Measurements of the Faraday rotation at room temperature over the light wavelength range of 300-680 nm for horse spleen ferritin (HSF), magnetoferritin with different loading factors (LFs) and nanoscale magnetite and Fe(2)O(3) suspensions are reported. The Faraday rotation and the magnetization of the materials studied present similar magnetic field dependences and are characteristic of a superparamagnetic system. The dependence of the Faraday rotation on the magnetic field is described, excluding HSF and Fe(2)O(3), by a Langevin function with a log-normal distribution of the particle size allowing the core diameters of the substances studied to be calculated. It was found that the specific Verdet constant depends linearly on the LF. Differences in the Faraday rotation spectra and their magnetic field dependences allow discrimination between magnetoferritin with maghemite and magnetite cores which can be very useful in biomedicine.

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The paper presents detailed experimental study of synthesis and characterization a bioinorganic magnetic molecule magnetoferritin. Magnetoferritin with loading of iron ions per protein molecule in the range from 300 to 3000 was prepared. Size distribution analysis (transmission electron microscopy, dynamic light scattering) shows spherical nanoparticles with particle size distribution from 2 to 12 nm, and hydrodynamic diameter from 12 to 25 nm. The thermomagnetic curves measured after cooling the sample in zero eld (zero-eld cooling) and under the presence of the measurement eld (eld cooling) show superparamagnetic behavior with the blocking temperature T b from 22 to 60 K and the magnetization loops measured below T b (at 2 K) show the hysteresis with coercive eld from 20 to 30 kA/m depending on the concentration of the magnetic nanoparticles.

Synthetic biological macromolecule of magnetoferritin containing an iron oxide core inside a protein shell (apoferritin) is prepared with different content of iron. Its structure in aqueous solution is analyzed by small-angle synchrotron X-ray (SAXS) and neutron (SANS) scattering.The loading factor (LF) defined as the average number of iron atoms per protein is varied up to LF=800. With an increase of the LF, the scattering curves exhibit a relative increase in the total scattered intensity, a partial smearing and a shift of the match point in the SANS contrast variation data. The analysis shows an increase in the polydispersity of the proteins and a corresponding effective increase in the relative content of magnetic material against the protein moiety of the shell with the LF growth. At LFs above ~150, the apoferritin shell undergoes structural changes, which is strongly indicative of the fact that the shell stability is affected by iron oxide presence.