A poplar plastocyanin mutant suitable for adsorption onto gold surface via disulfide bridge.
Identifieur interne : 004676 ( Main/Corpus ); précédent : 004675; suivant : 004677A poplar plastocyanin mutant suitable for adsorption onto gold surface via disulfide bridge.
Auteurs : L. Andolfi ; S. Cannistraro ; G W Canters ; P. Facci ; A G Ficca ; I M C. Van Amsterdam ; M Ph VerbeetSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 2002.
English descriptors
- KwdEn :
- Adsorption (MeSH), Binding Sites (MeSH), Cysteine (genetics), Disulfides (chemistry), Electrochemistry (MeSH), Electrodes (MeSH), Electron Spin Resonance Spectroscopy (MeSH), Electron Transport (MeSH), Gold (chemistry), Microscopy, Scanning Tunneling (MeSH), Models, Molecular (MeSH), Mutagenesis, Site-Directed (MeSH), Mutation (MeSH), Oxidation-Reduction (MeSH), Plastocyanin (chemistry), Plastocyanin (genetics), Plastocyanin (physiology), Spectrophotometry (MeSH), Spectrum Analysis, Raman (MeSH), Trees (MeSH).
- MESH :
- chemical , chemistry : Disulfides, Gold, Plastocyanin.
- chemical , genetics : Cysteine, Plastocyanin.
- chemical , physiology : Plastocyanin.
- Adsorption, Binding Sites, Electrochemistry, Electrodes, Electron Spin Resonance Spectroscopy, Electron Transport, Microscopy, Scanning Tunneling, Models, Molecular, Mutagenesis, Site-Directed, Mutation, Oxidation-Reduction, Spectrophotometry, Spectrum Analysis, Raman, Trees.
Abstract
Aiming to achieve stable immobilization for a redox-active cupredoxin protein onto a gold substrate and its consequent molecular level monitoring by Scanning Tunnelling Microscopy (STM), we introduced a disulphide bridge within poplar plastocyanin, while avoiding the perturbation of its active site. We selected and modified residues Ile-21 to Cys and Glu-25 to Cys by structurally conservative mutagenesis. Optical absorption spectroscopy (UV-Vis), electron paramagnetic resonance (EPR), and resonance raman scattering (RRS) results indicate that the active site of the Ile21Cys, Glu25Cys plastocyanin (PCSS) to a large extent retains the spectroscopic properties of the wild-type protein. Furthermore, the redox midpoint potential of the couple CuII/CuI in PCSS, determined by cyclic voltammetry was found to be +348 mV close to the wild-type value. The STM images display self-assembled PCSS molecules immobilised onto gold substrate. Moreover, the full potentiostatic control of the electron transfer reaction during STM imaging, suggests that the adsorbed molecule maintains essentially its native redox properties.
