Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans

Two soluble enzymes (FerA and FerB) catalyzing the reduction of a number of iron(III) complexes by NADH, were purified to near homogeneity from the aerobically grown iron‐limited culture of Paracoccus denitrificans using a combination of anion‐exchange chromatography (Sepharose Q), chromatofocusing...

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Veröffentlicht in:	European journal of biochemistry 2004-02, Vol.271 (3), p.553-562
Hauptverfasser:	Mazoch, Jiří, Tesařík, Radek, Sedláček, Vojtěch, Kučera, Igor, Turánek, Jaroslav
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Anion Exchange Resins Catalysis Chromatography, Ion Exchange Electrophoresis, Polyacrylamide Gel FMN Reductase - chemistry FMN Reductase - isolation & purification FMN Reductase - metabolism iron(III) reductase Isoenzymes - chemistry Isoenzymes - isolation & purification Isoenzymes - metabolism Kinetics Mass Spectrometry Molecular Sequence Data Molecular Weight NADH:flavin oxidoreductase Paracoccus denitrificans Paracoccus denitrificans - enzymology Sequence Homology, Amino Acid Solubility
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