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Title 

The effect of trifluoroethanol on tyrosinase activity and conformation: Inhibition kinetics and computational simulations

Authors 

Z R LuL ShiJ WangDae Ui ParkJong Hwa ParkJ M YangY D ParkH W ZhouF Zou

Publisher 

Humana Press

Issue Date 

2010

Citation 

Applied Biochemistry and Biotechnology, vol. 160, no. 7, pp. 1896-1908

Keywords 

Docking simulationInhibition kineticsSecondary structureTrifluoroethanolTyrosinase

Abstract 

We studied the inhibitory effects of trifluoroethanol (TFE) on the activity and conformation of tyrosinase. TFE increased the degree of secondary structure of tyrosinase, which directly resulted in enzyme inactivation. A reciprocal study showed that TFE inhibited tyrosinase in a slope-parabolic mixed-type inhibition manner (K I=0.5±0.096 M). Time-interval kinetic studies showed that the inhibition was best described as first order with biphasic processes. Intrinsic and 1-anilinonaphthalene-8-sulfonate-binding fluorescences were also measured to gain more insight into the supposed structural changes; these showed that TFE induced a conspicuous tertiary structural change in tyrosinase by exposing hydrophobic surfaces. We also predicted the tertiary structure of tyrosinase and simulated its docking with TFE. The docking simulation was successful with significant scores (binding energy for Autodock4=-4.75 kcal/mol; for Dock6=-23.07 kcal/mol) and suggested that the TRP173 residue was mainly responsible for the interaction with TFE. Our results provide insight into the structure of tyrosinase and allow us to describe a new inhibition strategy that works by inducing conformational changes rather than targeting the active site of the protein.

ISSN 

0273-2289

Link 

http://dx.doi.org/10.1007/s12010-009-8730-9

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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