Abstract
2-mercaptothiazoline (2-MT) is widely used in many industrial fields, but its residue is potentially harmful to the environment. In this study, to evaluate the biological toxicity of 2-MT at protein level, the interaction between 2-MT and the pivotal antioxidant enzyme—catalase (CAT) was investigated using multiple spectroscopic techniques and molecular modeling. The results indicated that the CAT fluorescence quenching caused by 2-MT should be dominated by a static quenching mechanism through formation of a 2-MT/CAT complex. Furthermore, the identifications of the binding constant, binding forces, and the number of binding sites demonstrated that 2-MT could spontaneously interact with CAT at one binding site mainly via Van der Waals’ forces and hydrogen bonding. Based on the molecular docking simulation and conformation dynamic characterization, it was found that 2-MT could bind into the junctional region of CAT subdomains and that the binding site was close to enzyme active sites, which induced secondary structural and micro-environmental changes in CAT. The experiments on 2-MT toxicity verified that 2-MT significantly inhibited CAT activity via its molecular interaction, where 2-MT concentration and exposure time both affected the inhibitory action. Therefore, the present investigation provides useful information for understanding the toxicological mechanism of 2-MT at the molecular level.
Highlights
Catalase (CAT, hydrogen peroxide oxidoreductase; EC.1.11.1.6) is a common enzyme found in most living organisms exposed to oxygen, which plays a pivotal role in protecting cells from oxidative injuries by catalyzing the detoxification of hydrogen peroxide to oxygen and water (2H2O2 → O2↑ + 2H2O) [1,2]
2-Mercaptothiazoline is classified as a harmful organic compound, according to its Material 2S-aMfeteyrcDaaptatoSthheiaetz.oHliennecei,sthcelapsositfienetdialarsisak hofar2m-MfTulexoprgosaunriec tcooomrgpaonuisnmds,sahcocuoldrdbienginvtoestiitgsaMteda.terial SafetyTeDngateat aSlh. deeemt. oHnsetnractee,dththeatp2o-tMenTtcioaul lrdisbkinodf i2n-tMo sTiteeIxIp(sousbudroemtoaionrIgIIaAn)iosmf bsovsihnoeusledrubmeailnbvuemsitnig, ated
The interaction behaviors were further elucidated by molecular docking simulation and conformation dynamic characterization
Summary
Catalase (CAT, hydrogen peroxide oxidoreductase; EC.1.11.1.6) is a common enzyme found in most living organisms exposed to oxygen, which plays a pivotal role in protecting cells from oxidative injuries by catalyzing the detoxification of hydrogen peroxide to oxygen and water (2H2O2 → O2↑ + 2H2O) [1,2]. As an important antioxidant enzyme, the toxic effects of contaminants on CAT as well as their action mechanisms should be intensively investigated in vivo and in vitro. The interaction behaviors were further elucidated by molecular docking simulation and conformation dynamic characterization. The potential inhibitory effects of 2-MT on CAT activity caused by their interaction were verified by confirmatory experiments. C2h.aRreacsutelrtiszaantidonDoifsctuhessBioinnding Interaction between 2-MT and CAT by Fluorescence Analysis. 2.1.1.2F.1l.uCohraersaccetenrcizeatQiouneonf cthheinBgindMinegchInatneriascmtion between 2-MT and CAT by Fluorescence Analysis. T = 29Q1uKen. ching mechanisms are usually classified into either dynamic or static quenching. Since a higher temperature can result in a larger diffusion coefficient, the dynamic quenching constant. Spectra at d(1i)fferent where F and F0 respectively represent the fluorescence intensities with and without the quencher, [Q]. The maximum quenching rate constant (kq) is 2.0 × 1010 L·mol−1·s−1 [28]. 7.4 1 R is3t1h8e correlation coe1ff.2ic3ient; 2 S.D. is the standard 1d.e2v3iation for the K0S.V99v1a0lues.0.0391
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