Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1410339 | Journal of Molecular Structure | 2009 | 7 Pages |
Abstract
The interaction between bovine hemoglobin (BHb) and phosphomolybdate acid (PMo12) was investigated by UV/vis absorption, IR, circular dichroism (CD), 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, ÎH° and ÎS° were estimated to be 28.69 K J molâ1, 158.20 J molâ1 Kâ1 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.
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Authors
Hong-Mei Zhang, Yan-Qing Wang, Qiu-Hua Zhou, Guang-Li Wang,