Electrochemical evidence of self-substrate inhibition as functions regulation for cellobiose dehydrogenase from Phanerochaete chrysosporium.
Identifieur interne : 000637 ( Main/Exploration ); précédent : 000636; suivant : 000638Electrochemical evidence of self-substrate inhibition as functions regulation for cellobiose dehydrogenase from Phanerochaete chrysosporium.
Auteurs : Leonard Stoica [Suède] ; Tautgirdas Ruzgas ; Lo GortonSource :
- Bioelectrochemistry (Amsterdam, Netherlands) [ 1878-562X ] ; 2009.
Descripteurs français
- KwdFr :
- Antienzymes (composition chimique), Antienzymes (métabolisme), Antienzymes (pharmacologie), Carbohydrate dehydrogenases (antagonistes et inhibiteurs), Carbohydrate dehydrogenases (composition chimique), Carbohydrate dehydrogenases (métabolisme), Cellobiose (composition chimique), Cellobiose (métabolisme), Cellobiose (pharmacologie), Cinétique (MeSH), Conformation des protéines (MeSH), Dichroïsme circulaire (MeSH), Dénaturation des protéines (MeSH), Fixation compétitive (MeSH), Hydroquinones (composition chimique), Hydroquinones (métabolisme), Lactose (composition chimique), Lactose (métabolisme), Phanerochaete (enzymologie), Relation dose-effet des médicaments (MeSH), Transport d'électrons (MeSH), Électrochimie (MeSH).
- MESH :
- antagonistes et inhibiteurs : Carbohydrate dehydrogenases.
- composition chimique : Antienzymes, Carbohydrate dehydrogenases, Cellobiose, Hydroquinones, Lactose.
- enzymologie : Phanerochaete.
- métabolisme : Antienzymes, Carbohydrate dehydrogenases, Cellobiose, Hydroquinones, Lactose.
- pharmacologie : Antienzymes, Cellobiose.
- Cinétique, Conformation des protéines, Dichroïsme circulaire, Dénaturation des protéines, Fixation compétitive, Relation dose-effet des médicaments, Transport d'électrons, Électrochimie.
English descriptors
- KwdEn :
- Binding, Competitive (MeSH), Carbohydrate Dehydrogenases (antagonists & inhibitors), Carbohydrate Dehydrogenases (chemistry), Carbohydrate Dehydrogenases (metabolism), Cellobiose (chemistry), Cellobiose (metabolism), Cellobiose (pharmacology), Circular Dichroism (MeSH), Dose-Response Relationship, Drug (MeSH), Electrochemistry (MeSH), Electron Transport (MeSH), Enzyme Inhibitors (chemistry), Enzyme Inhibitors (metabolism), Enzyme Inhibitors (pharmacology), Hydroquinones (chemistry), Hydroquinones (metabolism), Kinetics (MeSH), Lactose (chemistry), Lactose (metabolism), Phanerochaete (enzymology), Protein Conformation (MeSH), Protein Denaturation (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Carbohydrate Dehydrogenases.
- chemical , chemistry : Carbohydrate Dehydrogenases, Cellobiose, Enzyme Inhibitors, Hydroquinones, Lactose.
- chemical , metabolism : Carbohydrate Dehydrogenases, Cellobiose, Enzyme Inhibitors, Hydroquinones, Lactose.
- chemical , pharmacology : Cellobiose, Enzyme Inhibitors.
- enzymology : Phanerochaete.
- Binding, Competitive, Circular Dichroism, Dose-Response Relationship, Drug, Electrochemistry, Electron Transport, Kinetics, Protein Conformation, Protein Denaturation.
