Molecular interaction between phosphomolybdate acid and bovine hemoglobin

作者：Zhang, Hong-Mei; Wang, Yan-Qing^*; Zhou, Qiu-Hua; Wang, Guang-Li

来源：Journal of Molecular Structure, 2009, 921(1-3): 156-162.

DOI：10.1016/j.molstruc.2008.12.049

• Phosphomolybdate acid
• Bovine hemoglobin
• Fluorescence spectroscopy
• Interaction

The interaction between bovine hemoglobin (BHb) and phosphomolybdate acid (PMo12) Was investigated by UV/vis absorption, IR, circular dichroism (CID), fluorescence, resonance light scattering spectra, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. PMo12 effectively quenched the intrinsic fluorescence of BHb via static quenching. The process of binding PMo12 on BHb was a spontaneous molecular interaction procedure. The thermodynamic parameters, Delta H degrees and Delta S degrees were estimated to be 28.69 K J mol(-1), 158.20J mol(-1) K-1 according to the van' Hoff equation. This indicates that hydrophobic interaction played a major role in stabilizing the PMo12-BHb complex. The effect of PMo12 on the conformation of BHb was analyzed using synchronous fluorescence spectroscopy, IR and CD spectra.

• 出版日期2009-3-17
• 单位中国科学院长春应用化学研究所; 盐城师范学院