Spin-Flip via Subtle Electronic Perturbation in Axially Ligated Diiron(III) Porphyrin Dimer.

Spin state switching in the metal center is a crucial phenomenon in many enzymatic reactions in biology. The spin state alteration, a critical step in cytochrome P450 catalysis, is driven most likely through a weak perturbation upon substrate binding in the enzyme, which is still not well clarified. In the current work, the spin state transition of iron(III) from high to intermediate via an admixed state is observed upon a subtle electronic perturbation to the sulphonate moieties coordinated axially to a diiron(III)porphyrin dimer. While electron-donating substituents stabilize the high-spin state of iron(III), strongly electron-withdrawing groups stabilize an intermediate-spin state, whereas the moderate electron-withdrawing nature of axial ligands resulted in an admixed state. Confirmation of the molecular structures and their spin states have been made utilizing single-crystal X-ray structure analysis, Mössbauer, magnetic, EPR, and 1H NMR spectroscopic investigations. The position of the signals of the porphyrin macrocycle in the paramagnetic 1H NMR is found to be very characteristic of the spin state of the iron center in solution. The Curie plot for the pure high-spin complexes shows the signals' temperature dependency in line with the Curie law. Conversely, the pure intermediate-spin state of iron exhibits an anti-Curie temperature dependence, whereas the admixed-spin state of iron displays significant curvature of the lines in the Curie plot. An extensive DFT analysis displays a linear dependence between the energy difference between d x 2 - y 2 ${{_{x{^{2}}- y{^{2}}}}}$ and d z 2 ${{_{z{^{2}}}}}$ orbital versus Fe-Npor distance for the complexes reported here. Furthermore, a strong linear correlation between the Fe-O distance and the spin density over the oxygen atom, as well as the Fe-Npor distance for the complexes, has been observed. Thus, a slight electronic perturbation at the axial ligand of the diheme resulted in a large change in the electronic structures with a spin-flip. This is at par with the metalloenzymes, which employ minute perturbations around the periphery of the active sites, leading to spin state transitions.

Diheme cytochromes: Effect of mixed-axial ligation on the electronic structure and electrochemical properties with cobalt porphyrin dimer.

A series of six-coordinate diCo(III) porphyrin dimers, as synthetic analogues of diheme cytochromes, have been reported here having bis(imidazole), bis(pyridine) and mixed thiophenolate-pyridine/imidazole axial ligands. In the X-ray structures of bis(imidazole) and bis(pyridine) complexes, the axial ligands are in perpendicular orientation while they are parallelly oriented in their monomeric analog. The porphyrin rings are also highly ruffle-distorted in dimer but planar in monomer which reflect the effect of intramolecular interaction between two Co(porphyrin) units in dimers. In the X-ray structure of diCo(III) thiophenolate-pyridine mixed-ligated complex, the axial Co-S and Co-N(py) distances are 2.256(1) and 2.063(2) Å, respectively. The Co-N(py) distance of 2.063(2) Å is much longer than the distances of 1.961(3) and 1.972(3) Å observed in bis(pyridine) complex and the Co-S distance is larger than Co-N(py) in the mixed ligated complex which results in a displacement of Co by 0.15 Štowards the pyridine ligand from the mean porphyrin plane. Indeed, this is the first X-ray structure of a metalloporphyrin with mixed thiophenolate-pyridine axial ligands. The effect of mixed-axial ligation is demonstrated by a blue-shift of the Soret band in the UV-visible spectroscopy and also a positive shift of the Co(III)/Co(II) redox couple as compared to their bis(pyridine) analogue. The redox potentials are shifted to a large negative value just upon replacing the metal from iron to cobalt. The present investigation emphasizes the role of axial ligation, metal ions, and also the effect of heme-heme interaction in controlling the spectral and electrochemical properties.