DOI: 10.1006/abbi.2001.2735
PubMed: 11883906
Links to Exploration step
pubmed:11883906Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A poplar plastocyanin mutant suitable for adsorption onto gold surface via disulfide bridge.</title>
<author><name sortKey="Andolfi, L" sort="Andolfi, L" uniqKey="Andolfi L" first="L" last="Andolfi">L. Andolfi</name>
<affiliation><nlm:affiliation>INFM, Università della Tuscia, Viterbo, I-01100, Italy.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Cannistraro, S" sort="Cannistraro, S" uniqKey="Cannistraro S" first="S" last="Cannistraro">S. Cannistraro</name>
</author>
<author><name sortKey="Canters, G W" sort="Canters, G W" uniqKey="Canters G" first="G W" last="Canters">G W Canters</name>
</author>
<author><name sortKey="Facci, P" sort="Facci, P" uniqKey="Facci P" first="P" last="Facci">P. Facci</name>
</author>
<author><name sortKey="Ficca, A G" sort="Ficca, A G" uniqKey="Ficca A" first="A G" last="Ficca">A G Ficca</name>
</author>
<author><name sortKey="Van Amsterdam, I M C" sort="Van Amsterdam, I M C" uniqKey="Van Amsterdam I" first="I M C" last="Van Amsterdam">I M C. Van Amsterdam</name>
</author>
<author><name sortKey="Verbeet, M Ph" sort="Verbeet, M Ph" uniqKey="Verbeet M" first="M Ph" last="Verbeet">M Ph Verbeet</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">A poplar plastocyanin mutant suitable for adsorption onto gold surface via disulfide bridge.</title>
<author><name sortKey="Andolfi, L" sort="Andolfi, L" uniqKey="Andolfi L" first="L" last="Andolfi">L. Andolfi</name>
<affiliation><nlm:affiliation>INFM, Università della Tuscia, Viterbo, I-01100, Italy.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Cannistraro, S" sort="Cannistraro, S" uniqKey="Cannistraro S" first="S" last="Cannistraro">S. Cannistraro</name>
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<author><name sortKey="Canters, G W" sort="Canters, G W" uniqKey="Canters G" first="G W" last="Canters">G W Canters</name>
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<author><name sortKey="Facci, P" sort="Facci, P" uniqKey="Facci P" first="P" last="Facci">P. Facci</name>
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<author><name sortKey="Ficca, A G" sort="Ficca, A G" uniqKey="Ficca A" first="A G" last="Ficca">A G Ficca</name>
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<author><name sortKey="Van Amsterdam, I M C" sort="Van Amsterdam, I M C" uniqKey="Van Amsterdam I" first="I M C" last="Van Amsterdam">I M C. Van Amsterdam</name>
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<author><name sortKey="Verbeet, M Ph" sort="Verbeet, M Ph" uniqKey="Verbeet M" first="M Ph" last="Verbeet">M Ph Verbeet</name>
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<series><title level="j">Archives of biochemistry and biophysics</title>
<idno type="ISSN">0003-9861</idno>
<imprint><date when="2002" type="published">2002</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adsorption (MeSH)</term>
<term>Binding Sites (MeSH)</term>
<term>Cysteine (genetics)</term>
<term>Disulfides (chemistry)</term>
<term>Electrochemistry (MeSH)</term>
<term>Electrodes (MeSH)</term>
<term>Electron Spin Resonance Spectroscopy (MeSH)</term>
<term>Electron Transport (MeSH)</term>
<term>Gold (chemistry)</term>
<term>Microscopy, Scanning Tunneling (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Plastocyanin (chemistry)</term>
<term>Plastocyanin (genetics)</term>
<term>Plastocyanin (physiology)</term>
<term>Spectrophotometry (MeSH)</term>
<term>Spectrum Analysis, Raman (MeSH)</term>
<term>Trees (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term>
<term>Gold</term>
<term>Plastocyanin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine</term>
<term>Plastocyanin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Plastocyanin</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Adsorption</term>
<term>Binding Sites</term>
<term>Electrochemistry</term>
<term>Electrodes</term>
<term>Electron Spin Resonance Spectroscopy</term>
<term>Electron Transport</term>
<term>Microscopy, Scanning Tunneling</term>
<term>Models, Molecular</term>
<term>Mutagenesis, Site-Directed</term>
<term>Mutation</term>
<term>Oxidation-Reduction</term>
<term>Spectrophotometry</term>
<term>Spectrum Analysis, Raman</term>
