Kinetic and structural characterization of an intermediate in the biomineralization of bacterioferritin

FEBS Letters

Harrison, Pauline M.¹  Wilson, Michael T.³  Andrews, Simon C.¹  Le Brun, Nick E.²  Thomson, Andrew J.²  Moore, Geoffrey R.²  Guest, John R.¹ 

[1] The Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, UK;Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences, University of East Anglia, Norwich, NR4 7TJ, UK;Department of Chemistry and Biological Chemistry, University of Essex, Colchester, C04 3SQ, UK

关键词: Bacterioferritin;    Iron-uptake;    Kinetic phase;    Iron(II) dimer;   

DOI  :  10.1016/0014-5793(93)80404-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown