Inter-domain electron transfer in cellobiose dehydrogenase: modulation by pH and divalent cations.
Identifieur interne : 000258 ( Main/Exploration ); précédent : 000257; suivant : 000259Inter-domain electron transfer in cellobiose dehydrogenase: modulation by pH and divalent cations.
Auteurs : Daniel Kracher [Autriche] ; Kawah Zahma [Autriche] ; Christopher Schulz [Suède] ; Christoph Sygmund [Autriche] ; Lo Gorton [Suède] ; Roland Ludwig [Autriche]Source :
- The FEBS journal [ 1742-4658 ] ; 2015.
Descripteurs français
- KwdFr :
- Carbohydrate dehydrogenases (composition chimique), Carbohydrate dehydrogenases (métabolisme), Cations divalents (métabolisme), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Conformation des protéines (MeSH), Cytochromes c (métabolisme), Modèles moléculaires (MeSH), Motifs et domaines d'intéraction protéique (MeSH), Phanerochaete (enzymologie), Protéines fongiques (composition chimique), Protéines fongiques (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (métabolisme), Sites de fixation (MeSH), Sordariales (enzymologie), Transport d'électrons (MeSH), Électricité statique (MeSH).
- MESH :
- composition chimique : Carbohydrate dehydrogenases, Protéines fongiques, Protéines recombinantes.
- enzymologie : Phanerochaete, Sordariales.
- métabolisme : Carbohydrate dehydrogenases, Cations divalents, Cytochromes c, Protéines fongiques, Protéines recombinantes.
- Cinétique, Concentration en ions d'hydrogène, Conformation des protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Sites de fixation, Transport d'électrons, Électricité statique.
English descriptors
- KwdEn :
- Binding Sites (MeSH), Carbohydrate Dehydrogenases (chemistry), Carbohydrate Dehydrogenases (metabolism), Cations, Divalent (metabolism), Cytochromes c (metabolism), Electron Transport (MeSH), Fungal Proteins (chemistry), Fungal Proteins (metabolism), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), Models, Molecular (MeSH), Phanerochaete (enzymology), Protein Conformation (MeSH), Protein Interaction Domains and Motifs (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Sordariales (enzymology), Static Electricity (MeSH).
- MESH :
- chemical , chemistry : Carbohydrate Dehydrogenases, Fungal Proteins, Recombinant Proteins.
- chemical , metabolism : Carbohydrate Dehydrogenases, Cations, Divalent, Cytochromes c, Fungal Proteins, Recombinant Proteins.
- enzymology : Phanerochaete, Sordariales.
- Binding Sites, Electron Transport, Hydrogen-Ion Concentration, Kinetics, Models, Molecular, Protein Conformation, Protein Interaction Domains and Motifs, Static Electricity.
Abstract
The flavocytochrome cellobiose dehydrogenase (CDH) is secreted by wood-decomposing fungi, and is the only known extracellular enzyme with the characteristics of an electron transfer protein. Its proposed function is reduction of lytic polysaccharide mono-oxygenase for subsequent cellulose depolymerization. Electrons are transferred from FADH2 in the catalytic flavodehydrogenase domain of CDH to haem b in a mobile cytochrome domain, which acts as a mediator and transfers electrons towards the active site of lytic polysaccharide mono-oxygenase to activate oxygen. This vital role of the cytochrome domain is little understood, e.g. why do CDHs exhibit different pH optima and rates for inter-domain electron transfer (IET)? This study uses kinetic techniques and docking to assess the interaction of both domains and the resulting IET with regard to pH and ions. The results show that the reported elimination of IET at neutral or alkaline pH is caused by electrostatic repulsion, which prevents adoption of the closed conformation of CDH. Divalent alkali earth metal cations are shown to exert a bridging effect between the domains at concentrations of > 3 mm, thereby neutralizing electrostatic repulsion and increasing IET rates. The necessary high ion concentration, together with the docking results, show that this effect is not caused by specific cation binding sites, but by various clusters of Asp, Glu, Asn, Gln and the haem b propionate group at the domain interface. The results show that a closed conformation of both CDH domains is necessary for IET, but the closed conformation also increases the FAD reduction rate by an electron pulling effect.
