Resonance Raman spectroscopic studies of cellobiose dehydrogenase from Phanerochaete chrysosporium.
Identifieur interne : 000B98 ( Main/Exploration ); précédent : 000B97; suivant : 000B99Resonance Raman spectroscopic studies of cellobiose dehydrogenase from Phanerochaete chrysosporium.
Auteurs : J D Cohen [États-Unis] ; W. Bao ; V. Renganathan ; S S Subramaniam ; T M LoehrSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1997.
Descripteurs français
- KwdFr :
- Analyse spectrale Raman (MeSH), Basidiomycota (enzymologie), Carbohydrate dehydrogenases (composition chimique), Flavine adénine dinucléotide (composition chimique), Hème (composition chimique), Liaison aux protéines (MeSH), Oxydoréduction (MeSH), Protéines fongiques (composition chimique), Transport d'électrons (MeSH).
- MESH :
- composition chimique : Carbohydrate dehydrogenases, Flavine adénine dinucléotide, Hème, Protéines fongiques.
- enzymologie : Basidiomycota.
- Analyse spectrale Raman, Liaison aux protéines, Oxydoréduction, Transport d'électrons.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Carbohydrate Dehydrogenases, Flavin-Adenine Dinucleotide, Fungal Proteins, Heme.
- enzymology : Basidiomycota.
- Electron Transport, Oxidation-Reduction, Protein Binding, Spectrum Analysis, Raman.
Abstract
Cellobiose dehydrogenase (CDH), an extracellular hemoflavoenzyme produced by cellulose-degrading cultures of Phanerochaete chrysosporium, oxidizes cellobiose to cellobionolactone. The enzyme contains one 6-coordinate, low-spin b-type heme and one FAD cofactor per monomeric protein. In this work, resonance Raman (RR) spectra are reported for the oxidized, reduced, and deflavo forms of CDH as well as the individual flavin and heme domains of the enzyme obtained by peptide proteolysis. The RR spectra of the flavin and heme groups of CDH were assigned by comparison to the spectra of other hemoflavoenzymes and model compounds. Proteolytic cleavage of the CDH domains had only a minimal spectroscopic effect on the vibrational modes of the heme and FAD cofactors. Excitation of the oxidized CDH holoenzyme at 413 or 442 nm resulted in photoreduction of the heme. However, the same excitation wavelength used on the deflavo form of the enzyme or on the heme domain alone did not cause photoreduction, indicating that photoinitiated electron transfer requires the FAD cofactor. These observations suggest an enzymatic mechanism whereby reducing equivalents obtained from the oxidation of cellobiose are transferred from the FAD to the heme. A similar mechanism has been proposed for flavocytochrome b2 of Saccharomyces cerevisiae which oxidizes lactate to pyruvate (A. Desbois et al., 1989, Biochemistry 28, 8011-8022).
DOI: 10.1006/abbi.1997.9987
PubMed: 9169022
Affiliations:
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Bao</name></author><author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></author><author><name sortKey="Subramaniam, S S" sort="Subramaniam, S S" uniqKey="Subramaniam S" first="S S" last="Subramaniam">S S Subramaniam</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></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1997">1997</date><idno type="RBID">pubmed:9169022</idno><idno type="pmid">9169022</idno><idno type="doi">10.1006/abbi.1997.9987</idno><idno type="wicri:Area/Main/Corpus">000C10</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C10</idno><idno type="wicri:Area/Main/Curation">000C10</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C10</idno><idno type="wicri:Area/Main/Exploration">000C10</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Resonance Raman spectroscopic studies of cellobiose dehydrogenase from Phanerochaete chrysosporium.</title><author><name sortKey="Cohen, J D" sort="Cohen, J D" uniqKey="Cohen J" first="J D" last="Cohen">J D Cohen</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97291-1000, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97291-1000</wicri:regionArea><placeName><settlement type="city">Portland</settlement><region type="state">Oregon</region></placeName></affiliation></author><author><name sortKey="Bao, W" sort="Bao, W" uniqKey="Bao W" first="W" last="Bao">W. Bao</name></author><author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></author><author><name sortKey="Subramaniam, S S" sort="Subramaniam, S S" uniqKey="Subramaniam S" first="S S" last="Subramaniam">S S Subramaniam</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></analytic><series><title level="j">Archives of biochemistry and biophysics</title><idno type="ISSN">0003-9861</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Carbohydrate Dehydrogenases (chemistry)</term><term>Electron Transport (MeSH)</term><term>Flavin-Adenine Dinucleotide (chemistry)</term><term>Fungal Proteins (chemistry)</term><term>Heme (chemistry)</term><term>Oxidation-Reduction (MeSH)</term><term>Protein Binding (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>Carbohydrate dehydrogenases (composition chimique)</term><term>Flavine adénine dinucléotide (composition chimique)</term><term>Hème (composition chimique)</term><term>Liaison aux protéines (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines fongiques (composition chimique)</term><term>Transport d'électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Flavin-Adenine Dinucleotide</term><term>Fungal Proteins</term><term>Heme</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Carbohydrate dehydrogenases</term><term>Flavine adénine dinucléotide</term><term>Hème</term><term>Protéines fongiques</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" xml:lang="en"><term>Electron Transport</term><term>Oxidation-Reduction</term><term>Protein Binding</term><term>Spectrum Analysis, Raman</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse spectrale Raman</term><term>Liaison aux protéines</term><term>Oxydoréduction</term><term>Transport