Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance work on Wednesday 27th March 2019 from 11:00 AM to 1:00 PM (GMT).

During this time our website performance may be temporarily affected. We apologise for any inconvenience this might cause and thank you for your patience.


Issue 97, 2015
Previous Article Next Article

Molecular interaction of inorganic mercury(II) with catalase: a spectroscopic study in combination with molecular docking

Author affiliations

Abstract

The interaction between inorganic mercury(II) (Hg(II)) and catalase (CAT) was investigated using fluorescence, UV-visible absorption (UV-vis), circular dichroism (CD) spectroscopic techniques and molecular docking methods under simulated physiological conditions (in Tris–HCl buffer, pH = 7.40). The fluorescence quenching analysis showed that the intrinsic fluorescence of CAT was quenched by Hg(II) through a static quenching mechanism. Hg(II) can bind with CAT to form a Hg(II)–CAT complex, with a binding constant of 13.24 L mol−1 at 295 K. Thermodynamic analysis indicated that electrostatic force and van der Waals forces were the dominant intermolecular forces in stabilizing the complex. The results of UV-vis absorption and CD spectral analysis indicated that the formation of the Hg(II)–CAT complex induced some conformational changes in CAT, increasing and decreasing its α-helical content at low and high concentrations of Hg(II), respectively. The CAT activity can be inhibited by Hg(II) significantly, about a 67.2% drop with the presence of 5.0 × 10−4 mol L−1 Hg(II), and the relative activity values of CAT showed a good linear relationship with its fluorescence intensity. Molecular docking was employed to further investigate the interaction of CAT with different species of Hg(II) (HgCl2, [HgCl3] and [HgCl4]2−), to seek the optimum binding sites of Hg(II) in CAT, and to obtain detailed binding information. This study contributes to the understanding of the interaction mechanism between Hg(II) and CAT at the molecular level in vitro, which is helpful for clarifying the toxicity mechanism of Hg(II) on an antioxidant enzyme system in vivo.

Graphical abstract: Molecular interaction of inorganic mercury(ii) with catalase: a spectroscopic study in combination with molecular docking

Back to tab navigation

Supplementary files

Publication details

The article was received on 31 Jul 2015, accepted on 14 Sep 2015 and first published on 14 Sep 2015


Article type: Paper
DOI: 10.1039/C5RA15301H
Author version
available:
Download author version (PDF)
Citation: RSC Adv., 2015,5, 79874-79881

  •   Request permissions

    Molecular interaction of inorganic mercury(II) with catalase: a spectroscopic study in combination with molecular docking

    L. Chen, J. Zhang, Y. Zhu and Y. Zhang, RSC Adv., 2015, 5, 79874
    DOI: 10.1039/C5RA15301H

Search articles by author

Spotlight

Advertisements