Interpretation of the Mössbauer Spectra of the High‐Potential Iron Protein from Chromatium

TLDR: The Mossbauer spectra of both reduced and oxidized high-potential iron protein (Hipip) from Chromatium have been analysed using computer fits to theoretical spectra derived from a spin Hamiltonian and a model of the four-iron four-sulphide active centre is interpreted which is consistent with its electronic and magnetic properties in both redox states.

Abstract: The Mossbauer spectra of both reduced and oxidized high-potential iron protein (Hipip) from Chromatium have been analysed using computer fits to theoretical spectra derived from a spin Hamiltonian. Fits to spectra obtained over a range of temperatures between 4.2 and 195 K and in applied magnetic fields up to 10.0 T lead to a consistent set of hyperfine parameters. These results are interpreted in terms of a model of the four-iron four-sulphide active centre which is consistent with its electronic and magnetic properties in both redox states. In the model for the reduced centre all four iron atoms have essentially the same valence, intermediate between ferric and ferrous, with the spins being coupled antiferromagnetically to give the centre zero net spin. The oxidized centre has one less electron which at low temperatures appears to have come predominantly from one pair of iron atoms which thus become ferric with the other pair remaining substantially unchanged. It is clear from the Mossbauer hyperfine parameters obtained from the computer fits to the low-temperature spectra that a larger magnetic moment is associated with the ferric/ferrous pair of iron atoms than with the ferric pair of iron atoms. This also explains the g values with an average of greater than 2 which are observed in electron paramagnetic resonance (EPR) measurements. At higher temperatures the differences between the electron charge density at the different iron atoms in the oxidized centre appear to become smeared out.