Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases.
Identifieur interne : 000164 ( Main/Curation ); précédent : 000163; suivant : 000165Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases.
Auteurs : Sandra Acebes [Espagne] ; Francisco J. Ruiz-Due As [Espagne] ; Mario Toubes [Espagne] ; Veronica Sáez-Jiménez [Espagne] ; Marta Pérez-Boada [Espagne] ; M Fátima Lucas [Espagne] ; Angel T. Martínez [Espagne] ; Victor Guallar [Espagne]Source :
- The journal of physical chemistry. B [ 1520-5207 ] ; 2017.
Descripteurs français
- KwdFr :
- Lignine (métabolisme), Modèles moléculaires (MeSH), Mutagenèse dirigée (MeSH), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Pleurotus (composition chimique), Pleurotus (enzymologie), Pleurotus (génétique), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH), Transport d'électrons (MeSH).
- MESH :
- composition chimique : Peroxidases, Pleurotus.
- enzymologie : Pleurotus.
- génétique : Peroxidases, Pleurotus.
- métabolisme : Lignine, Peroxidases.
- Modèles moléculaires, Mutagenèse dirigée, Oxydoréduction, Spécificité du substrat, Séquence d'acides aminés, Transport d'électrons.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Electron Transport (MeSH), Lignin (metabolism), Models, Molecular (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Pleurotus (chemistry), Pleurotus (enzymology), Pleurotus (genetics), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Peroxidases.
- chemical , genetics : Peroxidases.
- chemical , metabolism : Lignin, Peroxidases.
- chemistry : Pleurotus.
- enzymology : Pleurotus.
- genetics : Pleurotus.
- Amino Acid Sequence, Electron Transport, Models, Molecular, Mutagenesis, Site-Directed, Oxidation-Reduction, Substrate Specificity.
Abstract
Combining a computational analysis with site-directed mutagenesis, we have studied the long-range electron transfer pathway in versatile and lignin peroxidases, two enzymes of biotechnological interest that play a key role for fungal degradation of the bulky lignin molecule in plant biomass. The in silico study established two possible electron transfer routes starting at the surface tryptophan residue previously identified as responsible for oxidation of the bulky lignin polymer. Moreover, in both enzymes, a second buried tryptophan residue appears as a top electron transfer carrier, indicating the prevalence of one pathway. Site-directed mutagenesis of versatile peroxidase (from Pleurotus eryngii) allowed us to corroborate the computational analysis and the role played by the buried tryptophan (Trp244) and a neighbor phenylalanine residue (Phe198), together with the surface tryptophan, in the electron transfer. These three aromatic residues are highly conserved in all the sequences analyzed (up to a total of 169). The importance of the surface (Trp171) and buried (Trp251) tryptophan residues in lignin peroxidase has been also confirmed by directed mutagenesis of the Phanerochaete chrysosporium enzyme. Overall, the combined procedure identifies analogous electron transfer pathways in the long-range oxidation mechanism for both ligninolytic peroxidases, constituting a good example of how computational analysis avoids making extensive trial-error mutagenic experiments.
DOI: 10.1021/acs.jpcb.7b00835
PubMed: 28375014
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Electron Transport (MeSH)</term>
<term>Lignin (metabolism)</term>
<term>Models, Molecular (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peroxidases (chemistry)</term>
<term>Peroxidases (genetics)</term>
<term>Peroxidases (metabolism)</term>
<term>Pleurotus (chemistry)</term>
<term>Pleurotus (enzymology)</term>
<term>Pleurotus (genetics)</term>
<term>Substrate Specificity (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Lignine (métabolisme)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Mutagenèse dirigée (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Peroxidases (composition chimique)</term>
<term>Peroxidases (génétique)</term>
<term>Peroxidases (métabolisme)</term>
<term>Pleurotus (composition chimique)</term>
<term>Pleurotus (enzymologie)</term>
<term>Pleurotus (génétique)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Transport d'électrons (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term>
<term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Pleurotus</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Peroxidases</term>
<term>Pleurotus</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Pleurotus</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Pleurotus</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Pleurotus</term>
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<term>Pleurotus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term>
<term>Peroxidases</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Electron Transport</term>
<term>Models, Molecular</term>
<term>Mutagenesis, Site-Directed</term>
<term>Oxidation-Reduction</term>
<term>Substrate Specificity</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Modèles moléculaires</term>
<term>Mutagenèse dirigée</term>
<term>Oxydoréduction</term>
