Spectral studies on the interaction between Cu2+ and urease.
The interactions of Cu(2+) with urease were investigated by fluorescence, UV/vis, CD, synchronous fluorescence, and three-dimensional fluorescence spectra techniques. Cu(2+) effectively quenched the intrinsic fluorescence of urease via static quenching. The binding constant K(A), the binding site n and the thermodynamic parameters are obtained. The process of binding Cu(2+) to urease was a spontaneous molecular interaction procedure with electrostatic interaction. The conformation of urease was discussed by UV/vis, CD, synchronous and three-dimensional fluorescence techniques.
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. wyqing76@126.com
Wang
W
Yan-Qing
Zhang
Z
Hong-Mei
D000042:Absorption; D002942:Circular Dichroism; D003300:Copper / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008968:Molecular Conformation; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature; D014510:Urease / Q000378:metabolism*
D003300:Copper; D014510:Urease