Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 118, Issue -, Pages 427-434Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2018.06.098
Keywords
Tyrosinase; Herbicides; Enzyme inhibition; Fluorescence spectroscopy; Computational Docking Analysis
Funding
- Generalitat de Catalunya [2015FI_B00523]
- Ministerio de Economia y Competitividad, Spain [BIO2012-30936]
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The inhibitory effect of 2,4,5-T, 2,4-D, glyphosate and paraquat on the diphenolase activity of mushroom tyrosinase for oxidation of L-DOPA has been investigated by kinetic measurements, fluorescence spectroscopy and computational docking analysis. 2,4,5-T and 2,4-D inhibit the diphenolase activity of the enzyme following a competitive mechanism, while glyphosate is a mixed inhibitor according to Lineweaver-Burk kinetic analysis. The inhibitory activity follows the order glyphosate >2,4,5-T > 2,4-D with IC50 values of 65, 90 and 106 mu M, respectively. Intrinsic tyrosinase fluorescence quenching and computational docking analysis suggest that 2,4,5-T and 2,4-D interact with the active site of the enzyme through hydrophobic interactions, while glyphosate also interacts with external residues of the active site of the enzyme by hydrogen bonding and hydrophilic interactions inducing conformational changes in the protein structure. (C) 2018 Elsevier B.V. All rights reserved.
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