<term>Spécificité du substrat</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Combining a computational analysis with site-directed mutagenesis, we have studied the long-range electron transfer pathway in versatile and lignin peroxidases, two enzymes of biotechnological interest that play a key role for fungal degradation of the bulky lignin molecule in plant biomass. The in silico study established two possible electron transfer routes starting at the surface tryptophan residue previously identified as responsible for oxidation of the bulky lignin polymer. Moreover, in both enzymes, a second buried tryptophan residue appears as a top electron transfer carrier, indicating the prevalence of one pathway. Site-directed mutagenesis of versatile peroxidase (from Pleurotus eryngii) allowed us to corroborate the computational analysis and the role played by the buried tryptophan (Trp244) and a neighbor phenylalanine residue (Phe198), together with the surface tryptophan, in the electron transfer. These three aromatic residues are highly conserved in all the sequences analyzed (up to a total of 169). The importance of the surface (Trp171) and buried (Trp251) tryptophan residues in lignin peroxidase has been also confirmed by directed mutagenesis of the Phanerochaete chrysosporium enzyme. Overall, the combined procedure identifies analogous electron transfer pathways in the long-range oxidation mechanism for both ligninolytic peroxidases, constituting a good example of how computational analysis avoids making extensive trial-error mutagenic experiments.</div>
</front>
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<Title>The journal of physical chemistry. B</Title>
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<ArticleTitle>Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases.</ArticleTitle>
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<Abstract><AbstractText>Combining a computational analysis with site-directed mutagenesis, we have studied the long-range electron transfer pathway in versatile and lignin peroxidases, two enzymes of biotechnological interest that play a key role for fungal degradation of the bulky lignin molecule in plant biomass. The in silico study established two possible electron transfer routes starting at the surface tryptophan residue previously identified as responsible for oxidation of the bulky lignin polymer. Moreover, in both enzymes, a second buried tryptophan residue appears as a top electron transfer carrier, indicating the prevalence of one pathway. Site-directed mutagenesis of versatile peroxidase (from Pleurotus eryngii) allowed us to corroborate the computational analysis and the role played by the buried tryptophan (Trp244) and a neighbor phenylalanine residue (Phe198), together with the surface tryptophan, in the electron transfer. These three aromatic residues are highly conserved in all the sequences analyzed (up to a total of 169). The importance of the surface (Trp171) and buried (Trp251) tryptophan residues in lignin peroxidase has been also confirmed by directed mutagenesis of the Phanerochaete chrysosporium enzyme. Overall, the combined procedure identifies analogous electron transfer pathways in the long-range oxidation mechanism for both ligninolytic peroxidases, constituting a good example of how computational analysis avoids making extensive trial-error mutagenic experiments.</AbstractText>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Acebes</LastName>
<ForeName>Sandra</ForeName>
<Initials>S</Initials>
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<Author ValidYN="Y"><LastName>Ruiz-Dueñas</LastName>
<ForeName>Francisco J</ForeName>
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<Author ValidYN="Y"><LastName>Toubes</LastName>
<ForeName>Mario</ForeName>
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<ForeName>Marta</ForeName>
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<Author ValidYN="Y"><LastName>Lucas</LastName>
<ForeName>M Fátima</ForeName>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Anaxomics Biotech , Balmes 89, 08008 Barcelona, Spain.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Martínez</LastName>
<ForeName>Angel T</ForeName>
<Initials>AT</Initials>
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<AffiliationInfo><Affiliation>Centro de Investigaciones Biológicas, CSIC , Ramiro de Maeztu 9, E-28040 Madrid, Spain.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Guallar</LastName>
<ForeName>Victor</ForeName>
<Initials>V</Initials>
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<AffiliationInfo><Affiliation>Barcelona Supercomputing Center, Joint BSC-CRG-IRB Research Program in Computational Biology , Jordi Girona 29, E-08034 Barcelona, Spain.</Affiliation>
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<AffiliationInfo><Affiliation>ICREA , Passeig Lluís Companys 23, E-08010 Barcelona, Spain.</Affiliation>
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<Month>04</Month>
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<ISSNLinking>1520-5207</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>9005-53-2</RegistryNumber>
<NameOfSubstance UI="D008031">Lignin</NameOfSubstance>
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<Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber>
<NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance>
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<MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName>
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<MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName>
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<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
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