The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Structural basis of biological nitrogen fixation
Abstract
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.
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Cites
The Guanine Nucleotide-Binding Switch in Three Dimensions
Vetter, I. R., & Wittinghofer, A. (2001) · Science · doi:10.1126/science.1062023 · Cited by 1,875
Structure–function relationships of alternative nitrogenases
Eady, R. R. (1996) · Chemical Reviews · doi:10.1021/cr950057h · Cited by 877
Aconitase as iron–sulfur protein, enzyme, and iron-regulatory protein
Beinert, H., Kennedy, M. C., & Stout, C. D. (1996) · Chemical Reviews · doi:10.1021/cr950040z · Cited by 606
Great Metalloclusters in Enzymology
Rees, D. C. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135406 · Cited by 220
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Cited by
Iron-sulfur clusters: nature's modular, multipurpose structures
Beinert, H., Holm, R. H., & Münck, E. (1997) · Science · doi:10.1126/science.277.5326.653 · Cited by 1,944
Mechanism of Nitrogen Fixation by Nitrogenase: The Next Stage
Hoffman, B. M., Lukoyanov, D., Yang, Z.-Y., Dean, D. R., & Seefeldt, L. C. (2014) · Chemical Reviews · doi:10.1021/cr400641x · Cited by 1,766
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
Proterozoic Ocean Chemistry and Evolution: A Bioinorganic Bridge?
Anbar, A. D., & Knoll, A. H. (2002) · Science · doi:10.1126/science.1069651 · Cited by 1,191
Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor
Spatzal, T., Aksoyoglu, M., Zhang, L., Andrade, S. L. A., Schleicher, E., Weber, S., Rees, D. C., & Einsle, O. (2011) · Science · doi:10.1126/science.1214025 · Cited by 914
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Metadata
- Authors
- Rees, D. C., Akif Tezcan, F., Haynes, C. A., Walton, M. Y., Andrade, S., Einsle, O., & Howard, J. B.
- Venue
- Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences
- Publisher
- The Royal Society
- Published
- 2005-04-05
- Volume
- 363
- Issue
- 1829
- Pages
- 971-984
- ISSN
- 1364-503X (ISSN-L)
- 1471-2962
- OpenAlex
- W2125771483
- Cited by
- 1,120
- References
- 4
- FWCI
- 44.05
- Type
- journal article
- Language
- en
- Open access
- closed
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- Rees, D. C., Akif Tezcan, F., Haynes, C. A., Walton, M. Y., Andrade, S., Einsle, O., & Howard, J. B. (2005). Structural basis of biological nitrogen fixation. Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences. https://doi.org/10.1098/rsta.2004.1539
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