Modeling of laccase inhibition by formetanate pesticide using theoretical approaches
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.22/9203 |
Resumo: | The inhibition of laccase enzymatic catalytic activity by formetanate hydrochloride (FMT) was investigated by cyclic voltammetry and by quantum chemical calculations based on density functional theory with a protein fragmentation approach. The cyclic voltammograms were obtained using a biosensor prepared by enzyme immobilization on gold electrodes modified with gold nanoparticles and 4-aminophenol as the target molecule. The decrease in the peak current in the presence of FMT was used to characterize the inhibition process. The calculations identified Asp206 as the most relevant moiety in the interaction of FMT with the laccase enzymatic ligand binding domain. The amino acid residue Cys453 was important, because the Cys453–FMT interaction energy was not affected by the dielectric constant, although it was not a very close residue. This study provides an overview of how FMT inhibits laccase catalytic activity. |
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7160 |
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Modeling of laccase inhibition by formetanate pesticide using theoretical approachesEnzymatic catalysisInhibitionAmino acid residuesQuantum chemical calculationsDensity functional theoryMolecular dockingThe inhibition of laccase enzymatic catalytic activity by formetanate hydrochloride (FMT) was investigated by cyclic voltammetry and by quantum chemical calculations based on density functional theory with a protein fragmentation approach. The cyclic voltammograms were obtained using a biosensor prepared by enzyme immobilization on gold electrodes modified with gold nanoparticles and 4-aminophenol as the target molecule. The decrease in the peak current in the presence of FMT was used to characterize the inhibition process. The calculations identified Asp206 as the most relevant moiety in the interaction of FMT with the laccase enzymatic ligand binding domain. The amino acid residue Cys453 was important, because the Cys453–FMT interaction energy was not affected by the dielectric constant, although it was not a very close residue. This study provides an overview of how FMT inhibits laccase catalytic activity.ElsevierRepositório Científico do Instituto Politécnico do PortoMartins, Ana C. V.Ribeiro, Francisco W. P.Zanatta, GeancarloFreire, Valder N.Morais, SimoneLima-Neto, Pedro deCorreia, Adriana N.20162115-06-01T00:00:00Z2016-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.22/9203eng10.1016/j.bioelechem.2015.12.004metadata only accessinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-03-13T12:49:05Zoai:recipp.ipp.pt:10400.22/9203Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T17:28:47.373531Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Modeling of laccase inhibition by formetanate pesticide using theoretical approaches |
title |
Modeling of laccase inhibition by formetanate pesticide using theoretical approaches |
spellingShingle |
Modeling of laccase inhibition by formetanate pesticide using theoretical approaches Martins, Ana C. V. Enzymatic catalysis Inhibition Amino acid residues Quantum chemical calculations Density functional theory Molecular docking |
title_short |
Modeling of laccase inhibition by formetanate pesticide using theoretical approaches |
title_full |
Modeling of laccase inhibition by formetanate pesticide using theoretical approaches |
title_fullStr |
Modeling of laccase inhibition by formetanate pesticide using theoretical approaches |
title_full_unstemmed |
Modeling of laccase inhibition by formetanate pesticide using theoretical approaches |
title_sort |
Modeling of laccase inhibition by formetanate pesticide using theoretical approaches |
author |
Martins, Ana C. V. |
author_facet |
Martins, Ana C. V. Ribeiro, Francisco W. P. Zanatta, Geancarlo Freire, Valder N. Morais, Simone Lima-Neto, Pedro de Correia, Adriana N. |
author_role |
author |
author2 |
Ribeiro, Francisco W. P. Zanatta, Geancarlo Freire, Valder N. Morais, Simone Lima-Neto, Pedro de Correia, Adriana N. |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Repositório Científico do Instituto Politécnico do Porto |
dc.contributor.author.fl_str_mv |
Martins, Ana C. V. Ribeiro, Francisco W. P. Zanatta, Geancarlo Freire, Valder N. Morais, Simone Lima-Neto, Pedro de Correia, Adriana N. |
dc.subject.por.fl_str_mv |
Enzymatic catalysis Inhibition Amino acid residues Quantum chemical calculations Density functional theory Molecular docking |
topic |
Enzymatic catalysis Inhibition Amino acid residues Quantum chemical calculations Density functional theory Molecular docking |
description |
The inhibition of laccase enzymatic catalytic activity by formetanate hydrochloride (FMT) was investigated by cyclic voltammetry and by quantum chemical calculations based on density functional theory with a protein fragmentation approach. The cyclic voltammograms were obtained using a biosensor prepared by enzyme immobilization on gold electrodes modified with gold nanoparticles and 4-aminophenol as the target molecule. The decrease in the peak current in the presence of FMT was used to characterize the inhibition process. The calculations identified Asp206 as the most relevant moiety in the interaction of FMT with the laccase enzymatic ligand binding domain. The amino acid residue Cys453 was important, because the Cys453–FMT interaction energy was not affected by the dielectric constant, although it was not a very close residue. This study provides an overview of how FMT inhibits laccase catalytic activity. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016 2016-01-01T00:00:00Z 2115-06-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.22/9203 |
url |
http://hdl.handle.net/10400.22/9203 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1016/j.bioelechem.2015.12.004 |
dc.rights.driver.fl_str_mv |
metadata only access info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
metadata only access |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1817552360947318784 |