Samaneh Rashtbari
1, Gholamreza Dehghan
1*, Reza Yekta
1, Abolghasem Jouyban
2, Mehrdad Iranshahi
31 Department of Biology, Faculty of Natural Sciences, University of Tabriz, Tabriz, Iran.
2 Pharmaceutical Analysis Research Center and Faculty of Pharmacy, Tabriz University of Medical Sciences, Tabriz, Iran.
3 Department of Pharmacognosy, Faculty of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran.
Abstract
Purpose: The
study on the interaction between various compounds and macromolecules such as
enzymes has been very important for monitoring the alteration of structural and
functional properties of them. Resveratrol (3, 5, 4-trihydroxy-stilbene; RES)
is a biologically active phytoallexin found in grapes and other food products.
This article shows an interaction of native bovine liver catalase (BLC) with
natural antioxidant product, trans resveratrol (tRES) using multispectroscopic
methods.
Methods: The
interaction between BLC and tRES is performed using UV-vis absorption,
fluorescence and circular dichroism (CD) spectroscopy and molecular docking
study.
Results: In
vitro kinetic studies indicated that tRES can decrease BLC
activity through uncompetitive inhibition. The results of spectroscopic methods
represented that the binding of tRES with BLC can change the micro-region
around aromatic amino acids (tryptophan (Trp) and tyrosine (Tyr)) and quench
intrinsic fluorescence of BLC by a static mechanism. According to fluorescence
quenching data analysis, it was revealed that tRES has one binding site on BLC.
The thermodynamic parameters were obtained, which demonstrated that tRES can
bind to BLC by van der Waals forces
and hydrogen bonds. Molecular docking results indicated that tRES binds
to BLC away from heme group and near to the Tyr 324 and Phe 265. These results
are in agreement with the experimental results.
Conclusion: The inhibitory effect of tRES
on BLC demonstrated that excessive consumption of the antioxidants could be
resulted in hazardous effects.