Trynda-Lemiesz L, Pruchnik F P
Faculty of Chemistry, University of Wrocåw, Poland.
J Inorg Biochem. 1997 May 15;66(3):187-92. doi: 10.1016/s0162-0134(96)00202-4.
Absorption, CD, fluorescence, and ICP(AES) methods were used to evaluate the interaction of Rh2(OAc)2(bpy)2(H2O)22 with human serum albumin (HSA). The rhodium complex reacts easily with HSA; the Rh atoms are coordinated to protein via the imidazole rings of His residues. When the protein was incubated for 24 h at 37 degrees C, the amount of rhodium was found to be approximately 7 mol per mol of HSA. Analysis of CD spectra showed the decreasing helix content to be about 15% in the metal-bound HSA. The relative fluorescence intensity of HSA bound with rhodium decreased to 20% of that of the native state, suggesting that perturbation around the Trp-214 residue took place. This was confirmed by the destruction of the warfarin binding site. The rhodium binding weakens the interaction of HSA with other molecules like heme or bilirubin.
采用吸收光谱、圆二色光谱（CD）、荧光光谱和电感耦合等离子体发射光谱（ICP(AES)）等方法评估了Rh2(OAc)2(bpy)2(H2O)22与人血清白蛋白（HSA）的相互作用。铑配合物能轻松与HSA发生反应；铑原子通过组氨酸残基的咪唑环与蛋白质配位。当蛋白质在37℃下孵育24小时后，发现每摩尔HSA中铑的含量约为7摩尔。对CD光谱的分析表明，与金属结合的HSA中螺旋含量下降了约15%。与铑结合的HSA的相对荧光强度降至天然状态的20%，这表明色氨酸-214残基周围发生了扰动。华法林结合位点的破坏证实了这一点。铑的结合削弱了HSA与其他分子（如血红素或胆红素）的相互作用。
