Structural basis of biological nitrogen fixation

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 reduct...

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Bibliographic Details
Published in:Philosophical transactions of the Royal Society of London. Series A: Mathematical, physical, and engineering sciences physical, and engineering sciences, 2005-04, Vol.363 (1829), p.971-984
Main Authors: Rees, Douglas C, Akif Tezcan, F, Haynes, Chad A, Walton, Mika Y, Andrade, Susana, Einsle, Oliver, Howard, James B
Format: Article
Language:English
Subjects:
Ammonia
Ammonia - chemistry
Ammonia - metabolism
Animals
Biochemistry
Biological Electron Transfer
Biological nitrogen fixation
Catalysis
Cell Physiological Phenomena
Electron transfer
Electron Transport
Electrons
Enzyme Activation
Humans
Hydrolysis
Iron
Iron-Sulphur Proteins
Ligands
Models, Biological
Models, Chemical
Multienzyme Complexes - chemistry
Multienzyme Complexes - metabolism
Nitrogen
Nitrogenase
Nitrogenase - chemistry
Nitrogenase - metabolism
Nucleotide-Switch Proteins
Nucleotides
Oxidation-Reduction
Signal Transduction - physiology
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Summary: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.
ISSN:1364-503X
1471-2962
DOI:10.1098/rsta.2004.1539