Study on the interaction mechanism of lysozyme and bromophenol blue by fluorescence spectroscopy.
The interaction of lysozyme with bromophenol blue (BPB) in acetate buffer (pH 6.0) was studied by fluorescence quenching method for the first time. It was found that BPB could conspicuously quench the fluorescence of lysozyme by the static quenching process, possibly due to the binding on the active site near Trp62. The binding parameters including the binding constant and the number of binding site were calculated. The thermodynamic parameters DeltaH degrees, DeltaS degrees and DeltaG degrees at different temperatures were obtained. The formation of lysozyme-BPB complex depended on the cooperation of the hydrophobic and electrostatic forces. And the binding average distance between lysozyme and BPB was determined. The effect of common metal ions on the binding constant of lysozyme-BPB was also examined.
Yue
Qiaoli
Q
Department of Chemistry, Northwest University, Xi'an, 710069 China.
Niu
Lichuan
L
Li
Xin
X
Shao
Xiaodong
X
Xie
Xiaofeng
X
Song
Zhenghua
Z
D001978:Bromphenol Blue / Q000378:metabolism*; D004735:Energy Transfer; D009113:Muramidase / Q000378:metabolism*; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
D001978:Bromphenol Blue; D009113:Muramidase