DOI: 10.1111/febs.13310
PubMed: 25913436
PubMed Central: PMC4676925
Affiliations:
Links toward previous steps (curation, corpus...)
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chimique)</term><term>Carbohydrate dehydrogenases (métabolisme)</term><term>Cations divalents (métabolisme)</term><term>Cinétique (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cytochromes c (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Motifs et domaines d'intéraction protéique (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (métabolisme)</term><term>Sites de fixation (MeSH)</term><term>Sordariales (enzymologie)</term><term>Transport d'électrons (MeSH)</term><term>Électricité statique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Fungal Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Cations, Divalent</term><term>Cytochromes c</term><term>Fungal Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Carbohydrate dehydrogenases</term><term>Protéines fongiques</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term><term>Sordariales</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term><term>Sordariales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carbohydrate dehydrogenases</term><term>Cations divalents</term><term>Cytochromes c</term><term>Protéines fongiques</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Electron Transport</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Models, Molecular</term><term>Protein Conformation</term><term>Protein Interaction Domains and Motifs</term><term>Static Electricity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Sites de fixation</term><term>Transport d'électrons</term><term>Électricité statique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The flavocytochrome cellobiose dehydrogenase (CDH) is secreted by wood-decomposing fungi, and is the only known extracellular enzyme with the characteristics of an electron transfer protein. Its proposed function is reduction of lytic polysaccharide mono-oxygenase for subsequent cellulose depolymerization. Electrons are transferred from FADH2 in the catalytic flavodehydrogenase domain of CDH to haem b in a mobile cytochrome domain, which acts as a mediator and transfers electrons towards the active site of lytic polysaccharide mono-oxygenase to activate oxygen. This vital role of the cytochrome domain is little understood, e.g. why do CDHs exhibit different pH optima and rates for inter-domain electron transfer (IET)? This study uses kinetic techniques and docking to assess the interaction of both domains and the resulting IET with regard to pH and ions. The results show that the reported elimination of IET at neutral or alkaline pH is caused by electrostatic repulsion, which prevents adoption of the closed conformation of CDH. Divalent alkali earth metal cations are shown to exert a bridging effect between the domains at concentrations of > 3 mm, thereby neutralizing electrostatic repulsion and increasing IET rates. The necessary high ion concentration, together with the docking results, show that this effect is not caused by specific cation binding sites, but by various clusters of Asp, Glu, Asn, Gln and the haem b propionate group at the domain interface. The results show that a closed conformation of both CDH domains is necessary for IET, but the closed conformation also increases the FAD reduction rate by an electron pulling effect.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25913436</PMID><DateCompleted><Year>2015</Year><Month>11</Month><Day>30</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1742-4658</ISSN><JournalIssue CitedMedium="Internet"><Volume>282</Volume><Issue>16</Issue><PubDate><Year>2015</Year><Month>Aug</Month></PubDate></JournalIssue><Title>The FEBS journal</Title><ISOAbbreviation>FEBS J</ISOAbbreviation></Journal><ArticleTitle>Inter-domain electron transfer in cellobiose dehydrogenase: modulation by pH and divalent cations.</ArticleTitle><Pagination><MedlinePgn>3136-48</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/febs.13310</ELocationID><Abstract><AbstractText>The flavocytochrome cellobiose dehydrogenase (CDH) is secreted by wood-decomposing fungi, and is the only known extracellular enzyme with the characteristics of an electron transfer protein. Its proposed function is reduction of lytic polysaccharide mono-oxygenase for subsequent cellulose depolymerization. Electrons are transferred from FADH2 in the catalytic flavodehydrogenase domain of CDH to haem b in a mobile cytochrome domain, which acts as a mediator and transfers electrons towards the active site of lytic polysaccharide mono-oxygenase to activate oxygen. This vital role of the cytochrome domain is little understood, e.g. why do CDHs exhibit different pH optima and rates for inter-domain electron transfer (IET)? This study uses kinetic techniques and docking to assess the interaction of both domains