<term>Trees</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Aiming to achieve stable immobilization for a redox-active cupredoxin protein onto a gold substrate and its consequent molecular level monitoring by Scanning Tunnelling Microscopy (STM), we introduced a disulphide bridge within poplar plastocyanin, while avoiding the perturbation of its active site. We selected and modified residues Ile-21 to Cys and Glu-25 to Cys by structurally conservative mutagenesis. Optical absorption spectroscopy (UV-Vis), electron paramagnetic resonance (EPR), and resonance raman scattering (RRS) results indicate that the active site of the Ile21Cys, Glu25Cys plastocyanin (PCSS) to a large extent retains the spectroscopic properties of the wild-type protein. Furthermore, the redox midpoint potential of the couple CuII/CuI in PCSS, determined by cyclic voltammetry was found to be +348 mV close to the wild-type value. The STM images display self-assembled PCSS molecules immobilised onto gold substrate. Moreover, the full potentiostatic control of the electron transfer reaction during STM imaging, suggests that the adsorbed molecule maintains essentially its native redox properties.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11883906</PMID>
<DateCompleted><Year>2002</Year>
<Month>03</Month>
<Day>21</Day>
</DateCompleted>
<DateRevised><Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN>
<JournalIssue CitedMedium="Print"><Volume>399</Volume>
<Issue>1</Issue>
<PubDate><Year>2002</Year>
<Month>Mar</Month>
<Day>01</Day>
</PubDate>
</JournalIssue>
<Title>Archives of biochemistry and biophysics</Title>
<ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation>
</Journal>
<ArticleTitle>A poplar plastocyanin mutant suitable for adsorption onto gold surface via disulfide bridge.</ArticleTitle>
<Pagination><MedlinePgn>81-8</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Aiming to achieve stable immobilization for a redox-active cupredoxin protein onto a gold substrate and its consequent molecular level monitoring by Scanning Tunnelling Microscopy (STM), we introduced a disulphide bridge within poplar plastocyanin, while avoiding the perturbation of its active site. We selected and modified residues Ile-21 to Cys and Glu-25 to Cys by structurally conservative mutagenesis. Optical absorption spectroscopy (UV-Vis), electron paramagnetic resonance (EPR), and resonance raman scattering (RRS) results indicate that the active site of the Ile21Cys, Glu25Cys plastocyanin (PCSS) to a large extent retains the spectroscopic properties of the wild-type protein. Furthermore, the redox midpoint potential of the couple CuII/CuI in PCSS, determined by cyclic voltammetry was found to be +348 mV close to the wild-type value. The STM images display self-assembled PCSS molecules immobilised onto gold substrate. Moreover, the full potentiostatic control of the electron transfer reaction during STM imaging, suggests that the adsorbed molecule maintains essentially its native redox properties.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Andolfi</LastName>
<ForeName>L</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>INFM, Università della Tuscia, Viterbo, I-01100, Italy.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cannistraro</LastName>
<ForeName>S</ForeName>
<Initials>S</Initials>
</Author>
<Author ValidYN="Y"><LastName>Canters</LastName>
<ForeName>G W</ForeName>
<Initials>GW</Initials>
</Author>
<Author ValidYN="Y"><LastName>Facci</LastName>
<ForeName>P</ForeName>
<Initials>P</Initials>
</Author>
<Author ValidYN="Y"><LastName>Ficca</LastName>
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<Author ValidYN="Y"><LastName>Van Amsterdam</LastName>
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<Author ValidYN="Y"><LastName>Verbeet</LastName>
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<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Arch Biochem Biophys</MedlineTA>
<NlmUniqueID>0372430</NlmUniqueID>
<ISSNLinking>0003-9861</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D004220">Disulfides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>7440-57-5</RegistryNumber>
<NameOfSubstance UI="D006046">Gold</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>9014-09-9</RegistryNumber>
<NameOfSubstance UI="D010970">Plastocyanin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>K848JZ4886</RegistryNumber>
<NameOfSubstance UI="D003545">Cysteine</NameOfSubstance>
</Chemical>
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<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000327" MajorTopicYN="N">Adsorption</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004563" MajorTopicYN="N">Electrochemistry</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004566" MajorTopicYN="N">Electrodes</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006046" MajorTopicYN="N">Gold</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016252" MajorTopicYN="N">Microscopy, Scanning Tunneling</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010970" MajorTopicYN="N">Plastocyanin</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013053" MajorTopicYN="N">Spectrophotometry</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013059" MajorTopicYN="N">Spectrum Analysis, Raman</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
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