The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
A bound reaction intermediate sheds light on the mechanism of nitrogenase
Open accessAbstract
Sulfur steps aside for nitrogen: Enzymatic conversion of molecular nitrogen to ammonia requires a dance of electrons and protons. The stage for that dance is the nitrogenase cofactor, a carefully constructed cluster of iron, sulfur, and carbon with homocitrate and, in some cases, bicarbonate appendages, as well as a secondary metal ion that defines the class of enzyme. The question of how this cofactor binds nitrogen has been vexingly difficult to answer. Sippel et al. report a high-resolution structure of the vanadium nitrogenase with a light atom, interpreted as nitrogen, bound to the FeV cofactor. A sulfur atom is displaced from the cofactor in this structure and is observed resting in a holding site formed by rearrangement of a glutamine residue. The putative bridging nitrogen atom suggests that diatomic nitrogen may bind to the cluster in a head-on manner, with the glutamine side chain stabilizing protonated intermediates as they are reduced. Science , this issue p. 1484
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Cited by
Catalytic Applications of Vanadium: A Mechanistic Perspective
Langeslay, R. R., Kaphan, D. M., Marshall, C. L., Stair, P. C., Sattelberger, A. P., & Delferro, M. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00245 · Cited by 503
Computational Approach to Molecular Catalysis by 3d Transition Metals: Challenges and Opportunities
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Structural Enzymology of Nitrogenase Enzymes
Einsle, O., & Rees, D. C. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00067 · Cited by 409
Self-citationReduction 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
Metadata
- Authors
- Sippel, D., Rohde, M., Netzer, J., Trncik, C., Gies, J., Grunau, K., Djurdjevic, I., Decamps, L., Andrade, S. L. A., & Einsle, O.
- Venue
- Science
- Published
- 2018-03-30
- Volume
- 359
- Issue
- 6383
- Pages
- 1484-1489
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2794637900
- Cited by
- 308
- References
- 45
- FWCI
- 8.99
- Type
- journal article
- Language
- en
- Open access
- green
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