Influence of reduction on the fluorescent units and proton binding of humic acids: Synchronous fluorescence spectrum and NICA-Donnan modeling

Author(s):  
Juan Xiong ◽  
Yin Wei ◽  
Jinling Xu ◽  
Jingtao Hou ◽  
Zhaoyang Liu ◽  
...  
2017 ◽  
Vol 38 (4) ◽  
pp. 535-542
Author(s):  
石东坡 SHI Dong-po ◽  
尹先清 YIN Xian-qing ◽  
陈 武 CHEN Wu ◽  
郑延成 ZHENG Yan-cheng ◽  
付家新 FU Jia-xin ◽  
...  

2013 ◽  
Vol 726-731 ◽  
pp. 199-203
Author(s):  
Rui Xin Guo ◽  
Zhi Liang Wang ◽  
Zhi Jun Hu ◽  
Guo Ling Li ◽  
Jian Qiu Chen

The binding studies of imidacloprid to bovine serum albumin (BSA) were investigated by UV-Vis absorption spectrum, fluorescence spectrum and synchronous fluorescence spectrometry. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on BSA and the dynamic quenching constants () were 6.851×104 L.mol-1 and 5.813×104 L.mol-1 at 310 and 315 K, respectively, proving the mode of action of imidacloprid with BSA as a static quenching. In addition, according to the Vant Hoff equation, ΔGθ <0 showed="" the="" combination="" of="" imidacloprid="" and="" bsa="" was="" a="" spontaneous="" process="" h="" sup="">θ <0 and="" s="" sup="">θ> 0, indicated an electrostatic interaction process. At the same time, synchronous fluorescence spectrum of BSA could tell us whether the conformation of BSA was changed by imidacloprid.


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