Abstract
The reaction mechanism of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium, adsorbed on graphite electrodes, was investigated by following its catalytic reaction with cellobiose registered in both direct and mediated electron transfer modes between the enzyme and the electrode. A wall-jet flow through amperometric cell housing the CDH-modified graphite electrode was connected to a single line flow injection system. In the present study, it is proven that cellobiose, at concentrations higher than 200 microM, competes for the reduced state of the FAD cofactor and it slows down the transfer of electrons to any 2e(-)/H(+) acceptors or further to the heme cofactor, via the internal electron transfer pathway. Based on and proven by electrochemical results, a kinetic model of substrate inhibition is proposed and supported by the agreement between simulation of plots and experimental data. The implications of this kinetic model, called pseudo-ping-pong mechanism, on the possible functions CDH are also discussed. The enzyme exhibits catalytic activity also for lactose, but in contrast to cellobiose, this sugar does not inhibit the enzyme. This suggests that even if some other substrates are coincidentally oxidized by CDH, however, they do not trigger all the possible natural functions of the enzyme. In this respect, cellobiose is regarded as the natural substrate of CDH.
DOI: 10.1016/j.bioelechem.2009.06.007
PubMed: 19640808
Affiliations:
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(pharmacology)</term><term>Circular Dichroism (MeSH)</term><term>Dose-Response Relationship, Drug (MeSH)</term><term>Electrochemistry (MeSH)</term><term>Electron Transport (MeSH)</term><term>Enzyme Inhibitors (chemistry)</term><term>Enzyme Inhibitors (metabolism)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Hydroquinones (chemistry)</term><term>Hydroquinones (metabolism)</term><term>Kinetics (MeSH)</term><term>Lactose (chemistry)</term><term>Lactose (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Protein Conformation (MeSH)</term><term>Protein Denaturation (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antienzymes (composition chimique)</term><term>Antienzymes (métabolisme)</term><term>Antienzymes (pharmacologie)</term><term>Carbohydrate dehydrogenases (antagonistes et inhibiteurs)</term><term>Carbohydrate dehydrogenases (composition chimique)</term><term>Carbohydrate dehydrogenases (métabolisme)</term><term>Cellobiose (composition chimique)</term><term>Cellobiose (métabolisme)</term><term>Cellobiose (pharmacologie)</term><term>Cinétique (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Dichroïsme circulaire (MeSH)</term><term>Dénaturation des protéines (MeSH)</term><term>Fixation compétitive (MeSH)</term><term>Hydroquinones (composition chimique)</term><term>Hydroquinones (métabolisme)</term><term>Lactose (composition chimique)</term><term>Lactose (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Relation dose-effet des médicaments (MeSH)</term><term>Transport d'électrons (MeSH)</term><term>Électrochimie (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Carbohydrate Dehydrogenases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Cellobiose</term><term>Enzyme Inhibitors</term><term>Hydroquinones</term><term>Lactose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Cellobiose</term><term>Enzyme Inhibitors</term><term>Hydroquinones</term><term>Lactose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cellobiose</term><term>Enzyme Inhibitors</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Carbohydrate dehydrogenases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Antienzymes</term><term>Carbohydrate dehydrogenases</term><term>Cellobiose</term><term>Hydroquinones</term><term>Lactose</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords 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type="abstract" xml:lang="en">The reaction mechanism of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium, adsorbed on graphite electrodes, was investigated by following its catalytic reaction with cellobiose registered in both direct and mediated electron transfer modes between the enzyme and the electrode. A wall-jet flow through amperometric cell housing the CDH-modified graphite electrode was connected to a single line flow injection system. In the present study, it is proven that cellobiose, at concentrations higher than 200 microM, competes for the reduced state of the FAD cofactor and it slows down the transfer of electrons to any 2e(-)/H(+) acceptors or further to the heme cofactor, via the internal electron transfer pathway. Based on and proven by electrochemical results, a kinetic model of substrate inhibition is proposed and supported by the agreement between simulation of plots and experimental data. The implications of this kinetic model, called pseudo-ping-pong mechanism, on the possible functions CDH are also discussed. The enzyme exhibits catalytic activity also for lactose, but in contrast to cellobiose, this sugar does not inhibit the enzyme. This suggests that even if some other substrates are coincidentally oxidized by CDH, however, they do not trigger all the possible natural functions of the enzyme. In this respect, cellobiose is regarded as the natural substrate of CDH.