Electron transfer chain reaction of the extracellular flavocytochrome cellobiose dehydrogenase from the basidiomycete Phanerochaete chrysosporium.
Identifieur interne : 000837 ( Main/Exploration ); précédent : 000836; suivant : 000838Electron transfer chain reaction of the extracellular flavocytochrome cellobiose dehydrogenase from the basidiomycete Phanerochaete chrysosporium.
Auteurs : Kiyohiko Igarashi [Japon] ; Makoto Yoshida ; Hirotoshi Matsumura ; Nobuhumi Nakamura ; Hiroyuki Ohno ; Masahiro Samejima ; Takeshi NishinoSource :
- The FEBS journal [ 1742-464X ] ; 2005.
Descripteurs français
- KwdFr :
- Carbohydrate dehydrogenases (composition chimique), Carbohydrate dehydrogenases (génétique), Carbohydrate dehydrogenases (métabolisme), Cellobiose (métabolisme), Cinétique (MeSH), Cytochromes c (composition chimique), Cytochromes c (métabolisme), Flavine adénine dinucléotide (composition chimique), Flavines (composition chimique), Flavines (métabolisme), Hème (composition chimique), Hème (métabolisme), Mutation (MeSH), Oxydoréduction (MeSH), Phanerochaete (composition chimique), Phanerochaete (enzymologie), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Thermodynamique (MeSH), Transport d'électrons (MeSH).
- MESH :
- composition chimique : Carbohydrate dehydrogenases, Cytochromes c, Flavine adénine dinucléotide, Flavines, Hème, Phanerochaete, Protéines fongiques.
- enzymologie : Phanerochaete.
- génétique : Carbohydrate dehydrogenases, Protéines fongiques.
- métabolisme : Carbohydrate dehydrogenases, Cellobiose, Cytochromes c, Flavines, Hème, Protéines fongiques.
- Cinétique, Mutation, Oxydoréduction, Thermodynamique, Transport d'électrons.
English descriptors
- KwdEn :
- Carbohydrate Dehydrogenases (chemistry), Carbohydrate Dehydrogenases (genetics), Carbohydrate Dehydrogenases (metabolism), Cellobiose (metabolism), Cytochromes c (chemistry), Cytochromes c (metabolism), Electron Transport (MeSH), Flavin-Adenine Dinucleotide (chemistry), Flavins (chemistry), Flavins (metabolism), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Heme (chemistry), Heme (metabolism), Kinetics (MeSH), Mutation (MeSH), Oxidation-Reduction (MeSH), Phanerochaete (chemistry), Phanerochaete (enzymology), Thermodynamics (MeSH).
- MESH :
- chemical , chemistry : Carbohydrate Dehydrogenases, Cytochromes c, Flavin-Adenine Dinucleotide, Flavins, Fungal Proteins, Heme.
- chemical , genetics : Carbohydrate Dehydrogenases, Fungal Proteins.
- chemical , metabolism : Carbohydrate Dehydrogenases, Cellobiose, Cytochromes c, Flavins, Fungal Proteins, Heme.
- chemistry : Phanerochaete.
- enzymology : Phanerochaete.
- Electron Transport, Kinetics, Mutation, Oxidation-Reduction, Thermodynamics.
Abstract
Cellobiose dehydrogenase (CDH) is an extracellular flavocytochrome containing flavin and b-type heme, and plays a key role in cellulose degradation by filamentous fungi. To investigate intermolecular electron transfer from CDH to cytochrome c, Phe166, which is located in the cytochrome domain and approaches one of propionates of heme, was mutated to Tyr, and the thermodynamic and kinetic properties of the mutant (F166Y) were compared with those of the wild-type (WT) enzyme. The mid-point potential of heme in F166Y was measured by cyclic voltammetry, and was estimated to be 25 mV lower than that of WT at pH 4.0. Although presteady-state reduction of flavin was not affected by the mutation, the rate of subsequent electron transfer from flavin to heme was halved in F166Y. When WT or F166Y was reduced with cellobiose and then mixed with cytochrome c, heme re-oxidation and cytochrome c reduction occurred synchronously, suggesting that the initial electron is transferred from reduced heme to cytochrome c. Moreover, in both enzymes the observed rate of the initial phase of cytochrome c reduction was concentration dependent, whereas the second phase of cytochrome c reduction was dependent on the rate of electron transfer from flavin to heme, but not on the cytochrome c concentration. In addition, the electron transfer rate from flavin to heme was identical to the steady-state reduction rate of cytochrome c in both WT and F166Y. These results clearly indicate that the first and second electrons of two-electron-reduced CDH are both transferred via heme, and that the redox reaction of CDH involves an electron-transfer chain mechanism in cytochrome c reduction.
