Abstract
The FeMo-cofactor of nitrogenase, a metal–sulfur cluster that contains eight transition metals, promotes the conversion of dinitrogen into ammonia when stored in the protein. Although various metal–sulfur clusters have been synthesized over the past decades, their use in the activation of N2 has remained challenging, and even the FeMo-cofactor extracted from nitrogenase is not able to reduce N2. Herein, we report the activation of N2 by a metal–sulfur cluster that contains molybdenum and titanium. An N2 moiety bridging two [Mo3S4Ti] cubes is converted into NH3 and N2H4 upon treatment with Brønsted acids in the presence of a reducing agent.
Highlights
The FeMo-cofactor of nitrogenase, a metal–sulfur cluster that contains eight transition metals, promotes the conversion of dinitrogen into ammonia when stored in the protein
The extracted form catalyzes the reduction of non-native C1 substrates, such as CO and CO2 in the presence of reducing agents and protons to furnish CH4 and short-chain hydrocarbons8,9, and similar catalytic reductions can be accomplished with the synthetic analog [Cp*MoFe5S9(SH)]3– (Cp* = η5-C5Me5)10
N2 cannot be reduced with the extracted FeMo-cofactor7 or its synthetic analogs, highlighting the difference in N2-reducing activity between the proteinsupported FeMo-cofactor and discrete metal–sulfur clusters in solution
Summary
The FeMo-cofactor of nitrogenase, a metal–sulfur cluster that contains eight transition metals, promotes the conversion of dinitrogen into ammonia when stored in the protein. The resulting [Mo3S4Ti] cluster (Fig. 2, top right) is reduced in the presence of N2, to generate a Ti-based reaction site for the activation of N2.
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