Spectral characterization of diarylpropane oxygenase, a novel peroxide-dependent, lignin-degrading heme enzyme.
Identifieur interne : 001054 ( Main/Curation ); précédent : 001053; suivant : 001055Spectral characterization of diarylpropane oxygenase, a novel peroxide-dependent, lignin-degrading heme enzyme.
Auteurs : L A Andersson ; V. Renganathan ; A A Chiu ; T M Loehr ; M H GoldSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1985.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Basidiomycota.
- métabolisme : Oxygénases.
- pharmacologie : Peroxyde d'hydrogène.
- Analyse spectrale Raman, Chimie, Lignine, Peroxidases, Phénomènes chimiques, Spectroscopie de résonance de spin électronique.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Oxygenases.
- chemical , pharmacology : Hydrogen Peroxide.
- enzymology : Basidiomycota.
- Chemical Phenomena, Chemistry, Electron Spin Resonance Spectroscopy, Lignin, Peroxidases, Spectrum Analysis, Raman.
Abstract
Diarylpropane oxygenase, an H2O2-dependent lignin-degrading enzyme from the basidiomycete fungus Phanerochaete chrysosporium, catalyzes the oxygenation of various lignin model compounds with incorporation of a single atom of dioxygen (O2). Diarylpropane oxygenase is also capable of oxidizing some alcohols to aldehydes and/or ketones. This enzyme (Mr = 41,000) contains a single iron protoporphyrin IX prosthetic group. Previous studies revealed that the Soret maximum of the ferrous-CO complex of diarylpropane oxygenase is at approximately 420 nm, as in ferrous-CO myoglobin (Mb), and not like the approximately 450 nm absorption of the CO complex of the ubiquitous heme monooxygenase, cytochrome P-450. This spectral difference between two functionally similar heme enzymes is of interest. To elucidate the structural requirements for heme iron-based oxygenase reactions, we have compared the electronic absorption, EPR, and resonance Raman (RR) spectral properties of diarylpropane oxygenase with those of other heme proteins and enzymes of known axial ligation. The absorption spectra of native (ferric), cyano, and ferrous diarylpropane oxygenase closely resemble those of the analogous myoglobin complexes. The EPR g values of native diarylpropane oxygenase, 5.83 and 1.99, also agree well with those of aquometMb. The RR spectra of ferric diarylpropane oxygenase have their spin- and oxidation-state marker bands at frequencies analogous to those of aquometMb and indicate a high-spin, hexacoordinate ferric iron. The RR spectra of ferrous diarylpropane oxygenase have frequencies analogous to those of deoxy-Mb that suggest a high-spin, pentacoordinate Fe(II) in the reduced form. The RR spectra of both ferric and ferrous diarylpropane oxygenase are less similar to those of horseradish peroxidase, catalase, or cytochrome c peroxidase and are clearly distinct from those of P-450. These observations suggest that the fifth ligand to the heme iron of diarylpropane oxygenase is a neutral histidine and that the iron environment must resemble that of the oxygen transport protein, myoglobin, rather than that of the peroxidases, catalase, or P-450. Given the functional similarity between diarylpropane oxygenase and P-450, this work implies that the mechanism of oxygen insertion for the two systems is different.
PubMed: 2987213
Links toward previous steps (curation, corpus...)
