Direct observation of the iron binding sites in a ferritin

FEBS Letters

Harrison, Pauline M.¹  Artymiuk, Peter J.¹  Banfield, Mark J.¹  Hudson, Aaron J.¹  Andrews, Simon C.¹  Guest, John R.¹  Hempstead, Paul D.¹ 

[1] The Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2UH, UK

关键词: Ferritin;    Iron-binding site;    Binuclear Fe complex;    Iron mineralisation;   

DOI  :  10.1016/0014-5793(94)00781-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

X-Ray analysis of the ferritin of Escherichia coli (Ec-FTN) and of Ec-FTN crystals soaked in (NH₄)₂Fe(SO₄)₂ has revealed the presence of three iron-binding sites per subunit. Two of these form a di-iron site in the centre of the subunit as has been proposed for the ‘ferroxidase centres’ of human ferritin H chains. This di-iron site, lying within the 4-alpha-helix bundle, resemble those of ribonucleotide reductase, methane monoxygenase and haemerythrin. The third iron is bound by ligands unique to Ec-FTN on the inner surface of the protein shell. It is speculated that this state may represent the nucleation centre of a novel type of Fe(III) cluster, recently observed in Ec-FTN.

【 授权许可】

Unknown