Biomimetic complexes are artificially engineered molecules that aim to reduce the structural complexity of biological systems in order to unveil the key electronic and structural factors relevant to a protein's function. In this work, a novel coordination compound (L22Fe22) which mimics non-heme binuclear proteins was synthesized from the Schiff-base ligand HL = (E)-N′-(phenyl(pyridin-2-yl)methylene)isonicotinohydrazide. The crystal structure of L22Fe22 showed that the intramolecular Fe–Fe distances (3.1–3.2 Å) were analogous to those found in non-heme binuclear ferric proteins. However, in L22Fe22, two methoxide groups act as bridging units for oxidized iron (Fe3+). Such a bridging motif is unprecedented in the biological realm. Magnetic susceptibility measurements demonstrated that L22Fe22 is characterized by a singlet (S = 0) ground state and a very small magnetic coupling constant J (≪ −1 cm−1). The J value featured by L22Fe22 differs considerably from the values observed in non-heme binuclear proteins in the oxidized form (−100 cm−1 < J < −10 cm−1), which encompass oxo/hydroxo and carboxylate bridging residues. The singlet ground state of L22Fe22 as well as the weak magnetic interaction between the two ferric cations was successfully predicted by density functional theory (DFT).