- to stream Main, to step Corpus: Pour aller vers cette notice dans l'étape Curation :001054
Links to Exploration step
pubmed:2987213Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Spectral characterization of diarylpropane oxygenase, a novel peroxide-dependent, lignin-degrading heme enzyme.</title>
<author><name sortKey="Andersson, L A" sort="Andersson, L A" uniqKey="Andersson L" first="L A" last="Andersson">L A Andersson</name>
</author>
<author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name>
</author>
<author><name sortKey="Chiu, A A" sort="Chiu, A A" uniqKey="Chiu A" first="A A" last="Chiu">A A Chiu</name>
</author>
<author><name sortKey="Loehr, T M" sort="Loehr, T M" uniqKey="Loehr T" first="T M" last="Loehr">T M Loehr</name>
</author>
<author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="1985">1985</date>
<idno type="RBID">pubmed:2987213</idno>
<idno type="pmid">2987213</idno>
<idno type="wicri:Area/Main/Corpus">001054</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001054</idno>
<idno type="wicri:Area/Main/Curation">001054</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001054</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Spectral characterization of diarylpropane oxygenase, a novel peroxide-dependent, lignin-degrading heme enzyme.</title>
<author><name sortKey="Andersson, L A" sort="Andersson, L A" uniqKey="Andersson L" first="L A" last="Andersson">L A Andersson</name>
</author>
<author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name>
</author>
<author><name sortKey="Chiu, A A" sort="Chiu, A A" uniqKey="Chiu A" first="A A" last="Chiu">A A Chiu</name>
</author>
<author><name sortKey="Loehr, T M" sort="Loehr, T M" uniqKey="Loehr T" first="T M" last="Loehr">T M Loehr</name>
</author>
<author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name>
</author>
</analytic>
<series><title level="j">The Journal of biological chemistry</title>
<idno type="ISSN">0021-9258</idno>
<imprint><date when="1985" type="published">1985</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term>
<term>Chemical Phenomena (MeSH)</term>
<term>Chemistry (MeSH)</term>
<term>Electron Spin Resonance Spectroscopy (MeSH)</term>
<term>Hydrogen Peroxide (pharmacology)</term>
<term>Lignin (MeSH)</term>
<term>Oxygenases (metabolism)</term>
<term>Peroxidases (MeSH)</term>
<term>Spectrum Analysis, Raman (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Analyse spectrale Raman (MeSH)</term>
<term>Basidiomycota (enzymologie)</term>
<term>Chimie (MeSH)</term>
<term>Lignine (MeSH)</term>
<term>Oxygénases (métabolisme)</term>
<term>Peroxidases (MeSH)</term>
<term>Peroxyde d'hydrogène (pharmacologie)</term>
<term>Phénomènes chimiques (MeSH)</term>
<term>Spectroscopie de résonance de spin électronique (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxygenases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Hydrogen Peroxide</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>Oxygénases</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Peroxyde d'hydrogène</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Chemical Phenomena</term>
<term>Chemistry</term>
<term>Electron Spin Resonance Spectroscopy</term>
<term>Lignin</term>
<term>Peroxidases</term>
<term>Spectrum Analysis, Raman</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Analyse spectrale Raman</term>
<term>Chimie</term>
<term>Lignine</term>
<term>Peroxidases</term>
<term>Phénomènes chimiques</term>
<term>Spectroscopie de résonance de spin électronique</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Diarylpropane oxygenase, an H2O2-dependent lignin-degrading enzyme from the basidiomycete fungus Phanerochaete chrysosporium, catalyzes the oxygenation of various lignin model compounds with incorporation of a single atom of dioxygen (O2). Diarylpropane oxygenase is also capable of oxidizing some alcohols to aldehydes and/or ketones. This enzyme (Mr = 41,000) contains a single iron protoporphyrin IX prosthetic group. Previous studies revealed that the Soret maximum of the ferrous-CO complex of diarylpropane oxygenase is at approximately 420 nm, as in ferrous-CO myoglobin (Mb), and not like the approximately 450 nm absorption of the CO complex of the ubiquitous heme monooxygenase, cytochrome P-450. This spectral difference between two functionally similar heme enzymes is of interest. To elucidate the structural requirements for heme iron-based oxygenase reactions, we have compared the electronic absorption, EPR, and resonance Raman (RR) spectral properties of diarylpropane oxygenase with those of other heme proteins and enzymes of known axial ligation. The absorption spectra of native (ferric), cyano, and ferrous diarylpropane oxygenase closely resemble those of the analogous myoglobin complexes. The EPR g values of native diarylpropane oxygenase, 5.83 and 1.99, also agree well with those of aquometMb. The RR spectra of ferric diarylpropane oxygenase have their spin- and oxidation-state marker bands at frequencies analogous to those of aquometMb and indicate a high-spin, hexacoordinate ferric iron. The RR spectra of ferrous diarylpropane oxygenase have frequencies analogous to those of deoxy-Mb that suggest a high-spin, pentacoordinate Fe(II) in the reduced form. The RR spectra of both ferric and ferrous diarylpropane oxygenase are less similar to those of horseradish peroxidase, catalase, or cytochrome c peroxidase and are clearly distinct from those of P-450. These observations suggest that the fifth ligand to the heme iron of diarylpropane oxygenase is a neutral histidine and that the iron environment must resemble that of the oxygen transport protein, myoglobin, rather than that of the peroxidases, catalase, or P-450. Given the functional similarity between diarylpropane oxygenase and P-450, this work implies that the mechanism of oxygen insertion for the two systems is different.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2987213</PMID>
