Abstract
Heavy metal chromium (Cr) poses a severe health risk to humans via food chain contamination. In this study, the interactions of either trivalent chromium (Cr(III)) or hexavalent chromium (Cr(VI)) with catalase (CAT) were investigated via multi-spectroscopic studies and computational simulations. The fluorescence analysis showed that Cr(III) and Cr(VI) quenched the fluorescence of CAT through a dynamic and a static quenching mechanism, respectively. The binding constant of Cr(VI) with CAT was 3.44×104lmol−1 at 298K. Other detailed binding characterizations of the Cr(VI)–CAT complex were also obtained using spectra analysis and molecular docking. Synchronous fluorescence, UV–vis and circular dichroism (CD) spectral studies showed that either Cr(III) or Cr(VI) induced conformational changes of CAT, but the degree of influence was different. The response of CAT activity to Cr(III) or Cr(VI) was found to be variable depending on their valence states and concentrations.
Published Version
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