THE HEMOGLOBIN-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 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.