کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1273779 | 1496905 | 2016 | 8 صفحه PDF | دانلود رایگان |
• This study provides an overview of how FMT inhibits laccase catalytic activity.
• Interaction energies obtained for 155 residues had the interaction radius of 15 Å.
• Asp206 is the most relevant moiety in the interaction between Lac and FMT.
• Cys453–FMT interaction energy was not affected by the dielectric constant.
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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Journal: Bioelectrochemistry - Volume 108, April 2016, Pages 46–53