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