Abstract
The reactivities of the model complexes, [Fe4S4(SPh)4]2- (1) and [Fe2S2(SPh)4]2- (2), of nonheme iron-sulfur proteins were compared. Complex 1 catalyzed the oxidation of benzenethiol to diphenyl disulfide with the reduction of dioxygen to H2O. Complex 2 did not catalyze it, but the reaction proceeded after an induction period during which complex 2 was converted to complex 1. In addition, complex 1 catalyzed the reduction of 1, 4-dinitrobenzene to N -(4-nitrophenyl)hydroxylamine (21 %) and 4-nitroaniline (16 %) with the oxidation of benzenethiol to diphenyl disulfide, but complex 2 induced mainly the displacement of nitro group to phenylthio group to give 1-nitro-4-(phenylthio)benzene (92 %). It was revealed that the reactivities of complex 1 complex 2 are quite different.
