Breaking the N2 triple bond: insights into the nitrogenase mechanism

Abstract

Nitrogenase is the metalloenzyme that performs biological nitrogen fixation by catalyzing the reduction of N₂ to ammonia. Understanding how the nitrogenase active site metal cofactor (FeMo-cofactor) catalyzes the cleavage of the N₂ 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, CS₂) 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 N₂, a diazene, and hydrazine, providing the first insights into binding modes and possible mechanisms for N₂ 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 N₂ triple bond.