DOI: 10.1111/j.1742-4658.2005.04707.x
PubMed: 15943818
Affiliations:
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last="Ohno">Hiroyuki Ohno</name></author><author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name></author><author><name sortKey="Nishino, Takeshi" sort="Nishino, Takeshi" uniqKey="Nishino T" first="Takeshi" last="Nishino">Takeshi Nishino</name></author></analytic><series><title level="j">The FEBS journal</title><idno type="ISSN">1742-464X</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carbohydrate Dehydrogenases (chemistry)</term><term>Carbohydrate Dehydrogenases (genetics)</term><term>Carbohydrate Dehydrogenases (metabolism)</term><term>Cellobiose (metabolism)</term><term>Cytochromes c (chemistry)</term><term>Cytochromes c (metabolism)</term><term>Electron Transport (MeSH)</term><term>Flavin-Adenine Dinucleotide (chemistry)</term><term>Flavins (chemistry)</term><term>Flavins (metabolism)</term><term>Fungal Proteins (chemistry)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Heme (chemistry)</term><term>Heme (metabolism)</term><term>Kinetics (MeSH)</term><term>Mutation (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Phanerochaete (chemistry)</term><term>Phanerochaete (enzymology)</term><term>Thermodynamics (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Carbohydrate dehydrogenases (composition chimique)</term><term>Carbohydrate dehydrogenases (génétique)</term><term>Carbohydrate dehydrogenases (métabolisme)</term><term>Cellobiose (métabolisme)</term><term>Cinétique (MeSH)</term><term>Cytochromes c (composition chimique)</term><term>Cytochromes c (métabolisme)</term><term>Flavine adénine dinucléotide (composition chimique)</term><term>Flavines (composition chimique)</term><term>Flavines (métabolisme)</term><term>Hème (composition chimique)</term><term>Hème (métabolisme)</term><term>Mutation (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Phanerochaete (composition chimique)</term><term>Phanerochaete (enzymologie)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Thermodynamique (MeSH)</term><term>Transport d'électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Cytochromes c</term><term>Flavin-Adenine Dinucleotide</term><term>Flavins</term><term>Fungal Proteins</term><term>Heme</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Fungal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Cellobiose</term><term>Cytochromes 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c</term><term>Flavines</term><term>Hème</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Transport</term><term>Kinetics</term><term>Mutation</term><term>Oxidation-Reduction</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Mutation</term><term>Oxydoréduction</term><term>Thermodynamique</term><term>Transport d'électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cellobiose dehydrogenase (CDH) is an extracellular flavocytochrome containing flavin and b-type heme, and plays a key role in cellulose degradation by filamentous fungi. To investigate intermolecular electron transfer from CDH to cytochrome c, Phe166, which is located in the cytochrome domain and approaches one of propionates of heme, was mutated to Tyr, and the thermodynamic and kinetic properties of the mutant (F166Y) were compared with those of the wild-type (WT) enzyme. The mid-point potential of heme in F166Y was measured by cyclic voltammetry, and was estimated to be 25 mV lower than that of WT at pH 4.0. Although presteady-state reduction of flavin was not affected by the mutation, the rate of subsequent electron transfer from flavin to heme was halved in F166Y. When WT or F166Y was reduced with cellobiose and then mixed with cytochrome c, heme re-oxidation and cytochrome c reduction occurred synchronously, suggesting that the initial electron is transferred from reduced heme to cytochrome c. Moreover, in both enzymes the observed rate of the initial phase of cytochrome c reduction was concentration dependent, whereas the second phase of cytochrome c reduction was dependent on the rate of electron transfer from flavin to heme, but not on the cytochrome c concentration. In addition, the electron transfer rate from flavin to heme was identical to the steady-state reduction rate of cytochrome c in both WT and F166Y. These results clearly indicate that the first and second electrons of two-electron-reduced CDH are both transferred via heme, and that the redox reaction of CDH involves an electron-transfer chain mechanism in cytochrome c reduction.