<DateCompleted><Year>1985</Year>
<Month>06</Month>
<Day>27</Day>
</DateCompleted>
<DateRevised><Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN>
<JournalIssue CitedMedium="Print"><Volume>260</Volume>
<Issue>10</Issue>
<PubDate><Year>1985</Year>
<Month>May</Month>
<Day>25</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J Biol Chem</ISOAbbreviation>
</Journal>
<ArticleTitle>Spectral characterization of diarylpropane oxygenase, a novel peroxide-dependent, lignin-degrading heme enzyme.</ArticleTitle>
<Pagination><MedlinePgn>6080-7</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Diarylpropane oxygenase, an H2O2-dependent lignin-degrading enzyme from the basidiomycete fungus Phanerochaete chrysosporium, catalyzes the oxygenation of various lignin model compounds with incorporation of a single atom of dioxygen (O2). Diarylpropane oxygenase is also capable of oxidizing some alcohols to aldehydes and/or ketones. This enzyme (Mr = 41,000) contains a single iron protoporphyrin IX prosthetic group. Previous studies revealed that the Soret maximum of the ferrous-CO complex of diarylpropane oxygenase is at approximately 420 nm, as in ferrous-CO myoglobin (Mb), and not like the approximately 450 nm absorption of the CO complex of the ubiquitous heme monooxygenase, cytochrome P-450. This spectral difference between two functionally similar heme enzymes is of interest. To elucidate the structural requirements for heme iron-based oxygenase reactions, we have compared the electronic absorption, EPR, and resonance Raman (RR) spectral properties of diarylpropane oxygenase with those of other heme proteins and enzymes of known axial ligation. The absorption spectra of native (ferric), cyano, and ferrous diarylpropane oxygenase closely resemble those of the analogous myoglobin complexes. The EPR g values of native diarylpropane oxygenase, 5.83 and 1.99, also agree well with those of aquometMb. The RR spectra of ferric diarylpropane oxygenase have their spin- and oxidation-state marker bands at frequencies analogous to those of aquometMb and indicate a high-spin, hexacoordinate ferric iron. The RR spectra of ferrous diarylpropane oxygenase have frequencies analogous to those of deoxy-Mb that suggest a high-spin, pentacoordinate Fe(II) in the reduced form. The RR spectra of both ferric and ferrous diarylpropane oxygenase are less similar to those of horseradish peroxidase, catalase, or cytochrome c peroxidase and are clearly distinct from those of P-450. These observations suggest that the fifth ligand to the heme iron of diarylpropane oxygenase is a neutral histidine and that the iron environment must resemble that of the oxygen transport protein, myoglobin, rather than that of the peroxidases, catalase, or P-450. Given the functional similarity between diarylpropane oxygenase and P-450, this work implies that the mechanism of oxygen insertion for the two systems is different.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Andersson</LastName>
<ForeName>L A</ForeName>
<Initials>LA</Initials>
</Author>
<Author ValidYN="Y"><LastName>Renganathan</LastName>
<ForeName>V</ForeName>
<Initials>V</Initials>
</Author>
<Author ValidYN="Y"><LastName>Chiu</LastName>
<ForeName>A A</ForeName>
<Initials>AA</Initials>
</Author>
<Author ValidYN="Y"><LastName>Loehr</LastName>
<ForeName>T M</ForeName>
<Initials>TM</Initials>
</Author>
<Author ValidYN="Y"><LastName>Gold</LastName>
<ForeName>M H</ForeName>
<Initials>MH</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 34468</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType>
<PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</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>9005-53-2</RegistryNumber>
<NameOfSubstance UI="D008031">Lignin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>BBX060AN9V</RegistryNumber>
<NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber>
<NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber>
<NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.13.-</RegistryNumber>
<NameOfSubstance UI="D010105">Oxygenases</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055598" MajorTopicYN="N">Chemical Phenomena</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002621" MajorTopicYN="N">Chemistry</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010105" MajorTopicYN="Y">Oxygenases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010544" MajorTopicYN="Y">Peroxidases</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013059" MajorTopicYN="N">Spectrum Analysis, Raman</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1985</Year>
<Month>5</Month>
<Day>25</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>1985</Year>
<Month>5</Month>
<Day>25</Day>
<Hour>0</Hour>
<Minute>1</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>1985</Year>
<Month>5</Month>
<Day>25</Day>
<Hour>0</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">2987213</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001054 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Curation/biblio.hfd -nk 001054 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Bois |area= PhanerochaeteV1 |flux= Main |étape= Curation |type= RBID |clé= pubmed:2987213 |texte= Spectral characterization of diarylpropane oxygenase, a novel peroxide-dependent, lignin-degrading heme enzyme. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Curation/RBID.i -Sk "pubmed:2987213" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Curation/biblio.hfd \ | NlmPubMed2Wicri -a PhanerochaeteV1
![]() | This area was generated with Dilib version V0.6.37. | ![]() |