The DOI matches its Crossref record; 184 of the 184 references it cites were found in a registry or an index.
Structural Enzymology of Nitrogenase Enzymes
Open accessAbstract
The reduction of dinitrogen to ammonia by nitrogenase reflects a complex choreography involving two component proteins, MgATP and reductant. At center stage of this process resides the active site cofactor, a complex metallocluster organized around a trigonal prismatic arrangement of iron sites surrounding an interstitial carbon. As a consequence of the choreography, electrons and protons are delivered to the active site for transfer to the bound N 2 . While the detailed mechanism for the substrate reduction remains enigmatic, recent developments highlight the role of hydrides and the privileged role for two irons of the trigonal prism in the binding of exogenous ligands. Outstanding questions concern the precise nature of the intermediates between N 2 and NH 3, and whether the cofactor undergoes significant rearrangement during turnover; resolution of these issues will require the convergence of biochemistry, structure, spectroscopy, computation, and model chemistry.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
(1961) · Journal of the Optical Society of America · doi:10.1364/josa.51.000248 · Cited by 2,288
Ingolia, N. T., Lareau, L. F., & Weissman, J. S. (2011) · Cell · doi:10.1016/j.cell.2011.10.002 · Cited by 2,187
COOPERATION OF CHARGES IN PHOTOSYNTHETIC O2 EVOLUTION–I. A LINEAR FOUR STEP MECHANISM
KOK, B., FORBUSH, B., & McGLOIN, M. (1970) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1970.tb06017.x · Cited by 2,114
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 Molybdenum Nitrogenase
Burgess, B. K., & Lowe, D. J. (1996) · Chemical Reviews · doi:10.1021/cr950055x · Cited by 1,854
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
Challenges in reduction of dinitrogen by proton and electron transfer
van der Ham, C. J. M., Koper, M. T. M., & Hetterscheid, D. G. H. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00085d · Cited by 1,583
Catalytic Reduction of Dinitrogen to Ammonia at a Single Molybdenum Center
Yandulov, D. V., & Schrock, R. R. (2003) · Science · doi:10.1126/science.1085326 · Cited by 1,433
Classification and evolution of P-loop GTPases and related ATPases
Leipe, D. D., Wolf, Y. I., Koonin, E. V., & Aravind, L. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5378 · Cited by 1,148
Nitrogenase MoFe-Protein at 1.16 Å Resolution: A Central Ligand in the FeMo-Cofactor
Einsle, O., Tezcan, F. A., Andrade, S. L. A., Schmid, B., Yoshida, M., Howard, J. B., & Rees, D. C. (2002) · Science · doi:10.1126/science.1073877 · Cited by 1,093
Self-citation
Cited by
Towards practical applications in quantum computational biology
Fedorov, A. K., & Gelfand, M. S. (2021) · Nature Computational Science · doi:10.1038/s43588-021-00024-z · Cited by 62
Architecture of the RNF1 complex that drives biological nitrogen fixation
Zhang, L., & Einsle, O. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01641-1 · Cited by 25
Self-citationIllava, G., Gillilan, R., & Ando, N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105039 · Cited by 5
Structural evolution of nitrogenase over 3 billion years
Cuevas Zuviría, B., Detemple, F., Amritkar, K., Garcia, A. K., Seefeldt, L., Einsle, O., & Kaçar, B. (2025) · eLife · doi:10.7554/elife.105613 · Cited by 4
Self-citation
Metadata
- Authors
- Einsle, O., & Rees, D. C.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2020-06-15
- Volume
- 120
- Issue
- 12
- Pages
- 4969-5004
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W3035190513
- Cited by
- 409
- References
- 184
- FWCI
- 1.94
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Structural Enzymology of Nitrogenase Enzymes. https://app.cochat.ai/papers/10.1021/acs.chemrev.0c00067
- The paper
- Einsle, O., & Rees, D. C. (2020). Structural Enzymology of Nitrogenase Enzymes. Chemical Reviews. https://doi.org/10.1021/acs.chemrev.0c00067
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
