Breaking the N 2 triple bond: Insights into the nitrogenase mechanism

Brett M. Barney, Hong In Lee, Patricia C. Dos Santos, Brian M. Hoffman, Dennis R. Dean, Lance C. Seefeldt

Research output: Contribution to journalArticlepeer-review

104 Scopus citations


Nitrogenase is the metalloenzyme that performs biological nitrogen fixation by catalyzing the reduction of N 2 to ammonia. Understanding how the nitrogenase active site metal cofactor (FeMo-cofactor) catalyzes the cleavage of the N 2 triple bond has been the focus of intense study for more than 50 years. Goals have included the determination of where and how substrates interact with the FeMo-cofactor, and the nature of reaction intermediates along the reduction pathway. Progress has included the trapping of intermediates formed during turnover of non-physiological substrates (e.g., alkynes, CS 2) providing insights into how these molecules interact with the nitrogenase FeMo-cofactor active site. More recently, substrate-derived species have been trapped at high concentrations during the reduction of N 2, a diazene, and hydrazine, providing the first insights into binding modes and possible mechanisms for N 2 reduction. A comparison of the current state of knowledge of the trapped species arising from non-physiological substrates and nitrogenous substrates is beginning to reveal some of the intricacies of how nitrogenase breaks the N 2 triple bond.

Original languageEnglish (US)
Pages (from-to)2277-2284
Number of pages8
JournalDalton Transactions
Issue number19
StatePublished - 2006


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