muramidase and 2-chlorophenol

The binding interactions of lysozyme with 2-chlorophenol, 2,4-dichlorophenol, 2,4,6-trichlorophenol and pentachlorophenol were investigated by UV-vis absorption, CD, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. The binding constants, quenching mechanism, and the number of binding sites were determined by the quenching of lysozyme fluorescence in presence of chlorophenols. H-bonds and hydrophobic interactions played major roles in stabilizing the chlorophenols-lysozyme complex. The distances r between chlorophenols and lysozyme were calculated to be 1.94nm, 2.75nm, 3.54nm, and 3.76nm for 2-CP, 2,4-DCP, 2,4,6-TCP, and PCP, respectively. The effects of chlorophenols on the conformation of lysozyme were analyzed using CD, synchronous fluorescence and three-dimensional fluorescence spectra.

Topics: Binding Sites; Chlorophenols; Circular Dichroism; Energy Transfer; Hydrogen Bonding; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Muramidase; Pentachlorophenol; Protein Binding; Protein Structure, Tertiary; Solutions; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Thermodynamics