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.
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This study was supported by the National Natural Science Foundation of China (No. 20907046) and the Undergraduate Scientific and Technological Innovation Project of Zhejiang Province (No. 2010R420014, No. 2012R420012).
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Xu, D., Jin, J., Shen, T. et al. Effect of Perfluorooctane Sulfonate on the Conformation of Wheat Germ Acid Phosphatase. Bull Environ Contam Toxicol 91, 577–582 (2013). https://doi.org/10.1007/s00128-013-1111-7
- Acid phosphatase
- Fluorescence spectroscopy