Spectroelectrochemical study of cellobiose dehydrogenase and diaphorase in a thiol-modified gold capillary in the absence of mediators.
Identifieur interne : 000A55 ( Main/Corpus ); précédent : 000A54; suivant : 000A56Spectroelectrochemical study of cellobiose dehydrogenase and diaphorase in a thiol-modified gold capillary in the absence of mediators.
Auteurs : T. Larsson ; A. Lindgren ; T. RuzgasSource :
- Bioelectrochemistry (Amsterdam, Netherlands) [ 1567-5394 ] ; 2001.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Carbohydrate Dehydrogenases, Dihydrolipoamide Dehydrogenase, Gold, Sulfhydryl Compounds.
- methods : Electrochemistry.
Abstract
A spectroelectrochemical cell was constructed from a gold capillary with 200 microm inner diameter as a working electrode. This allowed spectroelectrochemical study of liquid samples with available volumes less than 5 microl. The optical measurements were accomplished with an optical fibre spectrometer. The optical path of the cell was about 1 cm. To facilitate electrochemistry of biomolecules, the surface of the gold capillary was modified with thiols. The formal potential, E degrees', of the heme in cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium was determined by spectroelectrochemistry in the absence of redox mediators. The number of electrons per redox conversion of heme in CDH was found to be equal to 0.98 + 0.04 corresponding well to a theoretical value representing the redox reaction Fe3+ + e-= Fe2+. Similar spectroelectrochemical experiments with diaphorase from Bacillus stearothermophilus showed the redox conversion of the flavin mononucleotide in diaphorase in the absence of external redox mediators.
DOI: 10.1016/s0302-4598(01)00099-x
PubMed: 11339313
Links to Exploration step
pubmed:11339313Le document en format XML
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Ruzgas</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2001">2001</date><idno type="RBID">pubmed:11339313</idno><idno type="pmid">11339313</idno><idno type="doi">10.1016/s0302-4598(01)00099-x</idno><idno type="wicri:Area/Main/Corpus">000A55</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000A55</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Spectroelectrochemical study of cellobiose dehydrogenase and diaphorase in a thiol-modified gold capillary in the absence of mediators.</title><author><name sortKey="Larsson, T" sort="Larsson, T" uniqKey="Larsson T" first="T" last="Larsson">T. Larsson</name><affiliation><nlm:affiliation>Department of Physical Chemistry, Uppsala University, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Lindgren, A" sort="Lindgren, A" uniqKey="Lindgren A" first="A" last="Lindgren">A. Lindgren</name></author><author><name sortKey="Ruzgas, T" sort="Ruzgas, T" uniqKey="Ruzgas T" first="T" last="Ruzgas">T. Ruzgas</name></author></analytic><series><title level="j">Bioelectrochemistry (Amsterdam, Netherlands)</title><idno type="ISSN">1567-5394</idno><imprint><date when="2001" type="published">2001</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carbohydrate Dehydrogenases (chemistry)</term><term>Dihydrolipoamide Dehydrogenase (chemistry)</term><term>Electrochemistry (methods)</term><term>Gold (chemistry)</term><term>Sulfhydryl Compounds (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Dihydrolipoamide Dehydrogenase</term><term>Gold</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Electrochemistry</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A spectroelectrochemical cell was constructed from a gold capillary with 200 microm inner diameter as a working electrode. This allowed spectroelectrochemical study of liquid samples with available volumes less than 5 microl. The optical measurements were accomplished with an optical fibre spectrometer. The optical path of the cell was about 1 cm. To facilitate electrochemistry of biomolecules, the surface of the gold capillary was modified with thiols. The formal potential, E degrees', of the heme in cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium was determined by spectroelectrochemistry in the absence of redox mediators. The number of electrons per redox conversion of heme in CDH was found to be equal to 0.98 + 0.04 corresponding well to a theoretical value representing the redox reaction Fe3+ + e-= Fe2+. Similar spectroelectrochemical experiments with diaphorase from Bacillus stearothermophilus showed the redox conversion of the flavin mononucleotide in diaphorase in the absence of external redox mediators.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11339313</PMID><DateCompleted><Year>2001</Year><Month>09</Month><Day>20</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>04</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1567-5394</ISSN><JournalIssue CitedMedium="Print"><Volume>53</Volume><Issue>2</Issue><PubDate><Year>2001</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Bioelectrochemistry (Amsterdam, Netherlands)</Title><ISOAbbreviation>Bioelectrochemistry</ISOAbbreviation></Journal><ArticleTitle>Spectroelectrochemical study of cellobiose dehydrogenase and diaphorase in a thiol-modified gold capillary in the absence of mediators.</ArticleTitle><Pagination><MedlinePgn>243-9</MedlinePgn></Pagination><Abstract><AbstractText>A spectroelectrochemical cell was constructed from a gold capillary with 200 microm inner diameter as a working electrode. This allowed spectroelectrochemical study of liquid samples with available volumes less than 5 microl. The optical measurements were accomplished with an optical fibre spectrometer. The optical path of the cell was about 1 cm. To facilitate electrochemistry of biomolecules, the surface of the gold capillary was modified with thiols. The formal potential, E degrees', of the heme in cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium was determined by spectroelectrochemistry in the absence of redox mediators. The number of electrons per redox conversion of heme in CDH was found to be equal to 0.98 + 0.04 corresponding well to a theoretical value representing the redox reaction Fe3+ + e-= Fe2+. Similar spectroelectrochemical experiments with diaphorase from Bacillus stearothermophilus showed the redox conversion of the flavin mononucleotide in diaphorase in the absence of external redox mediators.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Larsson</LastName><ForeName>T</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Physical Chemistry, Uppsala University, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lindgren</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Ruzgas</LastName><ForeName>T</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>Netherlands</Country><MedlineTA>Bioelectrochemistry</MedlineTA><NlmUniqueID>100953583</NlmUniqueID><ISSNLinking>1567-5394</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>7440-57-5</RegistryNumber><NameOfSubstance UI="D006046">Gold</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>EC 1.8.1.4</RegistryNumber><NameOfSubstance UI="D008058">Dihydrolipoamide Dehydrogenase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008058" MajorTopicYN="N">Dihydrolipoamide Dehydrogenase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004563" MajorTopicYN="N">Electrochemistry</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006046" MajorTopicYN="N">Gold</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>5</Month><Day>8</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>9</Month><Day>21</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>5</Month><Day>8</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11339313</ArticleId><ArticleId IdType="pii">S0302-4598(01)00099-X</ArticleId><ArticleId IdType="doi">10.1016/s0302-4598(01)00099-x</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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