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Biological nitrogen fixation in theory, practice, and reality: a perspective on the molybdenum nitrogenase system

Threatt, Stephanie D. and Rees, Douglas C. (2023) Biological nitrogen fixation in theory, practice, and reality: a perspective on the molybdenum nitrogenase system. FEBS Letters, 597 (1). pp. 45-58. ISSN 0014-5793. PMCID PMC10100503. doi:10.1002/1873-3468.14534.

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Nitrogenase is the sole enzyme responsible for the ATP-dependent conversion of atmospheric dinitrogen into the bioavailable form of ammonia (NH₃), making this protein essential for the maintenance of the nitrogen cycle and thus life itself. Despite the widespread use of the Haber–Bosch process to industrially produce NH₃, biological nitrogen fixation still accounts for half of the bioavailable nitrogen on Earth. An important feature of nitrogenase is that it operates under physiological conditions, where the equilibrium strongly favours ammonia production. This biological, multielectron reduction is a complex catalytic reaction that has perplexed scientists for decades. In this review, we explore the current understanding of the molybdenum nitrogenase system based on experimental and computational research, as well as the limitations of the crystallographic, spectroscopic, and computational techniques employed. Finally, essential outstanding questions regarding the nitrogenase system will be highlighted alongside suggestions for future experimental and computational work to elucidate this essential yet elusive process.

Item Type:Article
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URLURL TypeDescription CentralArticle
Threatt, Stephanie D.0000-0002-2303-2166
Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. This is an open access article under the terms of the License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. We thank Dr Rebecca Warmack, Dr Trixia Buscagan, Dr Siobhan MacArdle and Ailiena Maggiolo for discussions, and Prof William Goddard and Charles Musgrave for their invaluable advice and insights on density functional calculations on nitrogenase. This work was supported by the Howard Hughes Medical Institute.
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Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Issue or Number:1
PubMed Central ID:PMC10100503
Record Number:CaltechAUTHORS:20221212-796808400.40
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ID Code:118324
Deposited By: Research Services Depository
Deposited On:14 Jan 2023 21:10
Last Modified:18 May 2023 22:46

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