| 光谱学与光谱分析 |
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| Spectral Properties of the Hemoporphyrin Derivative Interacting with Hemoglobin |
| FENG Shang-yuan1,2,CHEN Rong2*,YANG Wen-qin1,LI Yong-zeng2,HUANG Zu-fang2,LIAO Xiao-hua2 |
1. College of Chemistry and Material Science，Experimental Center, Fujian Normal University，Fuzhou 350007，China
2. Key Laboratory of Optoelectronic Science and Technology for Medicine, Ministry of Education，Fujian Normal University，Fuzhou 350007，China |
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Abstract The quenching reaction of hemoporphyrin derivative with hemoglobin (Hb) was studied by using fluorescence spectra and absorption spectra.It was shown that HpD has a powerful ability to quench the Hb fluorescence via a nonradiative energy transfer mechanism. The formation constants of them were analyzed at different temperature according to Stern-Volmer equation and double-reciprocal equation，which are bigger at high temperature than at low temperature. The critical binding site was calculated (R0＝3.22 nm) by Fster energy transfer mechanism, and the thermodynamic parameters were obtained.
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Received: 2006-08-16
Accepted: 2006-11-18
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Corresponding Authors:
CHEN Rong
E-mail: syfeng@fjnu.edu.cn
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| Cite this article: |
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FENG Shang-yuan,CHEN Rong,YANG Wen-qin, et al. Spectral Properties of the Hemoporphyrin Derivative Interacting with Hemoglobin [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2007, 27(11): 2279-2282.
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| URL: |
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https://www.gpxygpfx.com/EN/Y2007/V27/I11/2279 |
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