Anomalous nuclear magnetic relaxation of aqueous solutions of ferritin: an unprecedented first-order mechanism.

Ferritin, the iron-storing protein, speeds up proton transverse magnetic relaxation in aqueous solutions. This T(2) shortening is used in MRI to quantify iron in the brain and liver. Current theoretical models underestimate the relaxation enhancement by ferritin at imaging fields, and they do not predict the measured dependence of the rate enhancement on the magnetization of the particles. Here it is shown that a proton exchange dephasing model (PEDM) overcomes these limitations by allowing a first-order relaxation mechanism. The PEDM considers proton exchange between bulk water and exchangeable protons located at the surface of the hydrated iron oxide nanometric core of the protein. Relaxation is shown to depend on the distribution of the frequency shifts of the adsorption sites; the observed properties agree with a Lorentzian distribution. Computer simulations utilizing recent Mössbauer spectroscopy data show that the distribution of these shifts is effectively Lorentzian.

Susceptibility-induced T(2)-shortening and unrestricted diffusion.

In this work, discrepancies between recent theories for susceptibility-induced T(2)-shortening and classical results, namely outer sphere theory and diffusion through local fields with random gradients, are considered. These discrepancies are assigned to the use of unrestricted diffusion in the new theories.