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Is N2 A Triple Bond

Breaking the N2 triple bail: insights into the nitrogenase mechanism

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Abstruse

Nitrogenase is the metalloenzyme that performs biological nitrogen fixation by catalyzing the reduction of N two to ammonia. Agreement how the nitrogenase active site metal cofactor (FeMo-cofactor) catalyzes the cleavage of the N 2 triple bond has been the focus of intense report for more than 50 years. Goals have included the determination of where and how substrates collaborate with the FeMo-cofactor, and the nature of reaction intermediates forth 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 accept been trapped at loftier concentrations during the reduction of N two , a diazene, and hydrazine, providing the offset insights into binding modes and possible mechanisms for Due north 2 reduction. A comparison of the current state of knowledge of the trapped species arising from not-physiological substrates and nitrogenous substrates is beginning to reveal some of the intricacies of how nitrogenase breaks the North 2 triple bond.

Graphical abstract: Breaking the N2 triple bond: insights into the nitrogenase mechanism

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Article information

DOI
https://doi.org/x.1039/B517633F

Article blazon
Perspective

Submitted
xiii Dec 2005

Accepted
29 Mar 2006

First published
xi Apr 2006

Dalton Trans. , 2006, 2277-2284

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Breaking the N ii triple bond: insights into the nitrogenase mechanism

B. M. Barney, H. Lee, P. C. Dos Santos, B. One thousand. Hoffman, D. R. Dean and L. C. Seefeldt, Dalton Trans., 2006, 2277 DOI: 10.1039/B517633F

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Is N2 A Triple Bond,

Source: https://pubs.rsc.org/en/content/articlelanding/2006/dt/b517633f

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