Direct electron transfer--a favorite electron route for cellobiose dehydrogenase (CDH) from Trametes villosa. Comparison with CDH from Phanerochaete chrysosporium.
Identifieur interne : 000781 ( Main/Exploration ); précédent : 000780; suivant : 000782Direct electron transfer--a favorite electron route for cellobiose dehydrogenase (CDH) from Trametes villosa. Comparison with CDH from Phanerochaete chrysosporium.
Auteurs : Leonard Stoica [Suède] ; Tautgirdas Ruzgas ; Roland Ludwig ; Dietmar Haltrich ; Lo GortonSource :
- Langmuir : the ACS journal of surfaces and colloids [ 0743-7463 ] ; 2006.
Descripteurs français
- KwdFr :
- Adsorption (MeSH), Basidiomycota (enzymologie), Carbohydrate dehydrogenases (composition chimique), Concentration en ions d'hydrogène (MeSH), Graphite (composition chimique), Modèles moléculaires (MeSH), Phanerochaete (enzymologie), Propriétés de surface (MeSH), Sensibilité et spécificité (MeSH), Techniques de biocapteur (MeSH), Électrons (MeSH).
- MESH :
- composition chimique : Carbohydrate dehydrogenases, Graphite.
- enzymologie : Basidiomycota, Phanerochaete.
- Adsorption, Concentration en ions d'hydrogène, Modèles moléculaires, Propriétés de surface, Sensibilité et spécificité, Techniques de biocapteur, Électrons.
English descriptors
- KwdEn :
- Adsorption (MeSH), Basidiomycota (enzymology), Biosensing Techniques (MeSH), Carbohydrate Dehydrogenases (chemistry), Electrons (MeSH), Graphite (chemistry), Hydrogen-Ion Concentration (MeSH), Models, Molecular (MeSH), Phanerochaete (enzymology), Sensitivity and Specificity (MeSH), Surface Properties (MeSH).
- MESH :
- chemical , chemistry : Carbohydrate Dehydrogenases, Graphite.
- enzymology : Basidiomycota, Phanerochaete.
- Adsorption, Biosensing Techniques, Electrons, Hydrogen-Ion Concentration, Models, Molecular, Sensitivity and Specificity, Surface Properties.
Abstract
This paper presents some functional differences as well as similarities observed when comparing the newly discovered cellobiose dehydrogenase (CDH) from Trametes villosa (T.v.) with the well-characterized one from Phanerochaete chrysosporium (P.c.). The enzymes were physically adsorbed on spectrographic graphite electrodes placed in an amperometric flow through cell connected to a flow system. In the case of T.v.-CDH-modified graphite electrodes, a high direct electron transfer (DET) current was registered at the polarized electrode in the presence of the enzyme substrate reflecting a very efficient internal electron transfer (IET) process between the reduced FAD-cofactor and the oxidized heme-cofactor. In the case of P.c.-CDH-modified graphite electrodes, the DET process is not as efficient, and the current will greatly increase in the presence of a mediator (mediated electron transfer, MET). As a consequence, when comparing the two types of enzyme-modified electrodes an inverted DET/MET ratio for T.v.-CDH is shown, in comparison with P.c.-CDH. The rates of the catalytic reaction were estimated to be comparable for both enzymes, by measuring the combined DET + MET currents. The inverted DET/MET ratio for T.v.-CDH-modified electrodes might suggest that probably there is a better docking between the two domains of this enzyme and that the linker region of P.c.-CDH might have an active role in modulating the rate of the IET (by changing the interdomain distance), with respect to pH. Based on the new properties of T.v.-CDH emphasized in the present study, an analytical application of a third-generation biosensor for lactose was recently published.
DOI: 10.1021/la061190f
PubMed: 17129063
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Direct electron transfer--a favorite electron route for cellobiose dehydrogenase (CDH) from Trametes villosa. Comparison with CDH from Phanerochaete chrysosporium.</title><author><name sortKey="Stoica, Leonard" sort="Stoica, Leonard" uniqKey="Stoica L" first="Leonard" last="Stoica">Leonard Stoica</name><affiliation wicri:level="1"><nlm:affiliation>Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-221 00, Lund</wicri:regionArea><wicri:noRegion>Lund</wicri:noRegion></affiliation></author><author><name sortKey="Ruzgas, Tautgirdas" sort="Ruzgas, Tautgirdas" uniqKey="Ruzgas T" first="Tautgirdas" last="Ruzgas">Tautgirdas Ruzgas</name></author><author><name sortKey="Ludwig, Roland" sort="Ludwig, Roland" uniqKey="Ludwig R" first="Roland" last="Ludwig">Roland Ludwig</name></author><author><name sortKey="Haltrich, Dietmar" sort="Haltrich, Dietmar" uniqKey="Haltrich D" first="Dietmar" last="Haltrich">Dietmar Haltrich</name></author><author><name sortKey="Gorton, Lo" sort="Gorton, Lo" uniqKey="Gorton L" first="Lo" last="Gorton">Lo Gorton</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:17129063</idno><idno type="pmid">17129063</idno><idno type="doi">10.1021/la061190f</idno><idno type="wicri:Area/Main/Corpus">000756</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000756</idno><idno type="wicri:Area/Main/Curation">000756</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000756</idno><idno type="wicri:Area/Main/Exploration">000756</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Direct electron transfer--a favorite electron route for cellobiose dehydrogenase (CDH) from Trametes villosa. Comparison with CDH from Phanerochaete chrysosporium.