Is cellobiose oxidase from Phanerochaete chrysosporium a one-electron reductase?
Identifieur interne : 000D87 ( Main/Corpus ); précédent : 000D86; suivant : 000D88Is cellobiose oxidase from Phanerochaete chrysosporium a one-electron reductase?
Auteurs : G. Henriksson ; G. Johansson ; G. PetterssonSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 1993.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Carbohydrate Dehydrogenases, Heme.
- enzymology : Fungi.
- Electron Transport, Models, Chemical.
Abstract
The heme domain of cellobiose oxidase (CBO) from Phanerochaete chrysosporium increases the rate of electron transfer to one-electron acceptors. This conclusion was drawn from comparisons of the rates of reduction of 3,5-t-butyl-o-benzoquinone, triiodide ion, cytochrome c and ferricyanide by intact CBO, FAD fragment and CBO with the heme inactivated by cyanide. The oxidation of cellobiose produced hydrogen peroxide, but the enzyme disturbs peroxidase-based assays by reduction of the product or by direct interaction with the peroxidase. CBO can also degrade hydrogen peroxide in the presence of cellobiose. The 1,2,4,5-tetramethoxybenzene cation radical was rapidly reduced by CBO.
DOI: 10.1016/0005-2728(93)90171-b
PubMed: 8369336
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pubmed:8369336Le document en format XML
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Pettersson</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8369336</idno><idno type="pmid">8369336</idno><idno type="doi">10.1016/0005-2728(93)90171-b</idno><idno type="wicri:Area/Main/Corpus">000D87</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D87</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Is cellobiose oxidase from Phanerochaete chrysosporium a one-electron reductase?</title><author><name sortKey="Henriksson, G" sort="Henriksson, G" uniqKey="Henriksson G" first="G" last="Henriksson">G. Henriksson</name><affiliation><nlm:affiliation>Department of Biochemistry, University of Uppsala, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Johansson, G" sort="Johansson, G" uniqKey="Johansson G" first="G" last="Johansson">G. Johansson</name></author><author><name sortKey="Pettersson, G" sort="Pettersson, G" uniqKey="Pettersson G" first="G" last="Pettersson">G. Pettersson</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carbohydrate Dehydrogenases (chemistry)</term><term>Electron Transport (MeSH)</term><term>Fungi (enzymology)</term><term>Heme (chemistry)</term><term>Models, Chemical (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Heme</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Transport</term><term>Models, Chemical</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The heme domain of cellobiose oxidase (CBO) from Phanerochaete chrysosporium increases the rate of electron transfer to one-electron acceptors. This conclusion was drawn from comparisons of the rates of reduction of 3,5-t-butyl-o-benzoquinone, triiodide ion, cytochrome c and ferricyanide by intact CBO, FAD fragment and CBO with the heme inactivated by cyanide. The oxidation of cellobiose produced hydrogen peroxide, but the enzyme disturbs peroxidase-based assays by reduction of the product or by direct interaction with the peroxidase. CBO can also degrade hydrogen peroxide in the presence of cellobiose. The 1,2,4,5-tetramethoxybenzene cation radical was rapidly reduced by CBO.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8369336</PMID><DateCompleted><Year>1993</Year><Month>10</Month><Day>12</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1144</Volume><Issue>2</Issue><PubDate><Year>1993</Year><Month>Sep</Month><Day>13</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Is cellobiose oxidase from Phanerochaete chrysosporium a one-electron reductase?</ArticleTitle><Pagination><MedlinePgn>184-90</MedlinePgn></Pagination><Abstract><AbstractText>The heme domain of cellobiose oxidase (CBO) from Phanerochaete chrysosporium increases the rate of electron transfer to one-electron acceptors. This conclusion was drawn from comparisons of the rates of reduction of 3,5-t-butyl-o-benzoquinone, triiodide ion, cytochrome c and ferricyanide by intact CBO, FAD fragment and CBO with the heme inactivated by cyanide. The oxidation of cellobiose produced hydrogen peroxide, but the enzyme disturbs peroxidase-based assays by reduction of the product or by direct interaction with the peroxidase. CBO can also degrade hydrogen peroxide in the presence of cellobiose. The 1,2,4,5-tetramethoxybenzene cation radical was rapidly reduced by CBO.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Henriksson</LastName><ForeName>G</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Johansson</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Pettersson</LastName><ForeName>G</ForeName><Initials>G</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D002237">Carbohydrate Dehydrogenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.-</RegistryNumber><NameOfSubstance UI="C019858">cellobiose oxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="N">Models, Chemical</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1993</Year><Month>9</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1993</Year><Month>9</Month><Day>13</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1993</Year><Month>9</Month><Day>13</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8369336</ArticleId><ArticleId IdType="pii">0005-2728(93)90171-B</ArticleId><ArticleId IdType="doi">10.1016/0005-2728(93)90171-b</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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