FhuF, Part of a Siderophore-Reductase System

Berthold F. Matzanke*, Stefan Anemüller, Volker Schünemann, Alfred X. Trautwein, Klaus Hantke

*Corresponding author for this work
68 Citations (Scopus)


FhuF is a cytoplasmic 2Fe-2S protein of Escherichia coli loosely associated with the cytoplasmic membrane. E. coli fhuF mutants showed reduced growth on plates with ferrioxamine B as the sole iron source, although siderophore uptake was not defective in transport experiments. Removal of iron from coprogen, ferrichrome, and ferrioxamine B was significantly lower in fhuF mutants compared to the corresponding parental strains, which suggested that FhuF is involved in iron removal from these hydroxamate-type siderophores. A redox potential E1/2 of -310 ± 25 mV relative to the normal hydrogen electrode was determined for FhuF by EPR redox titration; this redox potential is sufficient to reduce the siderophores coprogen and ferrichrome. Mössbauer spectra revealed that FhuF in its [Fe2+-Fe 3+] state is also capable of direct reduction of ferrioxamine B-bound ferric iron, thus proving its reductase function. This is the first report on a bacterial siderophore-iron reductase which in vivo seems to be specific for a certain group of hydroxamates.

Original languageEnglish
Issue number5
Pages (from-to)1386-1392
Number of pages7
Publication statusPublished - 10.02.2004


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