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The Periodic Table and Organismal Elements

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Setup of Capillary Electrophoresis-Inductively Coupled Plasma Mass Spectrometry (CE-ICP-MS) for Quantification of Iron Redox Species (Fe(II), Fe(III))
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The interaction between desferrioxamine and hemin: a potential toxicological implication.

Naihao Lu1, Lian Yi, Qinqin Deng

  • 1Key Laboratory of Functional Small Organic Molecule, Ministry of Education and College of Life Science, Jiangxi Normal University, Nanchang 330022, PR China.

Toxicology in Vitro : an International Journal Published in Association with BIBRA
|March 27, 2012
PubMed
Summary

The iron chelating agent desferrioxamine (DFO) binds strongly with hemin, promoting cytotoxic radical formation. This interaction, driven by thermodynamics, may explain DFO

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Measurement of Heme Synthesis Levels in Mammalian Cells
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Measurement of Heme Synthesis Levels in Mammalian Cells

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Last Updated: May 23, 2026

Setup of Capillary Electrophoresis-Inductively Coupled Plasma Mass Spectrometry (CE-ICP-MS) for Quantification of Iron Redox Species (Fe(II), Fe(III))
04:48

Setup of Capillary Electrophoresis-Inductively Coupled Plasma Mass Spectrometry (CE-ICP-MS) for Quantification of Iron Redox Species (Fe(II), Fe(III))

Published on: May 4, 2020

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Area of Science:

  • Biochemistry
  • Analytical Chemistry

Background:

  • Desferrioxamine (DFO), an iron chelator, previously showed potential to enhance hemin-induced protein oxidation.
  • The binding affinity and thermodynamic parameters of the DFO-hemin interaction were previously uncharacterized.

Purpose of the Study:

  • To investigate the interaction between desferrioxamine (DFO) and hemin using affinity capillary electrophoresis (ACE).
  • To determine the binding constants and thermodynamic parameters governing the DFO-hemin interaction.

Main Methods:

  • Affinity capillary electrophoresis (ACE) was employed to study DFO-hemin binding.
  • Binding constants were calculated at various temperatures.

Main Results:

  • DFO-hemin binding constants were determined to be in the range of 10(4)-10(5) M(-1).
  • Thermodynamic parameters (ΔG, ΔS, ΔH) were negative, indicating spontaneous, exothermic, and entropically driven binding.
  • High binding affinity correlates with enhanced formation of cytotoxic radicals like superoxide (O(2)(-)).

Conclusions:

  • The study provides the first characterization of DFO-hemin binding constants and thermodynamics.
  • The strong binding affinity is a key factor in DFO's promotion of hemin-catalyzed cytotoxic radical formation.
  • Findings offer insights into the potential clinical toxicity of DFO related to its interaction with hemin.