The structures and stabilities of the complexes of biologically available ligands with Fe(III)-porphine: an ab initio...

Fe(III) porphine complexes and a limited number of Fe(II) porphine complexes were investigated at the 'MP2/LB'//B3LYP/SB level of theory, where SB and LB represent small and large basis sets, 6-31+G(d) and 6-311+G(2df,2p), respectively. Solvation effects were incorporated by the IEFPCM procedure. Most of the ligands whereby the heme prosthetic group is bound in biological systems were modeled in the study. These include H(2)O, Im (imidazole), CH(3)NH(2), CH(3)CO(2)(-), CH(3)S(-), CH(3)PhO(-), OH(-), and Cl(-). Fe(III) porphine, 2(+), and the pentacoordinated complexes, 2(+)(Im), 2(+)(CH(3)NH(2)), and 2(+)(H(2)O), have quartet ground states. The pentacoordinated complexes with negatively charged ligands all have high spin hextet ground states. All of the hexacoordinated complexes have low spin doublet ground states, with the exception of 2(+)(H(2)O)(2) and 2(+)(H(2)O)(Im) which have intermediate spin quartet ground states. None of the pentacoordinated complexes, 2(+)(OH(-)), 2(+)(CH(3)PhO(-)), and 2(+)(CH(3)S(-)), are predicted to form stable hexacoordinated complexes in water with any of the ligands of the present study. The most stable species in water is 2(+)(OH(-)). The hydroxide may be displaced by CH(3)PhOH and CH(3)SH at physiological pH, and by Cl(-), CH(3)CO(2)(-), and Im under acidic conditions, but not by CH(3)NH(3)(+). The relevance of the present results for the pH-dependent transitions of cytochrome c and the fragments, NAcMP8, and NAcMP11, the resting state of cytochrome P450, and the bonding interactions between heme and Aβ, is discussed.