Study of the interaction between bovine hemoglobin and analogs of biphenyldicarboxylate by spectrofluorimetry

被引：24

作者：

Wang, Ruiyong ^{[1
]}

Yin, Yujing ^{[1
]}

Wang, Ruiqiang ^{[2
]}

Xie, Yuanzhe ^{[1
]}

Ge, Baoyu ^{[1
]}

Li, Zhigang ^{[1
]}

Li, Zhen ^{[1
]}

Shi, Jie ^{[1
]}

Chang, Junbiao ^{[1
]}

机构：

[1] Zhengzhou Univ, Dept Chem, Zhengzhou 450001, Peoples R China

[2] Zhengzhou Univ, Afficiated Hosp 1, Zhengzhou 450052, Peoples R China

来源：

JOURNAL OF LUMINESCENCE | 2013年 / 144卷

基金：

中国国家自然科学基金;

关键词：

Interaction; Hemoglobin; Analogs; Biphenyldicarboxylate; SERUM-ALBUMIN; FLUORESCENCE; BINDING; BENZIDINE; EMISSION; MEDICINE; OXYGEN;

D O I：

10.1016/j.jlumin.2013.06.053

中图分类号：

O43 [光学];

学科分类号：

070207 ; 0803 ;

摘要：

The interaction between bovine hemoglobin and analogs of Biphenyldicarboxylate was investigated by fluorescence, synchronous fluorescence, ultraviolet-vis absorbance, resonance light-scattering spectra and three-dimensional fluorescence spectra at pH 7.40. The quenching mechanism and binding constants were determined by the quenching of bovine hemoglobin fluorescence in presence of analogs. Results showed that the nature of the quenching was of static type. Both the van der Waals and hydrogen bonding played a major role in stabilizing the complex. The distance between donor and acceptors was obtained to be 2.11-2.25 nm according to Forster's theory. The influence of analogs on the conformation of bovine hemoglobin was investigated. (C) 2013 Elsevier B.V. All rights reserved.

引用

页码：79 / 86

页数：8

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