaete chrysosporium.
Auteurs : S J Rasmussen [États-Unis] ; N. Chung ; A. Khindaria ; T A Grover ; S D AustSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1995.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Benzoquinones, Champignons, Cytochromes de type c, Peroxidases.
- synthèse chimique : Benzoquinones.
- Oxydoréduction, Spectroscopie de résonance de spin électronique.
English descriptors
- KwdEn :
- MESH :
- chemical , chemical synthesis : Benzoquinones.
- chemical , metabolism : Benzoquinones, Cytochrome c Group, Peroxidases.
- metabolism : Fungi.
- Electron Spin Resonance Spectroscopy, Oxidation-Reduction.
Abstract
A quinone produced from veratryl alcohol by lignin peroxidase from the white rot fungus Phanerochaete chrysosporium was tested for its ability to mediate reduction. The quinone (2-hydroxymethyl-5-methoxy-1,4-benzoquinone), reduced chemically or by cellobiose:quinone reductase isolated from cultures of the fungus, mediated the reduction of cytochrome c in reactions containing either Mn(III), a manganese-dependent peroxidase, Mn(II) and H2O2, or lignin peroxidase and H2O2. Formation of the semiquinone, the species responsible for reducing cytochrome c, was observed by electron spin resonance spectroscopy in these reactions. The production of the quinone was observed in the extracellular fraction of cultures grown under nutrient nitrogen-deficient conditions (2.4 mM ammonium tartrate) for over 10 days, starting on Day 2, but not under nutrient nitrogen-sufficient conditions. These results suggest that a quinone produced by lignin peroxidase can serve as a physiological mediator of reductive reactions catalyzed by the fungal peroxidases.
DOI: 10.1016/0003-9861(95)90006-3
PubMed: 7625830
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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The quinone (2-hydroxymethyl-5-methoxy-1,4-benzoquinone), reduced chemically or by cellobiose:quinone reductase isolated from cultures of the fungus, mediated the reduction of cytochrome c in reactions containing either Mn(III), a manganese-dependent peroxidase, Mn(II) and H2O2, or lignin peroxidase and H2O2. Formation of the semiquinone, the species responsible for reducing cytochrome c, was observed by electron spin resonance spectroscopy in these reactions. The production of the quinone was observed in the extracellular fraction of cultures grown under nutrient nitrogen-deficient conditions (2.4 mM ammonium tartrate) for over 10 days, starting on Day 2, but not under nutrient nitrogen-sufficient conditions. These results suggest that a quinone produced by lignin peroxidase can serve as a physiological mediator of reductive reactions catalyzed by the fungal peroxidases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7625830</PMID><DateCompleted><Year>1995</Year><Month>08</Month><Day>28</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>29</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>320</Volume><Issue>2</Issue><PubDate><Year>1995</Year><Month>Jul</Month><Day>10</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Reductions catalyzed by a quinone and peroxidases from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>243-9</MedlinePgn></Pagination><Abstract><AbstractText>A quinone produced from veratryl alcohol by lignin peroxidase from the white rot fungus Phanerochaete chrysosporium was tested for its ability to mediate reduction. The quinone (2-hydroxymethyl-5-methoxy-1,4-benzoquinone), reduced chemically or by cellobiose:quinone reductase isolated from cultures of the fungus, mediated the reduction of cytochrome c in reactions containing either Mn(III), a manganese-dependent peroxidase, Mn(II) and H2O2, or lignin peroxidase and H2O2. Formation of the semiquinone, the species responsible for reducing cytochrome c, was observed by electron spin resonance spectroscopy in these reactions. The production of the quinone was observed in the extracellular fraction of cultures grown under nutrient nitrogen-deficient conditions (2.4 mM ammonium tartrate) for over 10 days, starting on Day 2, but not under nutrient nitrogen-sufficient conditions. These results suggest that a quinone produced by lignin peroxidase can serve as a physiological mediator of reductive reactions catalyzed by the fungal peroxidases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rasmussen</LastName><ForeName>S J</ForeName><Initials>SJ</Initials><AffiliationInfo><Affiliation>Utah State University, Biotechnology Center, Logan 84322-4705, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chung</LastName><ForeName>N</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Khindaria</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Grover</LastName><ForeName>T A</ForeName><Initials>TA</Initials></Author><Author ValidYN="Y"><LastName>Aust</LastName><ForeName>S D</ForeName><Initials>SD</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>ES04922</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016227">Benzoquinones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003574">Cytochrome c Group</NameOfSubstance></Chemical><Chemical><RegistryNumber>3T006GV98U</RegistryNumber><NameOfSubstance UI="C004532">quinone</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D016227" MajorTopicYN="N">Benzoquinones</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003574" MajorTopicYN="N">Cytochrome c Group</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1995</Year><Month>7</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1995</Year><Month>7</Month><Day>10</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1995</Year><Month>7</Month><Day>10</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">7625830</ArticleId><ArticleId IdType="pii">0003-9861(95)90006-3</ArticleId><ArticleId IdType="doi">10.1016/0003-9861(95)90006-3</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name><name sortKey="Chung, N" sort="Chung, N" uniqKey="Chung N" first="N" last="Chung">N. Chung</name><name sortKey="Grover, T A" sort="Grover, T A" uniqKey="Grover T" first="T A" last="Grover">T A Grover</name><name sortKey="Khindaria, A" sort="Khindaria, A" uniqKey="Khindaria A" first="A" last="Khindaria">A. Khindaria</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Rasmussen, S J" sort="Rasmussen, S J" uniqKey="Rasmussen S" first="S J" last="Rasmussen">S J Rasmussen</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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