Incorporation of iron by the unusual dodecameric ferritin from Listeria innocua

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Incorporation of iron by the unusual dodecameric ferritin from Listeria innocua.

The polypeptide chain that assembles into the unusual dodecameric shell of Listeria innocua apoferritin lacks the ferroxidase centre characteristic of H-type mammalian chains, but is able to catalyse both Fe(II) oxidation and nucleation of the iron core. A cluster of five carboxylate residues, which correspond in part to the site of iron core nucleation typical of L-type mammalian ferritins, ha...

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Iron deposition in the unusual 12-subunit ferritin from thebacterium Listeria innocua proceeds in three phases: a rapidfirst phase in which Fe(2+) binds to the apoprotein, P(Z) of charge Z, according to the postulatedreaction 2Fe(2+)+P(Z)-->[Fe(2)-P](Z+2)+2H(+), where[Fe(2)-P](Z+2) represents adinuclear iron(II) complex formed at each of the 12 ferroxidase centresof the protein; a second phase ...

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1,2-β-Oligoglucan Phosphorylase from Listeria innocua

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1999

ISSN: 0264-6021

DOI: 10.1042/0264-6021:3380071