Nitrogen reduction by the Fe sites of synthetic [MoSFe] cubes.

Nitrogen (N) fixation by nature, which is a crucial process for the supply of bio-available forms of nitrogen, is performed by nitrogenase. This enzyme uses a unique transition-metal-sulfur-carbon cluster as its active-site co-factor ([(R-homocitrate)MoFeSC], FeMoco), and the sulfur-surrounded iron (Fe) atoms have been postulated to capture and reduce N (refs. ).

Synthesis of [MoS] Clusters from Half-Sandwich Molybdenum(V) Chlorides and Their Application as Platforms for [MoSFe] Cubes.

Triangular [MoS] clusters are known to serve as platforms to accommodate a metal atom M, furnishing cubic [MoSM] clusters. In this study, three [MoS] clusters supported by η-cyclopentadienyl (Cp) ligands, [CpMoS] (Cp = CMeSiMe, CMeSiEt, and CMeH), were synthesized via half-sandwich molybdenum chlorides CpMoCl. In the cyclic voltammogram of the [MoS] cluster having CMeH ligands, a weak feature appeared in addition to the [CpMoS] redox process, indicating the interaction between [CpMoS] and the [NBu] cation of the electrolyte, while such a feature was less significant for the CMeSiR variants.