The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Substrate Interactions with Nitrogenase: Fe versus Mo
Abstract
Biological nitrogen reduction is catalyzed by a complex two-component metalloenzyme called nitrogenase. For the Mo-dependent enzyme, the site of substrate reduction is provided by a [7Fe-9S-Mo-X-homocitrate] metallocluster, where X is proposed to be an N atom. Recent progress with organometallic model compounds, theoretical calculations, and biochemical, kinetic, and biophysical studies on nitrogenase has led to the formulation of two opposing models of where N(2) or alternative substrates might bind during catalysis. One model involves substrate binding to the Mo atom, whereas the other model involves the participation of one or more Fe atoms located in the central region of the metallocluster. Recently gathered evidence that has provided the basis for both models is summarized, and a perspective on future research in resolving this fundamental mechanistic question is presented.
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Cites
Structure–function relationships of alternative nitrogenases
Eady, R. R. (1996) · Chemical Reviews · doi:10.1021/cr950057h · Cited by 877
A Possible Prebiotic Formation of Ammonia from Dinitrogen on Iron Sulfide Surfaces
Dörr, M., Käßbohrer, J., Grunert, R., Kreisel, G., Brand, W. A., Werner, R. A., Geilmann, H., Apfel, C., Robl, C., & Weigand, W. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200250371 · Cited by 132
Cited by
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
Self-citationStructural basis of biological nitrogen fixation
Rees, D. C., Akif Tezcan, F., Haynes, C. A., Walton, M. Y., Andrade, S., Einsle, O., & Howard, J. B. (2005) · Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences · doi:10.1098/rsta.2004.1539 · Cited by 1,120
On the origin of biochemistry at an alkaline hydrothermal vent
Martin, W., & Russell, M. J. (2007) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2006.1881 · Cited by 771
Nitrogen fixation and hydrogen metabolism in cyanobacteria
Bothe, H., Schmitz, O., Yates, M. G., & Newton, W. E. (2010) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00033-10 · Cited by 416
Reduction of Substrates by Nitrogenases
Seefeldt, L. C., Yang, Z.-Y., Lukoyanov, D. A., Harris, D. F., Dean, D. R., Raugei, S., & Hoffman, B. M. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00556 · Cited by 396
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Metadata
- Authors
- Seefeldt, L. C., Dance, I. G., & Dean, D. R.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2004-01-13
- Volume
- 43
- Issue
- 6
- Pages
- 1401-1409
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2092054047
- Cited by
- 185
- References
- 2
- FWCI
- 19.30
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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