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Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua.

ABSTRACT: 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 corresponding to oxidation of thisputative complex, i.e. [Fe(2)-P](Z+2)+1/2 O(2)-->[Fe(2)O-P](Z)+2H(+);and a third phase of iron(II) oxidation/mineralization, i.e. 4Fe(2+)+O(2)+8H(2)O-->8FeOOH((s))+8H(+) [where FeOOH((s)) represents the hydrous ferric oxidemineral that precipitates from the solution], which occurs when iron isadded in excess of 24Fe(2+)/protein. In contrast with otherferritins, the ferroxidation reaction in L. innocua ferritinproceeds more slowly than the oxidation/mineralization reaction. Wateris the final product of dioxygen reduction in the 12-subunit L.innocua ferritin (the present work) and in the 24-subunit Escherichia coli bacterioferritin, whereas H(2)O(2) is produced in 24-subunit mammalian ferritins. Possible reasonsfor this difference are discussed.

SUBMITTER: Yang X

PROVIDER: S-EPMC1221205 | biostudies-other | 2000 Aug

REPOSITORIES: biostudies-other

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Project description:Electron magnetic resonance (EMR) spectroscopy was used to determine the magnetic properties of maghemite (γ-Fe(2)O(3)) nanoparticles formed within size-constraining Listeria innocua (LDps)-(DNA-binding protein from starved cells) protein cages that have an inner diameter of 5 nm. Variable-temperature X-band EMR spectra exhibited broad asymmetric resonances with a superimposed narrow peak at a gyromagnetic factor of g ≈ 2. The resonance structure, which depends on both superparamagnetic fluctuations and inhomogeneous broadening, changes dramatically as a function of temperature, and the overall linewidth becomes narrower with increasing temperature. Here, we compare two different models to simulate temperature-dependent lineshape trends. The temperature dependence for both models is derived from a Langevin behavior of the linewidth resulting from "anisotropy melting." The first uses either a truncated log-normal distribution of particle sizes or a bi-modal distribution and then a Landau-Liftshitz lineshape to describe the nanoparticle resonances. The essential feature of this model is that small particles have narrow linewidths and account for the g ≈ 2 feature with a constant resonance field, whereas larger particles have broad linewidths and undergo a shift in resonance field. The second model assumes uniform particles with a diameter around 4 nm and a random distribution of uniaxial anisotropy axes. This model uses a more precise calculation of the linewidth due to superparamagnetic fluctuations and a random distribution of anisotropies. Sharp features in the spectrum near g ≈ 2 are qualitatively predicted at high temperatures. Both models can account for many features of the observed spectra, although each has deficiencies. The first model leads to a nonphysical increase in magnetic moment as the temperature is increased if a log normal distribution of particles sizes is used. Introducing a bi-modal distribution of particle sizes resolves the unphysical increase in moment with temperature. The second model predicts low-temperature spectra that differ significantly from the observed spectra. The anisotropy energy density K(1), determined by fitting the temperature-dependent linewidths, was ∼50 kJ/m(3), which is considerably larger than that of bulk maghemite. The work presented here indicates that the magnetic properties of these size-constrained nanoparticles and more generally metal oxide nanoparticles with diameters d < 5 nm are complex and that currently existing models are not sufficient for determining their magnetic resonance signatures.

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Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua.

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