The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin

Yang, Xiaoke, Le Brun, Nick E., Thomson, Andrew J., Moore, Geoffrey R. and Chasteen, N. Dennis (2000) The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin. Biochemistry, 39 (16). pp. 4915-4923. ISSN 0006-2960

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Abstract

Bacterioferritins are members of a class of spherical shell-like iron storage proteins that catalyze the oxidation and hydrolysis of iron at specific sites inside the protein shell, resulting in formation of a mineral core of hydrated ferric oxide within the protein cavity. Electrode oximetry/pH stat was used to study iron oxidation and hydrolysis chemistry in E. coli bacterioferritin. Consistent with previous UV-visible absorbance measurements, three distinct kinetic phases were detected, and the stoichiometric equations corresponding to each have been determined. The rapid phase 1 reaction corresponds to pairwise binding of 2 Fe2+ ions at a dinuclear site, called the ferroxidase site, located within each of the 24 subunits, viz., 2Fe2+ + P(z) → [Fe2-P](z) + 4H+, where P(z) is the apoprotein of net charge Z and [Fe2-P](z) represents a diferrous ferroxidase complex. The slower phase 2 reaction corresponds to the oxidation of this complex by molecular oxygen according to the net equation: [Fe2-P](z) + 1/2 O2 → [Fe2O-P](z) where [Fe2O-P](z) represents an oxidized diferric ferroxidase complex, probably a μ-oxo-bridged species as suggested by UV- visible and EPR spectrometric titration data. The third phase corresponds to mineral core formation according to the net reaction: 4Fe2+ + O2 + 6H2O → 4FeO(OH)((core)) + 8H+. Iron oxidation is inhibited by the presence of Zn2+ ions. The patterns of phase 2 and phase 3 inhibition are different, though inhibition of both phases is complete at 48 Zn2+per 24mer, i.e., 2 Zn2+ per ferroxidase center.

Item Type: Article
Uncontrolled Keywords: biochemistry ,/dk/atira/pure/subjectarea/asjc/1300/1303
Faculty \ School: Faculty of Science > School of Chemistry (former - to 2024)
Faculty of Science > School of Chemical Sciences and Pharmacy (former - to 2009)
UEA Research Groups: Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Faculty of Science > Research Groups > Chemistry of Life Processes
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Depositing User: LivePure Connector
Date Deposited: 18 Jun 2025 09:30
Last Modified: 18 Jun 2025 11:30
URI: https://ueaeprints.uea.ac.uk/id/eprint/99605
DOI: 10.1021/bi992631f

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