The DOI matches its Crossref record.
Mechanism of Molybdenum Nitrogenase
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMechanism of Molybdenum NitrogenaseBarbara K. Burgess and David J. LoweView Author Information Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92717-3900, and Nitrogen Fixation Laboratory, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, U.K. Cite this: Chem. Rev. 1996, 96, 7, 2983–3012Publication Date (Web):November 7, 1996Publication History Received28 March 1996Revised15 August 1996Published online7 November 1996Published inissue 1 January 1996https://pubs.acs.org/doi/10.1021/cr950055xhttps://doi.org/10.1021/cr950055xresearch-articleACS PublicationsCopyright © 1996 American Chemical SocietyRequest reuse permissionsArticle Views14798Altmetric-Citations1567LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Cluster chemistry,FeMo cofactor,Metal organic frameworks,Peptides and proteins,Redox reactions Get e-Alerts
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
Cited by
Noble metal-free hydrogen evolution catalysts for water splitting
Zou, X., & Zhang, Y. (2015) · Chemical Society Reviews · doi:10.1039/c4cs00448e · Cited by 5,955
Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO 2 Fixation
Appel, A. M., Bercaw, J. E., Bocarsly, A. B., Dobbek, H., DuBois, D. L., Dupuis, M., Ferry, J. G., Fujita, E., Hille, R., Kenis, P. J. A., et al. (2013) · Chemical Reviews · doi:10.1021/cr300463y · Cited by 2,193
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
Proton-coupled electron transfer
Huynh, M. H. V., & Meyer, T. J. (2007) · Chemical Reviews · doi:10.1021/cr0500030 · Cited by 1,659
Quantum computational chemistry
McArdle, S., Endo, S., Aspuru-Guzik, A., Benjamin, S. C., & Yuan, X. (2020) · Reviews of Modern Physics · doi:10.1103/revmodphys.92.015003 · Cited by 1,621
The Mononuclear Molybdenum Enzymes
Hille, R. (1996) · Chemical Reviews · doi:10.1021/cr950061t · Cited by 1,501
A Review of Electrocatalytic Reduction of Dinitrogen to Ammonia under Ambient Conditions
Cui, X., Tang, C., & Zhang, Q. (2018) · Advanced Energy Materials · doi:10.1002/aenm.201800369 · Cited by 1,314
Molybdenum cofactors, enzymes and pathways
Schwarz, G., Mendel, R. R., & Ribbe, M. W. (2009) · Nature · doi:10.1038/nature08302 · Cited by 872
Wang, P., Chang, F., Gao, W., Guo, J., Wu, G., He, T., & Chen, P. (2017) · Nature Chemistry · doi:10.1038/nchem.2595 · Cited by 711
Nitrogen fixation and photosynthetic oxygen evolution in cyanobacteria
Berman-Frank, I., Lundgren, P., & Falkowski, P. (2003) · Research in Microbiology · doi:10.1016/s0923-2508(03)00029-9 · Cited by 522
Biomimetic Hydrogen Evolution Catalyzed by an Iron Carbonyl Thiolate
Gloaguen, F., Lawrence, J. D., & Rauchfuss, T. B. (2001) · Journal of the American Chemical Society · doi:10.1021/ja016516f · Cited by 441
Nitrogen Journey in Plants: From Uptake to Metabolism, Stress Response, and Microbe Interaction
Zayed, O., Hewedy, O. A., Abdelmoteleb, A., Ali, M., Youssef, M. S., Roumia, A. F., Seymour, D., & Yuan, Z.-C. (2023) · Biomolecules · doi:10.3390/biom13101443 · Cited by 412
Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase
Spatzal, T., Perez, K. A., Einsle, O., Howard, J. B., & Rees, D. C. (2014) · Science · doi:10.1126/science.1256679 · Cited by 401
Noodleman, L., Lovell, T., Han, W.-G., Li, J., & Himo, F. (2004) · Chemical Reviews · doi:10.1021/cr020625a · Cited by 373
Zhao, W., Zhang, L., Luo, Q., Hu, Z., Zhang, W., Smith, S., & Yang, J. (2019) · ACS Catalysis · doi:10.1021/acscatal.8b05061 · Cited by 336
Johnson, M. K., Rees, D. C., & Adams, M. W. W. (1996) · Chemical Reviews · doi:10.1021/cr950063d · Cited by 322
Iron-only hydrogenase: Synthetic, structural and reactivity studies of model compounds
LIU, X., IBRAHIM, S., TARD, C., & PICKETT, C. (2005) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2005.04.009 · Cited by 264
Biogeochemical signatures through time as inferred from whole microbial genomes
Zerkle, A. L. (2005) · American Journal of Science · doi:10.2475/ajs.305.6-8.467 · Cited by 223
Great Metalloclusters in Enzymology
Rees, D. C. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135406 · Cited by 220
Face the Edges: Catalytic Active Sites of Nanomaterials
Ni, B., & Wang, X. (2015) · Advanced Science · doi:10.1002/advs.201500085 · Cited by 219
The involvement of molybdenum in life
Williams, R. J. P., & Fraústo da Silva, J. J. R. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6518 · Cited by 181
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
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
Nitrous Oxide Metabolism in Nitrate-Reducing Bacteria
(2016) · Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2016.02.007 · Cited by 100
Nitrogenase Bioelectrochemistry for Synthesis Applications
Milton, R. D., & Minteer, S. D. (2019) · Accounts of Chemical Research · doi:10.1021/acs.accounts.9b00494 · Cited by 92
Nitrogenases—a tale of carbon atom(s)
Hu, Y., & Ribbe, M. W. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201600010 · Cited by 67
Structural insights into the iron nitrogenase complex
Schmidt, F. V., Schulz, L., Zarzycki, J., Prinz, S., Oehlmann, N. N., Erb, T. J., & Rebelein, J. G. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01124-2 · Cited by 56
On the evolution of coenzyme biosynthesis
Kirschning, A. (2022) · Natural Product Reports · doi:10.1039/d2np00037g · Cited by 37
Radical AdoMet enzymes in complex metal cluster biosynthesis
Duffus, B. R., Hamilton, T. L., Shepard, E. M., Boyd, E. S., Peters, J. W., & Broderick, J. B. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.01.002 · Cited by 26
Metadata
- Authors
- Burgess, B. K., & Lowe, D. J.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 1996-01-01
- Volume
- 96
- Issue
- 7
- Pages
- 2983-3012
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2061407935
- Cited by
- 1,854
- References
- 0
- FWCI
- 2.20
- Type
- journal article
- Language
- en
- Open access
- closed
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
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.
