PMID:1601132
| Citation |
Andrews, SC, Shipley, D, Keen, JN, Findlay, JB, Harrison, PM and Guest, JR (1992) The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductases. FEBS Lett. 302:247-52 |
|---|---|
| Abstract |
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 ferrisiderophore reductase activity. Database searches revealed that the C-terminal region of HMP (FsrB) is homologous to members of a family of flavoprotein oxidoreductases which includes ferredoxin NADP+ reductase (FNR). The combination of FNR-like and haemoglobin-like regions in HMP (FsrB) represents a novel pairing of functionally and structurally distinct domains. Structure-function properties of other FNR-like proteins, including LuxG and VanB, are also discussed. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Dihydropteridine Reductase/chemistry; Dihydropteridine Reductase/genetics; Dihydropteridine Reductase/metabolism; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli Proteins; Ferredoxin-NADP Reductase/chemistry; Genes, Bacterial; Hemeproteins; NADH, NADPH Oxidoreductases/chemistry; NADH, NADPH Oxidoreductases/isolation & purification; NADH, NADPH Oxidoreductases/metabolism; Pectobacterium chrysanthemi/genetics; Peptide Fragments/chemistry; Protein Conformation; Salmonella typhimurium/genetics; Sequence Homology, Nucleic Acid |
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