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

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.

Cubic Liquid Crystalline Nanostructures Involving Catalase and Curcumin: BioSAXS Study and Catalase Peroxidatic Function after Cubosomal Nanoparticle Treatment of Differentiated SH-SY5Y Cells

“…We established that the curcumin-containing dual-drug loaded nanoparticles (MO-FO-CU-CAT) maintain or increase the CAT activity (Figure 7), unlike other antioxidants, which can inhibit the catalase enzymatic function [56,57]. Molecular dynamic simulations have demonstrated that curcumin can significantly increase the activity of bovine liver catalase (BLC) as it favors the access of the substrate to the active site of the enzyme [59].…”

“…It should be emphasized that catalase undergoes rapid elimination from the bloodstream and is characterized by poor intracellular delivery. Thus, catalase exhibits a short half-life and poor operational stability and reusability as an enzyme, which limits its potential therapeutic applications [55,56,57,58,59,60]. The unstable biomacromolecule can be immobilized in order to increase its stability and improve its enzymatic performance, solubility and specificity [61,62,63,64,65,66,67].…”

Exploring the interactions of a Tb(III)–quercetin complex with serum albumins (HSA and BSA): spectroscopic and molecular docking studies

“…The inherent fluorescence emission of proteins is caused by three aromatic amino acid residues: tyrosine (Tyr), tryptophan (Trp), and phenylalanine (Phe). The Trp residue dominantly is responsible for observed inherent protein fluorescence, because of the low quantum yield of the Phe and Tyr residues . Trp fluorescence properties that come from the indole group in its structure are the most sensitive to its environment (polarity of its micro‐environment, noncovalent interactions, hydrogen bonding and denaturation) and can change upon interaction with various ligands (drugs or small molecules) and protein folding/unfolding.…”

A Sensitive, Simple and Direct Determination of Pantoprazole Based on a “Turn off-on” Fluorescence Nanosensor by Using Terbium-1,10-phenanthroline-silver Nanoparticles

“…These results confirmed the Tb(III)-phen-AgNPs system formation and energy transfer from Tb(III)-phen to AgNPs by the FRET process. 27,28 The Stern-Volmer equation was applied to a fluorescence quenching data analysis: 52,53…”