Molecular interaction between phosphomolybdate acid and bovine hemoglobin

被引：39

作者：

Zhang, Hong-Mei ^{[1
]}

Wang, Yan-Qing ^{[1
]}

Zhou, Qiu-Hua ^{[1
]}

Wang, Guang-Li ^{[1
]}

机构：

[1] Yancheng Teachers Univ, Inst Appl Chem & Environm Engn, Dept Chem, Jiangsu Prov Key Lab Coastal Wetland Bioresources, Yancheng City 224002, Jiangsu Prov, Peoples R China

来源：

JOURNAL OF MOLECULAR STRUCTURE | 2009年 / 921卷 / 1-3期

关键词：

Phosphomolybdate acid; Bovine hemoglobin; Fluorescence spectroscopy; Interaction; HUMAN SERUM-ALBUMIN; FLUORESCENCE EMISSION; CIRCULAR-DICHROISM; ENERGY-TRANSFER; BINDING; SPECTRA; PROTEINS; NANOPARTICLES; FLAVONOIDS; PARAQUAT;

D O I：

10.1016/j.molstruc.2008.12.049

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

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. (c) 2008 Elsevier B.V. All rights reserved.

引用

页码：156 / 162

页数：7

共 51 条

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