[Spectral properties of the hemoporphyrin derivative interacting with hemoglobin].
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 Föster energy transfer mechanism, and the thermodynamic parameters were obtained.
Feng
Shang-Yuan
SY
College of Chemistry and Material Science, Experimental Center, Fujian Normal University, Fuzhou 350007, China. syfeng@fjnu.edu.cn
Chen
Rong
R
Yang
Wen-Qin
WQ
Li
Yong-Zeng
YZ
Huang
Zu-Fang
ZF
Liao
Xiao-Hua
XH
D017324:Hematoporphyrin Derivative / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D007700:Kinetics; D011485:Protein Binding; D013816:Thermodynamics
D006454:Hemoglobins; D017324:Hematoporphyrin Derivative