Glyoxal oxidase from Phanerochaete chrysosporium is a new radical-copper oxidase.
Identifieur interne : 000C48 ( Main/Exploration ); précédent : 000C47; suivant : 000C49Glyoxal oxidase from Phanerochaete chrysosporium is a new radical-copper oxidase.
Auteurs : M M Whittaker [États-Unis] ; P J Kersten ; N. Nakamura ; J. Sanders-Loehr ; E S Schweizer ; J W WhittakerSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1996.
Descripteurs français
- KwdFr :
- MESH :
- classification : Oxidoreductases.
- enzymologie : Basidiomycota.
- métabolisme : Alcohol oxidoreductases, Oxidoreductases.
- Analyse spectrale Raman, Animaux, Oxydoréduction, Radicaux libres, Spectroscopie de résonance de spin électronique.
English descriptors
- KwdEn :
- MESH :
- chemical , classification : Oxidoreductases.
- chemical , metabolism : Alcohol Oxidoreductases, Oxidoreductases.
- enzymology : Basidiomycota.
- Animals, Electron Spin Resonance Spectroscopy, Free Radicals, Oxidation-Reduction, Spectrum Analysis, Raman.
Abstract
A free radical-coupled copper complex has been identified as the catalytic structure in the active site of glyoxal oxidase from Phanerochaete chrysosporium based on a combination of spectroscopic and biochemical studies. The native (inactive) enzyme is activated by oxidants leading to the elimination of the cupric EPR signal consistent with formation of an antiferromagnetically coupled radical-copper complex. Oxidation also leads to the appearance of a substoichiometric free radical EPR signal with an average g value (gav = 2.0055) characteristic of phenoxyl tau-radicals arising from a minority apoenzyme fraction. Optical absorption, CD, and spectroelectrochemical measurements on the active enzyme reveal complex spectra extending into the near IR and define the redox potential for radical formation (E 1/2 = 0.64 V versus NHE, pH 7.0). Resonance Raman spectra have identified the signature of a modified (cysteinyl-tyrosine) phenoxyl in the vibrational spectra of the active complex. This radical-copper motif has previously been found only in galactose oxidase, with which glyoxal oxidase shares many properties despite lacking obvious sequence identity, and catalyzing a distinct reaction. The enzymes thus represent members of a growing class of free radical metalloenzymes based on the radical-copper catalytic motif and appear to represent functional variants that have evolved to distinct catalytic roles.
DOI: 10.1074/jbc.271.2.681
PubMed: 8557673
Affiliations:
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Nakamura</name></author><author><name sortKey="Sanders Loehr, J" sort="Sanders Loehr, J" uniqKey="Sanders Loehr J" first="J" last="Sanders-Loehr">J. Sanders-Loehr</name></author><author><name sortKey="Schweizer, E S" sort="Schweizer, E S" uniqKey="Schweizer E" first="E S" last="Schweizer">E S Schweizer</name></author><author><name sortKey="Whittaker, J W" sort="Whittaker, J W" uniqKey="Whittaker J" first="J W" last="Whittaker">J W Whittaker</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1996">1996</date><idno type="RBID">pubmed:8557673</idno><idno type="pmid">8557673</idno><idno type="doi">10.1074/jbc.271.2.681</idno><idno type="wicri:Area/Main/Corpus">000C69</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C69</idno><idno type="wicri:Area/Main/Curation">000C69</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C69</idno><idno type="wicri:Area/Main/Exploration">000C69</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Glyoxal oxidase from Phanerochaete chrysosporium is a new radical-copper oxidase.</title><author><name sortKey="Whittaker, M M" sort="Whittaker, M M" uniqKey="Whittaker M" first="M M" last="Whittaker">M M Whittaker</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213-3890, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213-3890</wicri:regionArea><orgName type="university">Université Carnegie-Mellon</orgName><placeName><settlement type="city">Pittsburgh</settlement><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Kersten, P J" sort="Kersten, P J" uniqKey="Kersten P" first="P J" last="Kersten">P J Kersten</name></author><author><name sortKey="Nakamura, N" sort="Nakamura, N" uniqKey="Nakamura N" first="N" last="Nakamura">N. Nakamura</name></author><author><name sortKey="Sanders Loehr, J" sort="Sanders Loehr, J" uniqKey="Sanders Loehr J" first="J" last="Sanders-Loehr">J. Sanders-Loehr</name></author><author><name sortKey="Schweizer, E S" sort="Schweizer, E S" uniqKey="Schweizer E" first="E S" last="Schweizer">E S Schweizer</name></author><author><name sortKey="Whittaker, J W" sort="Whittaker, J W" uniqKey="Whittaker J" first="J W" last="Whittaker">J W Whittaker</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1996" type="published">1996</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (metabolism)</term><term>Animals (MeSH)</term><term>Basidiomycota (enzymology)</term><term>Electron Spin Resonance Spectroscopy (MeSH)</term><term>Free Radicals (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (classification)</term><term>Oxidoreductases (metabolism)</term><term>Spectrum Analysis, Raman (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcohol oxidoreductases (métabolisme)</term><term>Analyse spectrale Raman (MeSH)</term><term>Animaux (MeSH)</term><term>Basidiomycota (enzymologie)</term><term>Oxidoreductases (classification)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Radicaux libres (MeSH)</term><term>Spectroscopie de résonance de spin électronique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="fr"><term>Oxidoreductases</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>Alcohol oxidoreductases</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Electron Spin Resonance Spectroscopy</term><term>Free Radicals</term><term>Oxidation-Reduction</term><term>Spectrum Analysis, Raman</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse spectrale Raman</term><term>Animaux</term><term>Oxydoréduction</term><term>Radicaux libres</term><term>Spectroscopie de résonance de spin électronique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A free