PMID:14756576
| Citation |
Matzanke, BF, Anemüller, S, Schünemann, V, Trautwein, AX and Hantke, K (2004) FhuF, part of a siderophore-reductase system. Biochemistry 43:1386-92 |
|---|---|
| Abstract |
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 E(1/2) 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 [Fe(2+)-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. |
| Links |
PubMed Online version:10.1021/bi0357661 |
| Keywords |
Bacterial Outer Membrane Proteins; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Biological Transport/genetics; Deferoxamine/chemistry; Electron Spin Resonance Spectroscopy; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Ferric Compounds/chemistry; Iron/chemistry; Iron-Binding Proteins; Iron-Sulfur Proteins/chemistry; Nitrate Reductase (NADH); Nitrate Reductases/chemistry; Oxidation-Reduction; Periplasmic Binding Proteins; Siderophores/chemistry; Spectroscopy, Mossbauer |
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