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

Abstract

AbstractSpin 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 and d 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.