Biomimetic [MFe₃S₄]³⁺ Cubanes (M = V/Mo) as Catalysts for a Fischer–Tropsch-like Hydrocarbon Synthesis─A Computational Study

Nitrogenase is the enzyme primarily responsible for reducing atmospheric nitrogen to ammonia. There are three general forms of nitrogenase based on the metal ion present in the cofactor binding site, namely, molybdenum-dependent nitrogenases with the iron-molybdenum cofactor (FeMoco), the vanadium-dependent nitrogenases with FeVco, and the iron-only nitrogenases. It has been shown that the vanadium-dependent nitrogenases tend to have a lesser efficacy in reducing dinitrogen but a higher efficacy in binding and reducing carbon monoxide. In biomimetic chemistry, [MFe₃S₄] (M = Mo/V) cubanes have been synthesized, studied, and shown to be promising mimics of some of the geometric and electronic properties of the nitrogenase cofactors. In this work, a density functional theory (DFT) study is presented on Fischer-Tropsch catalysis by these cubane complexes by studying CO binding and reduction to hydrocarbons. Our work implies that molybdenum has stronger binding interactions with the iron-sulfur framework of the cubane, which results in easier reduction of substrates like N₂H₄. However, this inhibits the binding and activation of CO, and hence, the molybdenum-containing complexes are less suitable for Fischer-Tropsch catalysis than vanadium-containing complexes.