%0 Journal Article %1 WOS:000368222600007 %A Martins, Ana C V %A Ribeiro, Francisco W P %A Zanatta, Geancarlo %A Freire, Valder N %A Morais, Simone %A de Lima-Neto, Pedro %A Correia, Adriana N %C PO BOX 564, 1001 LAUSANNE, SWITZERLAND %D 2016 %I ELSEVIER SCIENCE SA %J BIOELECTROCHEMISTRY %K Amino Density Inhibition; Molecular Quantum acid calculations; catalysis; chemical docking} functional residues; theory; {Enzymatic %P 46-53 %R 10.1016/j.bioelechem.2015.12.004 %T Modeling of laccase inhibition by formetanate pesticide using theoretical approaches %V 108 %X 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. (C) 2015 Elsevier B.V. All rights reserved.

@article{WOS:000368222600007, abstract = {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. (C) 2015 Elsevier B.V. All rights reserved.}, added-at = {2022-05-23T20:00:14.000+0200}, address = {PO BOX 564, 1001 LAUSANNE, SWITZERLAND}, author = {Martins, Ana C V and Ribeiro, Francisco W P and Zanatta, Geancarlo and Freire, Valder N and Morais, Simone and de Lima-Neto, Pedro and Correia, Adriana N}, biburl = {https://www.bibsonomy.org/bibtex/2cc0aad54d74cad25c7c9c798ef58090c/ppgfis_ufc_br}, doi = {10.1016/j.bioelechem.2015.12.004}, interhash = {6699d8f168c78ea20b939484d4cd4d06}, intrahash = {cc0aad54d74cad25c7c9c798ef58090c}, issn = {1567-5394}, journal = {BIOELECTROCHEMISTRY}, keywords = {Amino Density Inhibition; Molecular Quantum acid calculations; catalysis; chemical docking} functional residues; theory; {Enzymatic}, pages = {46-53}, publisher = {ELSEVIER SCIENCE SA}, pubstate = {published}, timestamp = {2022-05-23T20:00:14.000+0200}, title = {Modeling of laccase inhibition by formetanate pesticide using theoretical approaches}, tppubtype = {article}, volume = 108, year = 2016 }