d'électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cellobiose dehydrogenase (CDH), an extracellular hemoflavoenzyme produced by cellulose-degrading cultures of Phanerochaete chrysosporium, oxidizes cellobiose to cellobionolactone. The enzyme contains one 6-coordinate, low-spin b-type heme and one FAD cofactor per monomeric protein. In this work, resonance Raman (RR) spectra are reported for the oxidized, reduced, and deflavo forms of CDH as well as the individual flavin and heme domains of the enzyme obtained by peptide proteolysis. The RR spectra of the flavin and heme groups of CDH were assigned by comparison to the spectra of other hemoflavoenzymes and model compounds. Proteolytic cleavage of the CDH domains had only a minimal spectroscopic effect on the vibrational modes of the heme and FAD cofactors. Excitation of the oxidized CDH holoenzyme at 413 or 442 nm resulted in photoreduction of the heme. However, the same excitation wavelength used on the deflavo form of the enzyme or on the heme domain alone did not cause photoreduction, indicating that photoinitiated electron transfer requires the FAD cofactor. These observations suggest an enzymatic mechanism whereby reducing equivalents obtained from the oxidation of cellobiose are transferred from the FAD to the heme. A similar mechanism has been proposed for flavocytochrome b2 of Saccharomyces cerevisiae which oxidizes lactate to pyruvate (A. Desbois et al., 1989, Biochemistry 28, 8011-8022).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9169022</PMID><DateCompleted><Year>1997</Year><Month>06</Month><Day>30</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>341</Volume><Issue>2</Issue><PubDate><Year>1997</Year><Month>May</Month><Day>15</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Resonance Raman spectroscopic studies of cellobiose dehydrogenase from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>321-8</MedlinePgn></Pagination><Abstract><AbstractText>Cellobiose dehydrogenase (CDH), an extracellular hemoflavoenzyme produced by cellulose-degrading cultures of Phanerochaete chrysosporium, oxidizes cellobiose to cellobionolactone. The enzyme contains one 6-coordinate, low-spin b-type heme and one FAD cofactor per monomeric protein. In this work, resonance Raman (RR) spectra are reported for the oxidized, reduced, and deflavo forms of CDH as well as the individual flavin and heme domains of the enzyme obtained by peptide proteolysis. The RR spectra of the flavin and heme groups of CDH were assigned by comparison to the spectra of other hemoflavoenzymes and model compounds. Proteolytic cleavage of the CDH domains had only a minimal spectroscopic effect on the vibrational modes of the heme and FAD cofactors. Excitation of the oxidized CDH holoenzyme at 413 or 442 nm resulted in photoreduction of the heme. However, the same excitation wavelength used on the deflavo form of the enzyme or on the heme domain alone did not cause photoreduction, indicating that photoinitiated electron transfer requires the FAD cofactor. These observations suggest an enzymatic mechanism whereby reducing equivalents obtained from the oxidation of cellobiose are transferred from the FAD to the heme. A similar mechanism has been proposed for flavocytochrome b2 of Saccharomyces cerevisiae which oxidizes lactate to pyruvate (A. Desbois et al., 1989, Biochemistry 28, 8011-8022).</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cohen</LastName><ForeName>J D</ForeName><Initials>JD</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97291-1000, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bao</LastName><ForeName>W</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Renganathan</LastName><ForeName>V</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Subramaniam</LastName><ForeName>S S</ForeName><Initials>SS</Initials></Author><Author ValidYN="Y"><LastName>Loehr</LastName><ForeName>T M</ForeName><Initials>TM</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM-34468</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>RR-02676</GrantID><Acronym>RR</Acronym><Agency>NCRR 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>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>146-14-5</RegistryNumber><NameOfSubstance UI="D005182">Flavin-Adenine Dinucleotide</NameOfSubstance></Chemical><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 1.1.99.18</RegistryNumber><NameOfSubstance UI="C019859">cellobiose-quinone oxidoreductase</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="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005182" MajorTopicYN="N">Flavin-Adenine Dinucleotide</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013059" MajorTopicYN="Y">Spectrum Analysis, Raman</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>5</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>5</Month><Day>15</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>5</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9169022</ArticleId><ArticleId IdType="pii">S0003-9861(97)99987-2</ArticleId><ArticleId IdType="doi">10.1006/abbi.1997.9987</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Oregon</li></region><settlement><li>Portland</li></settlement></list><tree><noCountry><name sortKey="Bao, W" sort="Bao, W" uniqKey="Bao W" first="W" last="Bao">W. Bao</name><name sortKey="Loehr, T M" sort="Loehr, T M" uniqKey="Loehr T" first="T M" last="Loehr">T M Loehr</name><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name><name sortKey="Subramaniam, S S" sort="Subramaniam, S S" uniqKey="Subramaniam S" first="S S" last="Subramaniam">S S Subramaniam</name></noCountry><country name="États-Unis"><region name="Oregon"><name sortKey="Cohen, J D" sort="Cohen, J D" uniqKey="Cohen J" first="J D" last="Cohen">J D Cohen</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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