</title><author><name sortKey="Stoica, Leonard" sort="Stoica, Leonard" uniqKey="Stoica L" first="Leonard" last="Stoica">Leonard Stoica</name><affiliation wicri:level="1"><nlm:affiliation>Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-221 00, Lund, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-221 00, Lund</wicri:regionArea><wicri:noRegion>Lund</wicri:noRegion></affiliation></author><author><name sortKey="Ruzgas, Tautgirdas" sort="Ruzgas, Tautgirdas" uniqKey="Ruzgas T" first="Tautgirdas" last="Ruzgas">Tautgirdas Ruzgas</name></author><author><name sortKey="Ludwig, Roland" sort="Ludwig, Roland" uniqKey="Ludwig R" first="Roland" last="Ludwig">Roland Ludwig</name></author><author><name sortKey="Haltrich, Dietmar" sort="Haltrich, Dietmar" uniqKey="Haltrich D" first="Dietmar" last="Haltrich">Dietmar Haltrich</name></author><author><name sortKey="Gorton, Lo" sort="Gorton, Lo" uniqKey="Gorton L" first="Lo" last="Gorton">Lo Gorton</name></author></analytic><series><title level="j">Langmuir : the ACS journal of surfaces and colloids</title><idno type="ISSN">0743-7463</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adsorption (MeSH)</term><term>Basidiomycota (enzymology)</term><term>Biosensing Techniques (MeSH)</term><term>Carbohydrate Dehydrogenases (chemistry)</term><term>Electrons (MeSH)</term><term>Graphite (chemistry)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Sensitivity and Specificity (MeSH)</term><term>Surface Properties (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adsorption (MeSH)</term><term>Basidiomycota (enzymologie)</term><term>Carbohydrate dehydrogenases (composition chimique)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Graphite (composition chimique)</term><term>Modèles moléculaires (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Propriétés de surface (MeSH)</term><term>Sensibilité et spécificité (MeSH)</term><term>Techniques de biocapteur (MeSH)</term><term>Électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Graphite</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Carbohydrate dehydrogenases</term><term>Graphite</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adsorption</term><term>Biosensing Techniques</term><term>Electrons</term><term>Hydrogen-Ion Concentration</term><term>Models, Molecular</term><term>Sensitivity and Specificity</term><term>Surface Properties</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adsorption</term><term>Concentration en ions d'hydrogène</term><term>Modèles moléculaires</term><term>Propriétés de surface</term><term>Sensibilité et spécificité</term><term>Techniques de biocapteur</term><term>Électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">This paper presents some functional differences as well as similarities observed when comparing the newly discovered cellobiose dehydrogenase (CDH) from Trametes villosa (T.v.) with the well-characterized one from Phanerochaete chrysosporium (P.c.). The enzymes were physically adsorbed on spectrographic graphite electrodes placed in an amperometric flow through cell connected to a flow system. In the case of T.v.-CDH-modified graphite electrodes, a high direct electron transfer (DET) current was registered at the polarized electrode in the presence of the enzyme substrate reflecting a very efficient internal electron transfer (IET) process between the reduced FAD-cofactor and the oxidized heme-cofactor. In the case of P.c.-CDH-modified graphite electrodes, the DET process is not as efficient, and the current will greatly increase in the presence of a mediator (mediated electron transfer, MET). As a consequence, when comparing the two types of enzyme-modified electrodes an inverted DET/MET ratio for T.v.-CDH is shown, in comparison with P.c.-CDH. The rates of the catalytic reaction were estimated to be comparable for both enzymes, by measuring the combined DET + MET currents. The inverted DET/MET ratio for T.v.-CDH-modified electrodes might suggest that probably there is a better docking between the two domains of this enzyme and that the linker region of P.c.-CDH might have an active role in modulating the rate of the IET (by changing the interdomain distance), with respect to pH. Based on the new properties of T.v.-CDH emphasized in the present study, an analytical application of a third-generation biosensor for lactose was recently published.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17129063</PMID><DateCompleted><Year>2007</Year><Month>01</Month><Day>19</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>28</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0743-7463</ISSN><JournalIssue CitedMedium="Print"><Volume>22</Volume><Issue>25</Issue><PubDate><Year>2006</Year><Month>Dec</Month><Day>05</Day></PubDate></JournalIssue><Title>Langmuir : the ACS journal of surfaces and colloids</Title><ISOAbbreviation>Langmuir</ISOAbbreviation></Journal><ArticleTitle>Direct electron transfer--a favorite electron route for cellobiose dehydrogenase (CDH) from Trametes villosa. Comparison with CDH from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>10801-6</MedlinePgn></Pagination><Abstract><AbstractText>This paper presents some functional differences as well as similarities observed when comparing the newly discovered cellobiose dehydrogenase (CDH) from Trametes villosa (T.v.) with the well-characterized one from Phanerochaete chrysosporium (P.c.). The enzymes were physically adsorbed on spectrographic graphite electrodes placed in an amperometric flow through cell connected to a flow system. In the case of T.v.-CDH-modified graphite electrodes, a high direct electron transfer (DET) current was registered at the polarized electrode in the presence of the enzyme substrate reflecting a very efficient internal electron transfer (IET) process between the reduced FAD-cofactor and the oxidized heme-cofactor. In the case of P.c.-CDH-modified graphite electrodes, the DET process is not as efficient, and the current will greatly increase in the presence of a mediator (mediated electron transfer, MET). As a consequence, when comparing the two types of enzyme-modified electrodes an inverted DET/MET ratio for T.v.-CDH is shown, in comparison with P.c.-CDH. The rates of the catalytic reaction were estimated to be comparable for both enzymes, by measuring the combined DET + MET currents. The inverted DET/MET ratio for T.v.-CDH-modified electrodes might suggest that probably there is a better docking between the two domains of this enzyme and that the linker region of P.c.-CDH might have an active role in modulating the rate of the IET (by changing the interdomain distance), with respect to pH. 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