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    FEBS Lett. 1994 Aug 22;350(2-3):258-62.

    Direct observation of the iron binding sites in a ferritin.

    Source

    Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, UK.

    Abstract

    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.

    PMID:
    8070575
    [PubMed - indexed for MEDLINE]

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