Synthesis, Characterization, and Nitrogenase-Relevant Reactions of an Iron Sulfide Complex with a Bridging Hydride

Abstract

The FeMoco of nitrogenase is an iron-sulfur cluster with exceptional bond-reducing abilities. ENDOR studies have suggested that E4, the state that binds and reduces N2, contains bridging hydrides as part of the active-site iron-sulfide cluster. However, there are no examples of any isolable iron-sulfide cluster with a hydride, which would test the feasibility of such a species. Here, we describe a diiron sulfide hydride complex that is prepared using a mild method involving C-S cleavage of added thiolate. Its reactions with nitrogenase substrates show that the hydride can act as a base or nucleophile and that reduction can cause the iron atoms to bind N2. These results add experimental support to hydride-based pathways for nitrogenase.

DOI: 10.1021/jacs.5b06841

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Cite this paper

@inproceedings{Arnet2015SynthesisCA, title={Synthesis, Characterization, and Nitrogenase-Relevant Reactions of an Iron Sulfide Complex with a Bridging Hydride}, author={Nicholas A. Arnet and Thomas R. Dugan and Fabian S Menges and Brandon Q. Mercado and William W Brennessel and Eckhard Bill and Mark A Johnson and Patrick L Holland}, booktitle={Journal of the American Chemical Society}, year={2015} }