The nature of tryptophan radicals involved in the long-range electron transfer of lignin peroxidase and lignin peroxidase-like systems: Insights from quantum mechanical/molecular mechanics simulations.
Identifieur interne : 000410 ( Main/Exploration ); précédent : 000409; suivant : 000411The nature of tryptophan radicals involved in the long-range electron transfer of lignin peroxidase and lignin peroxidase-like systems: Insights from quantum mechanical/molecular mechanics simulations.
Auteurs : Caterina Bernini [Italie] ; Rebecca Pogni ; Riccardo Basosi ; Adalgisa SinicropiSource :
- Proteins [ 1097-0134 ] ; 2012.
Descripteurs français
- KwdFr :
- Ions (composition chimique), Ions (métabolisme), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Simulation de dynamique moléculaire (MeSH), Transport d'électrons (MeSH), Tryptophane (composition chimique), Tryptophane (métabolisme).
- MESH :
- composition chimique : Ions, Peroxidases, Tryptophane.
- enzymologie : Phanerochaete.
- métabolisme : Ions, Peroxidases, Tryptophane.
- Oxydoréduction, Simulation de dynamique moléculaire, Transport d'électrons.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Ions, Peroxidases, Tryptophan.
- chemical , metabolism : Ions, Peroxidases, Tryptophan.
- enzymology : Phanerochaete.
- Electron Transport, Molecular Dynamics Simulation, Oxidation-Reduction.
Abstract
A catalytically active tryptophan radical has been demonstrated to be involved in the long-range electron transfer to the heme cofactor of lignin peroxidase (LiP) from Phanerochaete chrysosporium although no direct detection by EPR spectroscopy of the tryptophan radical intermediate has been reported to date. An engineering-based approach has been used to manipulate the microenvironment of the redox-active tryptophan site in LiP and Coprinus cinereus Peroxidase (CiP), allowing the direct evidence of the tryptophan radical species. In light of the newly available EPR experimental data, we performed a quantum mechanical/molecular mechanics computational study to characterize the tryptophan radicals in the above protein matrices as well as in pristine LiP. The nature of the tryptophan radicals is discussed together with the analysis of their environment with the aim of understanding the different behavior of pristine LiP in comparison with that of LiP and CiP variants.
DOI: 10.1002/prot.24046
PubMed: 22383280
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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last="Basosi">Riccardo Basosi</name></author><author><name sortKey="Sinicropi, Adalgisa" sort="Sinicropi, Adalgisa" uniqKey="Sinicropi A" first="Adalgisa" last="Sinicropi">Adalgisa Sinicropi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22383280</idno><idno type="pmid">22383280</idno><idno type="doi">10.1002/prot.24046</idno><idno type="wicri:Area/Main/Corpus">000446</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000446</idno><idno type="wicri:Area/Main/Curation">000446</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000446</idno><idno type="wicri:Area/Main/Exploration">000446</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The nature of tryptophan radicals involved in the long-range electron transfer of lignin peroxidase and lignin peroxidase-like systems: Insights from quantum mechanical/molecular mechanics simulations.</title><author><name sortKey="Bernini, Caterina" sort="Bernini, Caterina" uniqKey="Bernini C" first="Caterina" last="Bernini">Caterina Bernini</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Siena, Siena 53100, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Siena, Siena 53100</wicri:regionArea><wicri:noRegion>Siena 53100</wicri:noRegion></affiliation></author><author><name sortKey="Pogni, Rebecca" sort="Pogni, Rebecca" uniqKey="Pogni R" first="Rebecca" last="Pogni">Rebecca Pogni</name></author><author><name sortKey="Basosi, Riccardo" sort="Basosi, Riccardo" uniqKey="Basosi R" first="Riccardo" last="Basosi">Riccardo Basosi</name></author><author><name sortKey="Sinicropi, Adalgisa" sort="Sinicropi, Adalgisa" uniqKey="Sinicropi A" first="Adalgisa" last="Sinicropi">Adalgisa Sinicropi</name></author></analytic><series><title 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(composition chimique)</term><term>Tryptophane (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Ions</term><term>Peroxidases</term><term>Tryptophan</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Ions</term><term>Peroxidases</term><term>Tryptophan</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Ions</term><term>Peroxidases</term><term>Tryptophane</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 scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Ions</term><term>Peroxidases</term><term>Tryptophane</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Transport</term><term>Molecular Dynamics Simulation</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Oxydoréduction</term><term>Simulation de dynamique moléculaire</term><term>Transport