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Citation: ZHANG Gen-Cheng, XU Jie-Yan. Interaction Between Chromium(Ⅵ) and Bovine Serum Albumin[J]. Chinese Journal of Applied Chemistry, ;2010, 27(2): 191-196. doi: 10.3724/SP.J.1095.2010.90268 shu

Interaction Between Chromium(Ⅵ) and Bovine Serum Albumin

Institute of Applied Chemistry and Environmental Engineering, Yancheng Teachers University, Yancheng 224002

Received Date: 9 April 2009
Revised Date: 20 July 2009

The interaction between chromium(Ⅵ) and bovine serum albumin(BSA) was investigated via fluorescence,UV/Vis and CD spectroscopies. It is shown that Cr(Ⅵ) decreased the intensity of UV absorption peak of BSA,accompanied by red-shift. The fluorescence experimental results show that the fluorescence quenching of BSA by chromium(Ⅵ) is a result of the formation of Cr(Ⅵ)-BSA complex; static quenching was confirmed to result in the fluorescence quenching. The thermodynamic parameters were calculated(△G^θ<0,△H^θ=-12.60 kJ/mol,△S^θ=56.60 J/(mol·k)),the process of binding Cr(Ⅵ) molecule on BSA was a spontaneous molecular interaction procedure,during which the entropy increased and the Gibbs free energy decreased. The electrostatic force interaction plays a major role in stabilizing the complex. The distance between the tryptophane residue of BSA and Cr₂O₇^2- anion(2.85 nm) was determined by the mechanism of the energy transfer of dipole-dipole interaction. The results of synchronous fluorescence spectroscopy and CD spectroscopy indicate that Cr(Ⅵ) had a strong impact on BSA conformation,resulting in the change of the tryptophane residues environments and the decrease of the α-helical content of the protein.
- chromium(Ⅵ),
- bovine serum albumin,
- fluorescence spectroscopy,
- CD spectroscopy
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