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Issue 44, 2015
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Mechanistic insights into nitrogen fixation by nitrogenase enzymes

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Abstract

Biological nitrogen fixation by nitrogenase enzymes is a process that activates dinitrogen (N2) one of the most inert molecules in nature, within the confines of a living organism and at ambient conditions. Despite decades of study, there are still no complete explanations as to how this is possible. Here we describe a model of N2 reduction using the Mo-containing nitrogenase (FeMoco) that can explain the reactivity of the active site via a series of electrochemical steps that reversibly unseal a highly reactive Fe edge site. Our model can explain the 8 proton–electron transfers involved in biological ammonia synthesis within the kinetic scheme of Lowe and Thorneley, the obligatory formation of one H2 per N2 reduced, and the behavior of known inhibitors.

Graphical abstract: Mechanistic insights into nitrogen fixation by nitrogenase enzymes

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Supplementary files

Article information


Submitted
13 Jul 2015
Accepted
01 Sep 2015
First published
09 Sep 2015

Phys. Chem. Chem. Phys., 2015,17, 29541-29547
Article type
Paper

Mechanistic insights into nitrogen fixation by nitrogenase enzymes

J. B. Varley, Y. Wang, K. Chan, F. Studt and J. K. Nørskov, Phys. Chem. Chem. Phys., 2015, 17, 29541
DOI: 10.1039/C5CP04034E

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