Protoporphyrin IX iron(II) revisited. An overview of the Mössbauer spectroscopic parameters of low-spin porphyrin iron(II) complexes.

Abstract

Mössbauer parameters of low-spin six-coordinate [Fe(II)(Por)L₂] complexes (where Por is a synthetic porphyrin; L is a nitrogenous aliphatic, an aromatic base or a heterocyclic ligand, a P-bonding ligand, CO or CN) and low-spin [Fe(Por)LX] complexes (where L and X are different ligands) are reported. A known point charge calculation approach was extended to investigate how the axial ligands and the four porphyrinato-N atoms generate the observed quadrupole splittings (ΔE_Q) for the complexes. Partial quadrupole splitting (p.q.s.) and partial chemical shifts (p.c.s.) values were derived for all the axial ligands, and porphyrins reported in the literature. The values for each porphyrin are different emphasising the importance/uniqueness of the [Fe(PPIX)] moiety, (which is ubiquitous in nature). This new analysis enabled the construction of figures relating p.c.s and p.q.s values. The relationships presented in the figures indicates that strong field ligands such as CO can, and do change the sign of the electric field gradient in the [Fe(II)(Por)L₂] complexes. The limiting p.q.s. value a ligand can have and still form a six-coordinate low-spin [Fe(II)(Por)L₂] complex is established. It is shown that the control the porphyrin ligands exert on the low-spin Fe(II) atom limits its bonding to a defined range of axial ligands; outside this range the spin state of the iron is unstable and five-coordinate high-spin complexes are favoured. Amongst many conclusions, it was found that oxygen cannot form a stable low-spin [Fe(II)(Por)L(O₂)] complex and that oxy-haemoglobin is best described as an [Fe(III)(Por)L(O₂^-)] complex, the iron is ferric bound to the superoxide molecule.