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Investigation on the interaction of catalase with sodium lauryl sulfonate and the underlying mechanisms
Author(s) -
Wang Jing,
Jia Rui,
Wang Jiaxi,
Sun Zhiqiang,
Wu Zitao,
Liu Rutao,
Zong Wansong
Publication year - 2018
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.22025
Subject(s) - chemistry , isothermal titration calorimetry , hydrogen bond , sulfonate , catalase , van der waals force , hydrophobic effect , sodium , molecule , isothermal microcalorimetry , heme , biophysics , stereochemistry , antioxidant , enzyme , organic chemistry , biochemistry , enthalpy , thermodynamics , physics , biology
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.