Studies on the interactions of 2, 4-dinitrophenol and 2, 4-dichlorphenol with trypsin.
The interactions of 2, 4-dinitrophenol and 2, 4-dichlorphenol with trypsin were investigated by fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. The 2, 4-dinitrophenol and 2, 4-dichlorphenol effectively quenched the intrinsic fluorescence of trypsin via static quenching. The process of binding 2, 4-dinitrophenol and 2, 4-dichlorphenol with trypsin was a spontaneous molecular interaction procedure. The electrostatic repulsion does favor the interaction between 2, 4-DNP and trypsin. However, the interaction of 2, 4-DCP and trypsin can be explained on the basis of hydrogen bonding and van der Waals. The results of synchronous fluorescence spectroscopy and three-dimensional fluorescence spectra indicated that the structure of these trytophan and tyrosine residues environments were altered by 2, 4-DNP and 2, 4-DCP.
Zhang
Hong-Mei
HM
Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Institute of Applied Chemistry and Environmental Engineering, Yancheng Teachers University, Yancheng City, Jiangsu Province 224002, People's Republic of China.
Zhou
Qiu-Hua
QH
Wang
Yan-Qing
YQ
D019297:2,4-Dinitrophenol / Q000737:chemistry*; D000465:Algorithms; D000818:Animals; D002417:Cattle; D031541:Fluorescence Resonance Energy Transfer; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D008956:Models, Chemical; D010179:Pancreas / Q000737:chemistry; D010636:Phenols / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods; D055672:Static Electricity; D013696:Temperature; D013816:Thermodynamics; D014357:Trypsin / Q000737:chemistry*; D014443:Tyrosine / Q000737:chemistry
C549935:2,4-dichlorphenol; D010636:Phenols; D014443:Tyrosine; D014357:Trypsin; D019297:2,4-Dinitrophenol