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Iron Transport: Siderophores

  1. Berthold F. Matzanke

Published Online: 15 DEC 2011

DOI: 10.1002/9781119951438.eibc0110

Encyclopedia of Inorganic and Bioinorganic Chemistry

Encyclopedia of Inorganic and Bioinorganic Chemistry

How to Cite

Matzanke, B. F. 2011. Iron Transport: Siderophores. Encyclopedia of Inorganic and Bioinorganic Chemistry. .

Author Information

  1. University of Lübeck, Lübeck, Germany

Publication History

  1. Published Online: 15 DEC 2011


Siderophores (from the Greek: iron carrier) are low molecular mass (500–1500 Da) iron chelators that are synthesized in bacteria and fungi under conditions of iron deficiency. Siderophores exhibit extraordinarily high complex formation constants for ferric iron with β-values ranging from 1020 to approximately 1050. Fe2+-siderophores are some 20 orders of magnitude less stable than their Fe3+ counterparts. The d5 electronic configuration of Fe3+ rules out any crystal field stabilization energy and makes ferric iron complexes relatively labile with respect to isomerization and ligand exchange. Siderophores display a selectivity for iron that is reflected in the corresponding complex stability constants that are higher with Fe3+ than with Al3+, or with bivalent cations like Ca2+, Cu2+ or Zn2+. Microorganisms excrete desferrisiderophores in order to scavenge iron from the environment. The competition for iron by siderophores, the mechanisms of siderophore uptake through microbial membranes, and the intracellular pathways of siderophore-iron utilization strongly depend on thermodynamic, kinetic, and structural features of the ferric iron siderophore complexes.

The structural features of siderophores are diverse. The ligating groups contain oxygen atoms of hydroxamate, catecholate, α-hydroxy carboxylic and salicylic acids, or oxazoline and thiazoline nitrogen. Reduction potentials of ferric siderophore complexes vary between −700 and −150 mV. In particular at the low potential end below −450 mV, special biological strategies of reductive iron removal are required because these potentials are too negative for typical cellular reductases.

The coordination and redox chemistry of siderophores is also reflected in the mechanisms of siderophore-mediated iron uptake in microorganisms. A classic example is the intracellular removal of iron from enterobactin. The permeation of cell walls or bacterial membranes by siderophores is in most microbes a highly specific process requiring an array of up to eight proteins. The advent of modern molecular biology delivered a cornucopia of methods enabling high-yield production of specific gene products relevant to siderophore synthesis and transport, analyses of structure-function relationships (employing site directed mutagenesis), and detailed insights into the regulation of the corresponding processes.

One siderophore, ferrioxamine B, serves as a detoxifier in iron overload diseases and in the treatment of β-thalassemia. Siderophores and siderophore analogs also play a role in MRI and are employed as basic models for actinide chelators in order to remove these metals from the environment or from a contaminated body.


  • siderophore;
  • chromic siderophores;
  • complex formation constants;
  • redox potentials;
  • microbial iron transport;
  • siderophore receptors;
  • infection;
  • medical therapy;
  • actinides