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Updated: Jun 22, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
[Spectral properties of the hemoporphyrin derivative interacting with hemoglobin]
Shang-Yuan Feng1, Rong Chen, Wen-Qin Yang
1College of Chemistry and Material Science, Experimental Center, Fujian Normal University, Fuzhou 350007, China. syfeng@fjnu.edu.cn
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.
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