Cited by 877Metalloenzymes and iron-sulfur proteinsLegume Nitrogen Fixing SymbiosisAmmonia Synthesis and Nitrogen Reduction

Structure–function relationships of alternative nitrogenases

Eady, Robert R.·1996·Chemical Reviews

Abstract

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructure−Function Relationships of Alternative NitrogenasesRobert R. EadyView Author Information Nitrogen Fixation Laboratory, John Innes Institute, Colney Lane Norwich NR4 7UH U.K.Cite this: Chem. Rev. 1996, 96, 7, 3013–3030Publication Date (Web):November 7, 1996Publication History Received17 April 1996Revised23 August 1996Published online7 November 1996Published inissue 1 January 1996https://pubs.acs.org/doi/10.1021/cr950057hhttps://doi.org/10.1021/cr950057hresearch-articleACS PublicationsCopyright © 1996 American Chemical SocietyRequest reuse permissionsArticle Views6104Altmetric-Citations708LEARN 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

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  • Because nitrogenases with a Mo-Fe cofactor are more efficient than Fe-Fe and V-Fe versions, low Mo concentrations would have negatively impacted primary producers' ability to fix N2.

    “As nitrogenases containing a Mo-Fe metal cofactor are more efficient than alternative Fe-Fe and V-Fe versions (Eady, 1996), low Mo concentrations would have negatively impacted the ability of primary producers to fix N2.”
  • V-Fe nitrogenase varieties might have contributed to nitrogen fixation during the Paleoproterozoic, although the V variety is less efficient.

    “Both Anbar and Knoll (2002) and Zhang et al. (2014) suggested that the V-Fe nitrogenase varieties might have contributed to nitrogen fixation during the Paleoproterozoic, although the V variety is less efficient (Eady, 1996).”

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Authors
Eady, R. R.
Affiliations
John Innes Centre (GB)
Corresponding author
Eady, Robert R.
Venue
Chemical Reviews
Published
1996-01-01
Volume
96
Issue
7
Pages
3013-3030
ISSN
  • 0009-2665 (ISSN-L)
  • 1520-6890
OpenAlex
W2011994941
Cited by
877
References
100
Citations by year
2026: 22 · 2025: 27 · 2024: 30 · 2023: 35 · 2022: 38 · 2021: 52 · 2020: 61 · 2019: 50 · 2018: 50 · 2017: 36 · 2016: 29 · 2015: 32 · 2014: 35 · 2013: 36 · 2012: 19
FWCI
0.70
Type
journal article
Language
en
Open access
closed
Locations
  • Chemical Reviews (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Legume Nitrogen Fixing Symbiosis
  • Physical Sciences › Chemical Engineering › Catalysis › Ammonia Synthesis and Nitrogen Reduction
Keywords
alternative nitrogenases, nitrogen fixation, structure-function relationship, FeMo cofactor, nitrogenase active site, metalloenzyme active site, nitrogenase reconstitution

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