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.
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[Spectral properties of the hemoporphyrin derivative interacting with hemoglobin].
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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.
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