Influence of the Nitrogen Donors on Nonheme Iron Models of Superoxide Reductase: High-Spin FeIII-OOR Complexes

A new five-coordinate, (N4S(thiolateffe))Fe-II complex, containing tertiary amine donors, [Fe-II(Me-4[15]aneN(4))(SPh)]BPh4 (2), was synthesized and structurally characterized as a model of the reduced active site of superoxide reductase (SOR). Reaction of 2 with tert-butyl hydroperoxide (tBuOOH) at -78 degrees C led to the generation of the alkylperoxo-iron(III) complex [Fe-III(Me-4[15]aneN(4))(SPh) (OOtBu)](+) (2a). The nonthiolate-ligated complex, [Fe-II(Me-4[15]aneN(4))(OTf)(2)] (3), was also reacted with tBuOOH and yielded the corresponding alkylperoxo-iron(III) complex [Fe-II(Me-4[15]aneN(4))(OTf)(OOtBu)](+) (3a) at an elevated temperature of -23 degrees C. These species were characterized by low-temperature UV-vis, EPR, and resonance Raman spectroscopies. Complexes 2a and 3a exhibit distinctly different spectroscopic signatures than the analogous alkylperoxo complexes [Fe-III([15]aneN(4))(SAr)(OOR)](+), which contain secondary amine donors. Importantly, alkylation at nitrogen leads to a change from low-spin (S = 1/2) to high-spin (S = 5/2) of the iron(Ill) center. The resonance Raman data reveal that this change in spin state has a large effect on the nu(Fe-O) and nu(O-O) vibrations, and a comparison between 2a and the nonthiolate-ligated complex 3a shows that axial ligation has an additional significant impact on these vibrations. To our knowledge this study is the first in which the influence of a ligand trans to a peroxo moiety has been evaluated for a structurally equivalent pair of high-spin/low-spin peroxo-iron(III) complexes. The implications of spin state and thiolate ligation are discussed with regard to the functioning of SOR.