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N2 activation on a molybdenum-titanium-sulfur cluster.

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.

SUBMITTER: Ohki Y

PROVIDER: S-EPMC6086867 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature

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N2 activation on a molybdenum-titanium-sulfur cluster.

Ohki Yasuhiro Y Uchida Keisuke K Tada Mizuki M Cramer Roger E RE Ogura Takashi T Ohta Takehiro T

Nature communications 20180810 1

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 tha ...[more]

PMID: 30097563

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