Mechanistic insights into nitrogen fixation by nitrogenase enzymes

J. B. Varley*, Y. Wang, K. Chan, F. Studt, J. K. Nørskov

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

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.

Original languageEnglish
JournalPhysical Chemistry Chemical Physics
Volume17
Issue number44
Pages (from-to)29541-29547
Number of pages7
ISSN1463-9076
DOIs
Publication statusPublished - 2015
Externally publishedYes

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