title: Studies on the interaction between chromium(VI) and human serum albumin: spectroscopic approach.
abstract: The interaction between Cr(2)O(7)(2-) and human serum albumin (HSA) was investigated using fluorescence, UV/vis, FT-IR, CD spectroscopy, and molecular modeling method. The experimental results showed that the fluorescence quenching of HSA by Cr(2)O(7)(2-) is a result of the formation of HSA-chromium(VI) complex; static quenching was confirmed to result in the fluorescence quenching. The corresponding thermodynamic parameters showed that the process of binding Cr(2)O(7)(2-) on HSA was a spontaneous molecular interaction procedure. Ionic, H-bonds and van der Waals interactions play a major role in stabilizing the complex. The Cr(2)O(7)(2-) altered the environments of Trp and Tyr residues in HSA.
authors: Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Yancheng City, Jiangsu Province 224002, People's Republic of China. genchengzhang@126.com
authors: Gen-Cheng
authors: GC
authors: Zhang
authors: Jie-Yan
authors: JY
authors: Xu
authors: Yan-Qing
authors: YQ
authors: Wang
mesh_terms: D000042:Absorption; D001665:Binding Sites; D002857:Chromium / Q000378:metabolism*; D002942:Circular Dichroism; D006801:Humans; D007700:Kinetics; D017433:Protein Structure, Secondary; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013057:Spectrum Analysis / Q000379:methods*; D013696:Temperature
chemical_list: D012709:Serum Albumin; D002857:Chromium; C074702:chromium hexavalent ion