An analysis of the g values in semi-met forms of hemerythrin and in related proteins.
The two semi-met (FeIII, FeII) forms of hemerythrin prepared by either oxidation of the deoxy form or reduction of the met form, exhibit rather different EPR spectra. It is shown that a very weak difference in the rhombic distortion of the ferrous site is sufficient to account for this large shift of the g values. It is proposed that the important departure from g = 2.00 and the large anisotropy of the g tensor reflect directly the octahedral coordination of the ferrous ion. Such a coordination could then be present in other proteins which contain binuclear clusters characterized by similar EPR spectra.
D004578:Electron Spin Resonance Spectroscopy; D006422:Hemerythrin; D008024:Ligands; D008433:Mathematics; D008667:Metalloproteins; D008956:Models, Chemical; D010084:Oxidation-Reduction
D006422:Hemerythrin; D008024:Ligands; D008667:Metalloproteins; C019004:methemerythrin