Effect of perfluorooctane sulfonate on the conformation of wheat germ acid phosphatase.
Fluorescence spectroscopy was used to study the quenching mechanism, the type of force and the binding sites of perfluorooctane sulfonate (PFOS) on wheat germ acid phosphatase (ACPase). The results showed that the quenching effect of PFOS on ACPase was mainly due to a static quenching mechanism that occurred via the formation of hydrogen bonds and van der Waals forces. The results from synchronous fluorescence spectroscopy demonstrated that PFOS interacts with ACPase close to the tryptophan residues. In addition, synchronous fluorescence spectroscopy also showed that PFOS increases the hydrophobicity of the microenvironment of the tyrosine residues, hence decreasing the local polarity.
College of Biology and Environmental Engineering, Zhejiang Shuren University, Hangzhou, 310015, Zhejiang, China, dm25xu@163.com.
Dongmei
D
Xu
Jianchang
J
Jin
Tong
T
Shen
Yanhua
Y
Wang
D000135:Acid Phosphatase / Q000378:metabolism; D017738:Alkanesulfonic Acids / Q000633:toxicity*; D001665:Binding Sites; D005466:Fluorocarbons / Q000633:toxicity*; D006860:Hydrogen Bonding; D012989:Soil Pollutants / Q000633:toxicity*; D014908:Triticum / Q000187:drug effects* / Q000502:physiology; D014364:Tryptophan / Q000378:metabolism
D017738:Alkanesulfonic Acids; D005466:Fluorocarbons; D012989:Soil Pollutants; D014364:Tryptophan; C076994:perfluorooctane sulfonic acid; D000135:Acid Phosphatase