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19640808</PMID><DateCompleted><Year>2009</Year><Month>12</Month><Day>01</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1878-562X</ISSN><JournalIssue CitedMedium="Internet"><Volume>76</Volume><Issue>1-2</Issue><PubDate><Year>2009</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Bioelectrochemistry (Amsterdam, Netherlands)</Title><ISOAbbreviation>Bioelectrochemistry</ISOAbbreviation></Journal><ArticleTitle>Electrochemical evidence of self-substrate inhibition as functions regulation for cellobiose dehydrogenase from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>42-52</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bioelechem.2009.06.007</ELocationID><Abstract><AbstractText>The reaction mechanism of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium, adsorbed on graphite electrodes, was investigated by following its catalytic reaction with cellobiose registered in both direct and mediated electron transfer modes between the enzyme and the electrode. A wall-jet flow through amperometric cell housing the CDH-modified graphite electrode was connected to a single line flow injection system. In the present study, it is proven that cellobiose, at concentrations higher than 200 microM, competes for the reduced state of the FAD cofactor and it slows down the transfer of electrons to any 2e(-)/H(+) acceptors or further to the heme cofactor, via the internal electron transfer pathway. Based on and proven by electrochemical results, a kinetic model of substrate inhibition is proposed and supported by the agreement between simulation of plots and experimental data. The implications of this kinetic model, called pseudo-ping-pong mechanism, on the possible functions CDH are also discussed. The enzyme exhibits catalytic activity also for lactose, but in contrast to cellobiose, this sugar does not inhibit the enzyme. This suggests that even if some other substrates are coincidentally oxidized by CDH, however, they do not trigger all the possible natural functions of the enzyme. In this respect, cellobiose is regarded as the natural substrate of CDH.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Stoica</LastName><ForeName>Leonard</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden. leonard.stoica@rub.de</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ruzgas</LastName><ForeName>Tautgirdas</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Gorton</LastName><ForeName>Lo</ForeName><Initials>L</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><ArticleDate DateType="Electronic"><Year>2009</Year><Month>06</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Bioelectrochemistry</MedlineTA><NlmUniqueID>100953583</NlmUniqueID><ISSNLinking>1567-5394</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006873">Hydroquinones</NameOfSubstance></Chemical><Chemical><RegistryNumber>16462-44-5</RegistryNumber><NameOfSubstance UI="D002475">Cellobiose</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><Chemical><RegistryNumber>J2B2A4N98G</RegistryNumber><NameOfSubstance UI="D007785">Lactose</NameOfSubstance></Chemical><Chemical><RegistryNumber>XV74C1N1AE</RegistryNumber><NameOfSubstance UI="C031927">hydroquinone</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001667" MajorTopicYN="N">Binding, Competitive</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002475" MajorTopicYN="N">Cellobiose</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004563" MajorTopicYN="N">Electrochemistry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006873" MajorTopicYN="N">Hydroquinones</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007785" MajorTopicYN="N">Lactose</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year><Month>03</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2009</Year><Month>06</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2009</Year><Month>06</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>7</Month><Day>31</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>7</Month><Day>31</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>12</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19640808</ArticleId><ArticleId IdType="pii">S1567-5394(09)00119-4</ArticleId><ArticleId IdType="doi">10.1016/j.bioelechem.2009.06.007</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Gorton, Lo" sort="Gorton, Lo" uniqKey="Gorton L" first="Lo" last="Gorton">Lo Gorton</name><name sortKey="Ruzgas, Tautgirdas" sort="Ruzgas, Tautgirdas" uniqKey="Ruzgas T" first="Tautgirdas" last="Ruzgas">Tautgirdas Ruzgas</name></noCountry><country 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