Binding of Al(III)-tetracarboxyphthalocyanine to Hemoglobin and Myoglobin |
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| Authors: | Qiu-Hua Zhou Hong-Mei Zhang Lin Wu Yan-Qing Wang |
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| Affiliation: | (1) Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Yancheng, China;(2) Chemistry Department, Institute of Applied Chemistry and Environmental Engineering, Yancheng Teachers University, Yancheng City, Jiangsu Province, 224002, People’s Republic of China; |
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| Abstract: | The interactions between Al(III)-tetracarboxyphthalocyanine (AlPc(COOH)4) and hemoglobin (or myoglobin) have been studied. The results showed that AlPc(COOH)4 effectively quenched the intrinsic fluorescence of Hb and Mb via static quenching. The hydrophobic and electrostatic interactions played a major role in stabilizing the AlPc(COOH)4-protein complex. The distance r between donor and acceptor was obtained to be 3.92 and 3.67 nm for AlPc(COOH)4-Hb and AlPc(COOH)4-Mb system, respectively. The effect of AlPc(COOH)4 on the conformation of Hb and Mb was analyzed using UV–vis absorption spectroscopy, circular dichroism spectra, synchronous fluorescence and three-dimensional fluorescence spectra. |
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