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Substrate Interactions with the Nitrogenase Active Site
Abstract
The chemical mechanism for biological cleavage of the N(2) triple bond at ambient pressure and temperature has been the subject of intense study for many years. The site of substrate activation and reduction has been localized to a complex cofactor, called FeMo cofactor, yet until now the complexity of the system has denied information concerning exactly where and how substrates interact with the metal-sulfur framework of the active site. In this Account, we describe a combined genetic, biophysical, and biochemical approach that was used to provide direct and detailed information concerning where alternative alkyne substrates interact with FeMo cofactor during catalysis. The relevance and limitations of this work with respect to N(2) binding and reduction also are discussed.
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Cites
Structure–function relationships of alternative nitrogenases
Eady, R. R. (1996) · Chemical Reviews · doi:10.1021/cr950057h · Cited by 877
Cooperation of GGAs and AP-1 in Packaging MPRs at the Trans-Golgi Network
Doray, B., Ghosh, P., Griffith, J., Geuze, H. J., & Kornfeld, S. (2002) · Science · doi:10.1126/science.1075327 · Cited by 312
Cited by
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Self-citationStudies of Low-Coordinate Iron Dinitrogen Complexes
Smith, J. M., Sadique, A. R., Cundari, T. R., Rodgers, K. R., Lukat-Rodgers, G., Lachicotte, R. J., Flaschenriem, C. J., Vela, J., & Holland, P. L. (2006) · Journal of the American Chemical Society · doi:10.1021/ja052707x · Cited by 323
Serpentinization: connecting geochemistry, ancient metabolism and industrial hydrogenation
Preiner, M., Xavier, J. C., Sousa, F. L., Zimorski, V., Neubeck, A., Lang, S. Q., Greenwell, H. C., Kleinermanns, K., Tüysüz, H., McCollom, T. M., et al. (2018) · Life · doi:10.3390/life8040041 · Cited by 97
Metadata
- Authors
- Dos Santos, P. C., Igarashi, R. Y., Lee, H.-I., Hoffman, B. M., Seefeldt, L. C., & Dean, D. R.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-02-02
- Volume
- 38
- Issue
- 3
- Pages
- 208-214
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2074222618
- Cited by
- 216
- References
- 2
- FWCI
- 11.99
- Type
- journal article
- Language
- en
- Open access
- closed
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