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The haemoglobin‐like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C‐terminal domain shares homology with ferredoxin NADP + reductases
Author(s) -
Andrews Simon C.,
Shipley Darren,
Keen Jeffrey N.,
Findlay John B.C.,
Harrison Pauline M.,
Guest John R.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80452-m
Subject(s) - ferredoxin—nadp(+) reductase , ferredoxin , escherichia coli , reductase , flavoprotein , homology (biology) , biochemistry , biology , enzyme , amino acid , gene
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.