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Kinetic and structural characterization of an intermediate in the biomineralization of bacterioferritin
Author(s) -
Le Brun Nick E.,
Wilson Michael T.,
Andrews Simon C.,
Guest John R.,
Harrison Pauline M.,
Thomson Andrew J.,
Moore Geoffrey R.
Publication year - 1993
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(93)80404-i
Subject(s) - chemistry , electron paramagnetic resonance , dimer , crystallography , biomineralization , phase (matter) , ceruloplasmin , biochemistry , chemical engineering , nuclear magnetic resonance , organic chemistry , physics , engineering
The mechanism by which iron‐storage proteins take up and oxidise iron(II) is not understood. We show by rapid‐kinetic and EPR measurements that iron uptake, in vitro, by a bacterial iron‐storage protein, bacterioferritin, involves at least three kinetically distinguishable phases: phase 1, the binding of Fe(II) ions, probably at a dimeric iron ferroxidase centre; phase 2, oxidation of the Fe(II) dimer and production of mononuclear Fe(III); and phase 3, iron core formation.