and the resulting IET with regard to pH and ions. The results show that the reported elimination of IET at neutral or alkaline pH is caused by electrostatic repulsion, which prevents adoption of the closed conformation of CDH. Divalent alkali earth metal cations are shown to exert a bridging effect between the domains at concentrations of > 3 mm, thereby neutralizing electrostatic repulsion and increasing IET rates. The necessary high ion concentration, together with the docking results, show that this effect is not caused by specific cation binding sites, but by various clusters of Asp, Glu, Asn, Gln and the haem b propionate group at the domain interface. The results show that a closed conformation of both CDH domains is necessary for IET, but the closed conformation also increases the FAD reduction rate by an electron pulling effect.</AbstractText><CopyrightInformation>© 2015 The Authors. FEBS Journal published by John Wiley & Sons Ltd on behalf of FEBS.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kracher</LastName><ForeName>Daniel</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Food Sciences and Technology, Food Biotechnology Laboratory, University of Natural Resources and Life Sciences, Vienna, Austria.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zahma</LastName><ForeName>Kawah</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Food Sciences and Technology, Food Biotechnology Laboratory, University of Natural Resources and Life Sciences, Vienna, Austria.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schulz</LastName><ForeName>Christopher</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Analytical Chemistry, Biochemistry and Structural Biology, Lund University, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sygmund</LastName><ForeName>Christoph</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Food Sciences and Technology, Food Biotechnology Laboratory, University of Natural Resources and Life Sciences, Vienna, Austria.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gorton</LastName><ForeName>Lo</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Analytical Chemistry, Biochemistry and Structural Biology, Lund University, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ludwig</LastName><ForeName>Roland</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Food Sciences and Technology, Food Biotechnology Laboratory, University of Natural Resources and Life Sciences, Vienna, Austria.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>W 1224</GrantID><Agency>Austrian Science Fund FWF</Agency><Country>Austria</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>05</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS J</MedlineTA><NlmUniqueID>101229646</NlmUniqueID><ISSNLinking>1742-464X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002413">Cations, Divalent</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</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="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002413" MajorTopicYN="N">Cations, Divalent</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045304" MajorTopicYN="N">Cytochromes c</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020037" MajorTopicYN="N">Sordariales</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055672" MajorTopicYN="N">Static Electricity</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">cellobiose dehydrogenase</Keyword><Keyword MajorTopicYN="N">divalent cation bridging effect</Keyword><Keyword MajorTopicYN="N">domain docking</Keyword><Keyword MajorTopicYN="N">inter-domain electron transfer</Keyword><Keyword MajorTopicYN="N">oxidative cellulose degradation</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>10</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>04</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>04</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>4</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>4</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Daniel" sort="Kracher, Daniel" uniqKey="Kracher D" first="Daniel" last="Kracher">Daniel Kracher</name></region><name sortKey="Ludwig, Roland" sort="Ludwig, Roland" uniqKey="Ludwig R" first="Roland" last="Ludwig">Roland Ludwig</name><name sortKey="Sygmund, Christoph" sort="Sygmund, Christoph" uniqKey="Sygmund C" first="Christoph" last="Sygmund">Christoph Sygmund</name><name sortKey="Zahma, Kawah" sort="Zahma, Kawah" uniqKey="Zahma K" first="Kawah" last="Zahma">Kawah Zahma</name></country><country name="Suède"><noRegion><name sortKey="Schulz, Christopher" sort="Schulz, Christopher" uniqKey="Schulz C" first="Christopher" last="Schulz">Christopher Schulz</name></noRegion><name sortKey="Gorton, Lo" sort="Gorton, Lo" uniqKey="Gorton L" first="Lo" last="Gorton">Lo Gorton</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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