d'électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A catalytically active tryptophan radical has been demonstrated to be involved in the long-range electron transfer to the heme cofactor of lignin peroxidase (LiP) from Phanerochaete chrysosporium although no direct detection by EPR spectroscopy of the tryptophan radical intermediate has been reported to date. An engineering-based approach has been used to manipulate the microenvironment of the redox-active tryptophan site in LiP and Coprinus cinereus Peroxidase (CiP), allowing the direct evidence of the tryptophan radical species. In light of the newly available EPR experimental data, we performed a quantum mechanical/molecular mechanics computational study to characterize the tryptophan radicals in the above protein matrices as well as in pristine LiP. The nature of the tryptophan radicals is discussed together with the analysis of their environment with the aim of understanding the different behavior of pristine LiP in comparison with that of LiP and CiP variants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22383280</PMID><DateCompleted><Year>2012</Year><Month>09</Month><Day>20</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1097-0134</ISSN><JournalIssue CitedMedium="Internet"><Volume>80</Volume><Issue>5</Issue><PubDate><Year>2012</Year><Month>May</Month></PubDate></JournalIssue><Title>Proteins</Title><ISOAbbreviation>Proteins</ISOAbbreviation></Journal><ArticleTitle>The nature of tryptophan radicals involved in the long-range electron transfer of lignin peroxidase and lignin peroxidase-like systems: Insights from quantum mechanical/molecular mechanics simulations.</ArticleTitle><Pagination><MedlinePgn>1476-83</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/prot.24046</ELocationID><Abstract><AbstractText>A catalytically active tryptophan radical has been demonstrated to be involved in the long-range electron transfer to the heme cofactor of lignin peroxidase (LiP) from Phanerochaete chrysosporium although no direct detection by EPR spectroscopy of the tryptophan radical intermediate has been reported to date. An engineering-based approach has been used to manipulate the microenvironment of the redox-active tryptophan site in LiP and Coprinus cinereus Peroxidase (CiP), allowing the direct evidence of the tryptophan radical species. In light of the newly available EPR experimental data, we performed a quantum mechanical/molecular mechanics computational study to characterize the tryptophan radicals in the above protein matrices as well as in pristine LiP. The nature of the tryptophan radicals is discussed together with the analysis of their environment with the aim of understanding the different behavior of pristine LiP in comparison with that of LiP and CiP variants.</AbstractText><CopyrightInformation>Copyright © 2012 Wiley Periodicals, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bernini</LastName><ForeName>Caterina</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Siena, Siena 53100, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pogni</LastName><ForeName>Rebecca</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Basosi</LastName><ForeName>Riccardo</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Sinicropi</LastName><ForeName>Adalgisa</ForeName><Initials>A</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>2012</Year><Month>03</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proteins</MedlineTA><NlmUniqueID>8700181</NlmUniqueID><ISSNLinking>0887-3585</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007477">Ions</NameOfSubstance></Chemical><Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber><NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007477" MajorTopicYN="N">Ions</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D056004" MajorTopicYN="Y">Molecular Dynamics Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>10</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>01</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>01</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>3</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>3</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>9</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22383280</ArticleId><ArticleId IdType="doi">10.1002/prot.24046</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><noCountry><name sortKey="Basosi, Riccardo" sort="Basosi, Riccardo" uniqKey="Basosi R" first="Riccardo" last="Basosi">Riccardo Basosi</name><name sortKey="Pogni, Rebecca" sort="Pogni, Rebecca" uniqKey="Pogni R" first="Rebecca" last="Pogni">Rebecca Pogni</name><name sortKey="Sinicropi, Adalgisa" sort="Sinicropi, Adalgisa" uniqKey="Sinicropi A" first="Adalgisa" last="Sinicropi">Adalgisa Sinicropi</name></noCountry><country name="Italie"><noRegion><name sortKey="Bernini, Caterina" sort="Bernini, Caterina" uniqKey="Bernini C" first="Caterina" last="Bernini">Caterina Bernini</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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