Spectroscopy, calorimetry and molecular simulation studies on the interaction of catalase with copper ion

Zheng

J Biochem & Molecular Tox

et al. 2018

Self Cite

Because cadmium might interact with proteins and, thus, exert toxicity in organisms, it is vital to understand the molecular mechanism of the interaction between cadmium and biologically relevant proteins as well as the structural and functional changes in these proteins. In this study, the interaction between α-chymotrypsin (α-ChT) and cadmium chloride (CdCl 2 ) was investigated by performing enzyme activity determinations, multispectroscopic measurements, isothermal titration calorimetry, and molecular docking studies. It was demonstrated that CdCl 2 binds to α-ChT mainly via electrostatic forces with (21.0 ± 0.982) binding sites, leading to the increase of α-helix and the decrease of β-sheet. The interaction between CdCl 2 and α-ChT loosened the protein skeleton and increased the molecular volume of α-ChT. CdCl 2 first binds to the interface of α-ChT and then interacts with the key residues His 57 or Asp 102 or both in the active sites, leading to the activity inhibition of α-ChT under the exposure of high CdCl 2 concentrations. K E Y W O R D S cadmium, enzymatic activity, protein structure, α-chymotrypsin (α-ChT) J Biochem Mol Toxicol. 2019;33:e22248. wileyonlinelibrary.com/journal/jbt Additional supporting information may be found online in the Supporting Information section at the end of the article. How to cite this article: Wang J, Zheng X, Wang W, Guo H, Liu R, Zong W. A study on the interaction between cadmium and α-chymotrypsin and the underlying mechanisms.

Section: Resultsmentioning

confidence: 96%

A study on the interaction between cadmium and α‐chymotrypsin and the underlying mechanisms

Zheng

J Biochem & Molecular Tox

et al. 2018

Self Cite

“…As the characteristic peak of aromatic amino acids (TRP, TYR, and PHE), the band from 260 to 290 nm could reflect the microenvironment of these chromophores . The spectra in Figure showed that these two bands exhibited no shifts and no obvious intensity changes for SLS concentration ranging from 0.1 to 800 μM, suggesting no obvious change occurred in the framework conformation and the microenvironment around the aromatic amino acid residues of CAT …”

Section: Resultsmentioning

confidence: 99%

Investigation on the interaction of catalase with sodium lauryl sulfonate and the underlying mechanisms

J Biochem & Molecular Tox

Jia

Sun

et al. 2017

Self Cite

As a classic type of anionic surfactants, sodium lauryl sulfonate (SLS) might change the structure and function of antioxidant enzyme catalase (CAT) through their direct interactions. However, the underlying molecular mechanism is still unknown. This study investigated the direct interaction of SLS with CAT molecule and the underlying mechanisms using multi-spectroscopic methods, isothermal titration calorimetry, and molecular docking studies. No obvious effects were observed on CAT structure and activity under low SLS concentration exposure. The particle size of CAT molecule decreased and CAT activity was slightly inhibited under high SLS concentration exposure. SLS prefers to bind to the interface of CAT mainly via van der Waals' forces and hydrogen bonds. Subsequently, SLS interacts with the amino acid residues around the heme groups of CAT via hydrophobic interactions and might inhibit CAT activity.

“…Catalase activity was partially restored when samples were treated with CoHu after inactivation, while treatment before inactivation had a tendency to protect the enzyme ( Figure 10 ). Copper affects the secondary structure when it binds near a heme group in catalase, as well as the binding of Cu 2+ to bovine liver catalase destroyed H-bonds [ 29 ]. We specifically used the least damaging effect and the lowest effective concentration of the MFO so that irreversible damage to the enzymes did not occur, after which there would be no hope of any restoration of function.…”

Section: Discussionmentioning

confidence: 99%

Effect of Humid Air Exposed to IR Radiation on Enzyme Activity

Yablonskaya

Воейков

Новиков

et al. 2022

IJMS

Water vapor absorbs well in the infra-red region of the electromagnetic spectrum. Absorption of radiant energy by water or water droplets leads to formation of exclusion zone water that possesses peculiar physico-chemical properties. In the course of this study, normally functioning and damaged alkaline phosphatase, horseradish peroxidase and catalase were treated with humid air irradiated with infrared light with a wavelength in the range of 1270 nm and referred to as coherent humidity (CoHu). One-minute long treatment with CoHu helped to partially protect enzymes from heat inactivation, mixed function oxidation, and loss of activity due to partial unfolding. Authors suggest that a possible mechanism underlying the observed effects involves altering the physicochemical properties of aqueous media while treatment of the objects with CoHu where CoHu acts as an intermediary.