Studies on the binding of CO to low-spin [Fe(II)(Por)L2] complexes: an aid to understanding the binding of CO to haemoglobin and myoglobin.

The visible and Mössbauer spectra of [Fe(II)(Por)L2] and [Fe(II)(Por)L(CO)] complexes (where Por = protoporphyrin IX (PPIX) or tetra(p-sulfophenyl)porphyrin (TPPS) and L = an aliphatic or aromatic nitrogenous base) are reported and discussed. The results are compared to those of previously reported [Fe(II)(Por)L(CO)] complexes (where Por = PPIX, TPPS, PMXPP, TPP, OMTBP and OEP; L = a nitrogenous aromatic ligand) and HbCO (where Hb = haemoglobin) and MyCO (where My = myoglobin). A new approach, to extracting information from the Mössbauer parameters has been developed by plotting those of the [Fe(II)(Por)L2] complexes against those of [Fe(II)(Por)L(CO)] complexes for the same ligands, has yielded a series of trend lines that show a significant dependence on both the nature of the porphyrin and also of the nitrogenous ligand. Different trend lines were found for aromatic nitrogenous ligands to aliphatic nitrogenous ligands showing that the porphyrins could donate different amounts of charge to the Fe(II) cations as the L ligand changed, and hence, they display electron sink properties. From the plots, it was shown that haemoglobin and myoglobin both bind CO very strongly compared to the model complexes studied herein. Using the reported structural and Mössbauer data for the [Fe(II)(Por)L2] and [Fe(II)(Por)L(CO)] complexes, it proved possible and instructive to plot the Mössbauer parameters against a number of the bond lengths around the Fe(II) cations. The interpretation of the resulting trend lines both supported and facilitated the extension of our findings enabling further understanding of the geometry of the bonding in CO haemoglobin and CO myoglobin.

Studies on the binding of nitrogenous bases to protoporphyrin IX iron(II) in aqueous solution at high pH values.

Studies are reported on the formation of low-spin six-coordinate [Fe(PPIX)L2] complexes from iron(II) protoporphyrin where L is one of a series of nitrogenous ligands (aliphatic, aromatic or heterocyclic). The bonding constants have been determined by titration of the metal complex with these ligands and are compared in relation to previous studies. The adduct formation was monitored utilising optical spectroscopy. In addition, MÓ§ssbauer spectroscopic experiments were conducted to monitor the electronic environment around the central iron atom in these complexes. The two complementary spectroscopic methods indicated that all nitrogen ligands formed low-spin octahedral complexes. The magnitude of the overall binding constants (ß2 values) are discussed and related to (a) the pKa values of the free ligands and (b) the Mössbauer parameter ΔEQ, which represents the quadrupole splitting of the haem iron. The ß2 and ΔEQ values are also discussed in terms of the structure of the ligand. Cooperative binding was observed for nearly all the ligands with Hill coefficients close to 2 for iron(II) protoporphyrin; one of these ligands displayed a much greater affinity than any we previously studied, and this was a direct consequence of the structure of the ligand. Overall conclusions on these and previous studies are drawn in terms of aliphatic ligands versus aromatic ring structures and the absence or presence of sterically hindered nitrogen atoms. The implications of the work for the greater understanding of haem proteins in general and in particular how the nitrogenous ligand binding results are relevant to and aid the understanding of the binding of inhibitor molecules to the cytochrome P450 mono-oxygenases (for therapeutic purposes) are also discussed. Changes in the electronic absorption spectra of five-coordinate [Fe(II)(PPIX)(2-MeIm)] that occurred as the temperature was lowered from room temperature to 78° K.