The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP + reductases

Three soluble ferrisiderophore reductases (FsrA, FsrB and FsrC) were detected in Escherichia coli. FsrB was purified and identified as the haemoglobin-like protein (HMP) by size and N-terminal sequence analyses. HMP was previously isolated as a dihydropteridine reductase and is now shown to have fer...

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Veröffentlicht in:	FEBS letters 1992-05, Vol.302 (3), p.247-252
Hauptverfasser:	Andrews, Simon C., Shipley, Darren, Keen, Jeffrey N., Findlay, John B.C., Harrison, Pauline M., Guest, John R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biological and medical sciences Dihydropteridine Reductase - chemistry Dihydropteridine Reductase - genetics Dihydropteridine Reductase - metabolism Enzymes and enzyme inhibitors Escherichia coli - chemistry Escherichia coli - enzymology Escherichia coli Proteins Ferredoxin NADP + reductase Ferredoxin-NADP Reductase - chemistry Ferrisiderophore reductase flavin reductase enzyme FNR Fre FSR Fundamental and applied biological sciences. Psychology Genes, Bacterial Haemoglobin haemoglobin-like protein Hemeproteins HMP LuxG Mosaic protein NADH, NADPH Oxidoreductases - chemistry NADH, NADPH Oxidoreductases - isolation & purification NADH, NADPH Oxidoreductases - metabolism Oxidoreductases Pectobacterium chrysanthemi - genetics Peptide Fragments - chemistry Protein Conformation Salmonella typhimurium - genetics Sequence Homology, Nucleic Acid VanB
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