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Structural basis of biological nitrogen fixation

Rees, Douglas C. and Tezcan, F. Akif and Haynes, Chad A. and Walton, Mika Y. and Andrade, Susana and Einsle, Oliver and Howard, James B. (2005) Structural basis of biological nitrogen fixation. Philosophical Transactions A: Mathematical, Physical and Engineering Sciences, 363 (1829). pp. 971-984. ISSN 1364-503X.

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Biological nitrogen fixation is mediated by the nitrogenase enzyme system that catalyses the ATP dependent reduction of atmospheric dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the MoFe-protein with the FeMo-cofactor that provides the active site for substrate reduction, and the Fe-protein that couples ATP hydrolysis to electron transfer. An overview of the nitrogenase system is presented that emphasizes the structural organization of the proteins and associated metalloclusters that have the remarkable ability to catalyse nitrogen fixation under ambient conditions. Although the mechanism of ammonia formation by nitrogenase remains enigmatic, mechanistic inferences motivated by recent developments in the areas of nitrogenase biochemistry, spectroscopy, model chemistry and computational studies are discussed within this structural framework.

Item Type:Article
Related URLs:
URLURL TypeDescription
Rees, Douglas C.0000-0003-4073-1185
Tezcan, F. Akif0000-0002-4733-6500
Additional Information:© 2005 The Royal Society. Published online 5 April 2005. We thank the US National Institutes of Health for research support (GM45162) and the Helen Hay Whitney Foundation for a postdoctoral fellowship to F.A.T.
Funding AgencyGrant Number
Helen Hay Whitney FoundationUNSPECIFIED
Subject Keywords:nitrogenase; iron–sulphur proteins; nucleotide-switch proteins; biological electron transfer
Issue or Number:1829
Record Number:CaltechAUTHORS:20180507-142707424
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Official Citation:Structural basis of biological nitrogen fixation Douglas C Rees, F Akif Tezcan, Chad A Haynes, Mika Y Walton, Susana Andrade, Oliver Einsle, James B Howard Phil. Trans. R. Soc. A 2005 363 971-984; DOI: 10.1098/rsta.2004.1539. Published 15 April 2005
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:86269
Deposited By: Tony Diaz
Deposited On:07 May 2018 21:37
Last Modified:31 Jan 2020 22:36

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