radical-coupled copper complex has been identified as the catalytic structure in the active site of glyoxal oxidase from Phanerochaete chrysosporium based on a combination of spectroscopic and biochemical studies. The native (inactive) enzyme is activated by oxidants leading to the elimination of the cupric EPR signal consistent with formation of an antiferromagnetically coupled radical-copper complex. Oxidation also leads to the appearance of a substoichiometric free radical EPR signal with an average g value (gav = 2.0055) characteristic of phenoxyl tau-radicals arising from a minority apoenzyme fraction. Optical absorption, CD, and spectroelectrochemical measurements on the active enzyme reveal complex spectra extending into the near IR and define the redox potential for radical formation (E 1/2 = 0.64 V versus NHE, pH 7.0). Resonance Raman spectra have identified the signature of a modified (cysteinyl-tyrosine) phenoxyl in the vibrational spectra of the active complex. This radical-copper motif has previously been found only in galactose oxidase, with which glyoxal oxidase shares many properties despite lacking obvious sequence identity, and catalyzing a distinct reaction. The enzymes thus represent members of a growing class of free radical metalloenzymes based on the radical-copper catalytic motif and appear to represent functional variants that have evolved to distinct catalytic roles.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8557673</PMID><DateCompleted><Year>1996</Year><Month>02</Month><Day>26</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>271</Volume><Issue>2</Issue><PubDate><Year>1996</Year><Month>Jan</Month><Day>12</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Glyoxal oxidase from Phanerochaete chrysosporium is a new radical-copper oxidase.</ArticleTitle><Pagination><MedlinePgn>681-7</MedlinePgn></Pagination><Abstract><AbstractText>A free radical-coupled copper complex has been identified as the catalytic structure in the active site of glyoxal oxidase from Phanerochaete chrysosporium based on a combination of spectroscopic and biochemical studies. The native (inactive) enzyme is activated by oxidants leading to the elimination of the cupric EPR signal consistent with formation of an antiferromagnetically coupled radical-copper complex. Oxidation also leads to the appearance of a substoichiometric free radical EPR signal with an average g value (gav = 2.0055) characteristic of phenoxyl tau-radicals arising from a minority apoenzyme fraction. Optical absorption, CD, and spectroelectrochemical measurements on the active enzyme reveal complex spectra extending into the near IR and define the redox potential for radical formation (E 1/2 = 0.64 V versus NHE, pH 7.0). Resonance Raman spectra have identified the signature of a modified (cysteinyl-tyrosine) phenoxyl in the vibrational spectra of the active complex. This radical-copper motif has previously been found only in galactose oxidase, with which glyoxal oxidase shares many properties despite lacking obvious sequence identity, and catalyzing a distinct reaction. The enzymes thus represent members of a growing class of free radical metalloenzymes based on the radical-copper catalytic motif and appear to represent functional variants that have evolved to distinct catalytic roles.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Whittaker</LastName><ForeName>M M</ForeName><Initials>MM</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213-3890, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kersten</LastName><ForeName>P J</ForeName><Initials>PJ</Initials></Author><Author ValidYN="Y"><LastName>Nakamura</LastName><ForeName>N</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Sanders-Loehr</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Schweizer</LastName><ForeName>E S</ForeName><Initials>ES</Initials></Author><Author ValidYN="Y"><LastName>Whittaker</LastName><ForeName>J W</ForeName><Initials>JW</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM 18865</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM 46749</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005609">Free Radicals</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.-</RegistryNumber><NameOfSubstance UI="C052371">glyoxal oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.16.-</RegistryNumber><NameOfSubstance UI="C024748">copper oxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000429" MajorTopicYN="N">Alcohol Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005609" MajorTopicYN="N">Free Radicals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013059" MajorTopicYN="N">Spectrum Analysis, Raman</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year><Month>1</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1996</Year><Month>1</Month><Day>12</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1996</Year><Month>1</Month><Day>12</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8557673</ArticleId><ArticleId IdType="doi">10.1074/jbc.271.2.681</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Pennsylvanie</li></region><settlement><li>Pittsburgh</li></settlement><orgName><li>Université Carnegie-Mellon</li></orgName></list><tree><noCountry><name sortKey="Kersten, P J" sort="Kersten, P J" uniqKey="Kersten P" first="P J" last="Kersten">P J Kersten</name><name sortKey="Nakamura, N" sort="Nakamura, N" uniqKey="Nakamura N" first="N" last="Nakamura">N. Nakamura</name><name sortKey="Sanders Loehr, J" sort="Sanders Loehr, J" uniqKey="Sanders Loehr J" first="J" last="Sanders-Loehr">J. Sanders-Loehr</name><name sortKey="Schweizer, E S" sort="Schweizer, E S" uniqKey="Schweizer E" first="E S" last="Schweizer">E S Schweizer</name><name sortKey="Whittaker, J W" sort="Whittaker, J W" uniqKey="Whittaker J" first="J W" last="Whittaker">J W Whittaker</name></noCountry><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Whittaker, M M" sort="Whittaker, M M" uniqKey="Whittaker M" first="M M" last="Whittaker">M M Whittaker</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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