Martins Ana C V, Ribeiro Francisco W P, Zanatta Geancarlo, Freire Valder N, Morais Simone, de Lima-Neto Pedro, Correia Adriana N
Departamento de Química Analítica e Físico-Química, Centro de Ciências, Universidade Federal do Ceará, Bloco 940, Campus do Pici, 60440-900 Fortaleza, CE, Brazil.
Departamento de Bioquímica, Universidade Federal do Rio Grande do Sul, 90035-003 Porto Alegre, RS, Brazil.
Bioelectrochemistry. 2016 Apr;108:46-53. doi: 10.1016/j.bioelechem.2015.12.004. Epub 2015 Dec 21.
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.
采用循环伏安法以及基于密度泛函理论和蛋白质片段化方法的量子化学计算，研究了盐酸甲胺磷（FMT）对漆酶酶催化活性的抑制作用。循环伏安图是使用一种生物传感器获得的，该生物传感器通过将酶固定在修饰有金纳米颗粒和4-氨基苯酚的金电极上制备而成，以4-氨基苯酚作为目标分子。利用FMT存在时峰值电流的降低来表征抑制过程。计算确定天冬氨酸206是FMT与漆酶酶配体结合域相互作用中最相关的部分。氨基酸残基半胱氨酸453很重要，因为半胱氨酸453-FMT相互作用能不受介电常数影响，尽管它不是非常靠近的残基。本研究概述了FMT如何抑制漆酶催化活性。
