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Adv Pharm Bull. 2017;7(3): 349-357.
doi: 10.15171/apb.2017.042
PMID: 29071216
PMCID: PMC5651055
Scopus ID: 85030117458
  Abstract View: 2207
  PDF Download: 1605

Research Article

Effects of Resveratrol on the Structure and Catalytic Function of Bovine Liver catalase (BLC): Spectroscopic and Theoretical Studies

Samaneh Rashtbari 1, Gholamreza Dehghan 1*, Reza Yekta 1, Abolghasem Jouyban 2, Mehrdad Iranshahi 3

1 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.
*Corresponding Author: Email: gdehghan@tabrizu.ac.ir

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.
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Submitted: 07 May 2017
Revision: 25 Jun 2017
Accepted: 05 Jul 2017
ePublished: 25 Sep 2017
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