Axial Thiophenolate Coordination on Diiron(III)bisporphyrin: Influence of Heme–Heme Interactions on Structure, Function and Electrochemical Properties of the Individual Heme Center

The binding of a series of substituted thiophenols as axial ligands on a highly flexible ethane-bridged diiron­(III)­bisporphyrin framework has been investigated as a model of diheme proteins. Spectroscopic characterization reveals a high-spin (<i>S</i> = 5/2) state of iron for all of the pentacoordinate thiophenolato complexes. In the UV–visible spectra of the complexes, the positions of the Soret and band I have been found to be dependent on the p<i>K</i> <sub>a</sub> of thiophenols. The alternating shift pattern, which has opposite sign of the chemical shifts for meta- vs. ortho- and para- protons in the <sup>1</sup>H NMR spectra, is attributed to negative and positive spin densities, respectively, on thiophenolate carbon atoms and is indicative of π-spin delocalization to the bound thiophenolate ligand. The Fe­(III)/Fe­(II) redox couple of the complexes bears a linear relationship with the p<i>K</i> <sub>a</sub> of thiophenol and is found to be positively shifted with decreasing p<i>K</i> <sub>a</sub>. The effect of the electronic nature of the substituent on the thiophenolate ring has also been demonstrated in which a large potential range of 540 mV was observed (in contrast to the value of only 270 mV in case of monoheme analogues) for the Fe­(III)/Fe­(II) redox couple on going from monoheme to diheme and is attributed to the interheme interaction. Also, the Fe­(III)/Fe­(II) redox potential of the thiophenolato complexes has been found to be more positively shifted compared to their phenolato analogues, which was further supported by DFT calculation. The addition of another thiophenol at the sixth axial position of the five-coordinate thiophenolato complex causes a change in iron spin from high (<i>S</i> = 5/2) to low (<i>S</i> = 1/2) along with a large positive shift of 490 mV for the Fe­(III)/Fe­(II) redox couple.