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15943818</PMID><DateCompleted><Year>2005</Year><Month>07</Month><Day>21</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1742-464X</ISSN><JournalIssue CitedMedium="Print"><Volume>272</Volume><Issue>11</Issue><PubDate><Year>2005</Year><Month>Jun</Month></PubDate></JournalIssue><Title>The FEBS journal</Title><ISOAbbreviation>FEBS J</ISOAbbreviation></Journal><ArticleTitle>Electron transfer chain reaction of the extracellular flavocytochrome cellobiose dehydrogenase from the basidiomycete Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>2869-77</MedlinePgn></Pagination><Abstract><AbstractText>Cellobiose dehydrogenase (CDH) is an extracellular flavocytochrome containing flavin and b-type heme, and plays a key role in cellulose degradation by filamentous fungi. To investigate intermolecular electron transfer from CDH to cytochrome c, Phe166, which is located in the cytochrome domain and approaches one of propionates of heme, was mutated to Tyr, and the thermodynamic and kinetic properties of the mutant (F166Y) were compared with those of the wild-type (WT) enzyme. The mid-point potential of heme in F166Y was measured by cyclic voltammetry, and was estimated to be 25 mV lower than that of WT at pH 4.0. Although presteady-state reduction of flavin was not affected by the mutation, the rate of subsequent electron transfer from flavin to heme was halved in F166Y. When WT or F166Y was reduced with cellobiose and then mixed with cytochrome c, heme re-oxidation and cytochrome c reduction occurred synchronously, suggesting that the initial electron is transferred from reduced heme to cytochrome c. Moreover, in both enzymes the observed rate of the initial phase of cytochrome c reduction was concentration dependent, whereas the second phase of cytochrome c reduction was dependent on the rate of electron transfer from flavin to heme, but not on the cytochrome c concentration. In addition, the electron transfer rate from flavin to heme was identical to the steady-state reduction rate of cytochrome c in both WT and F166Y. These results clearly indicate that the first and second electrons of two-electron-reduced CDH are both transferred via heme, and that the redox reaction of CDH involves an electron-transfer chain mechanism in cytochrome c reduction.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Igarashi</LastName><ForeName>Kiyohiko</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan. aquarius@mail.ess.u-tokyo.ac.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yoshida</LastName><ForeName>Makoto</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Matsumura</LastName><ForeName>Hirotoshi</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Nakamura</LastName><ForeName>Nobuhumi</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Ohno</LastName><ForeName>Hiroyuki</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Samejima</LastName><ForeName>Masahiro</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Nishino</LastName><ForeName>Takeshi</ForeName><Initials>T</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>England</Country><MedlineTA>FEBS J</MedlineTA><NlmUniqueID>101229646</NlmUniqueID><ISSNLinking>1742-464X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005415">Flavins</NameOfSubstance></Chemical><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>16462-44-5</RegistryNumber><NameOfSubstance UI="D002475">Cellobiose</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-43-6</RegistryNumber><NameOfSubstance UI="D045304">Cytochromes c</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="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002475" MajorTopicYN="N">Cellobiose</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045304" MajorTopicYN="N">Cytochromes c</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="Y">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005182" MajorTopicYN="N">Flavin-Adenine Dinucleotide</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005415" MajorTopicYN="N">Flavins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>6</Month><Day>10</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>7</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>6</Month><Day>10</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15943818</ArticleId><ArticleId IdType="pii">EJB4707</ArticleId><ArticleId IdType="doi">10.1111/j.1742-4658.2005.04707.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><noCountry><name sortKey="Matsumura, Hirotoshi" sort="Matsumura, Hirotoshi" uniqKey="Matsumura H" first="Hirotoshi" last="Matsumura">Hirotoshi Matsumura</name><name sortKey="Nakamura, Nobuhumi" sort="Nakamura, Nobuhumi" uniqKey="Nakamura N" first="Nobuhumi" last="Nakamura">Nobuhumi Nakamura</name><name sortKey="Nishino, Takeshi" sort="Nishino, Takeshi" uniqKey="Nishino T" first="Takeshi" last="Nishino">Takeshi Nishino</name><name sortKey="Ohno, Hiroyuki" sort="Ohno, Hiroyuki" uniqKey="Ohno H" first="Hiroyuki" last="Ohno">Hiroyuki Ohno</name><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name><name sortKey="Yoshida, Makoto" sort="Yoshida, Makoto" uniqKey="Yoshida M" first="Makoto" last="Yoshida">Makoto Yoshida</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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