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

FEBS Letters

Harrison, Pauline M.²  Andrews, Simon C.²  Keen, Jeffrey N.¹  Findlay, John B.C.¹  Guest, John R.²  Shipley, Darren² 

[1] Department of Biochemistry and Molecular Biology, The University of Leeds, Leeds LS2 9JT, UK;The Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, Firth Court, Western Bank, The University of Sheffield, Sheffield S10 2UH, UK

关键词: Ferrisiderophore reductase;    Haemoglobin;    Ferredoxin NADP+ reductase;    Mosaic protein;    LuxG;    VanB;    HMP;    haemoglobin-like protein;    FSR;    ferrisiderophore reductase;    FNR;    ferredoxin NADP+ reductase;    Fre;    flavin reductase enzyme;   

DOI  :  10.1016/0014-5793(92)80452-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown