The Mononuclear Molybdenum Enzymes
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThe Mononuclear Molybdenum Enzymes†Russ HilleView Author Information Department of Medical Biochemistry, The Ohio State University, Columbus, Ohio 43210-1218 Cite this: Chem. Rev. 1996, 96, 7, 2757–2816Publication Date (Web):November 7, 1996Publication History Received28 March 1996Revised7 August 1996Published online7 November 1996Published inissue 1 January 1996https://pubs.acs.org/doi/10.1021/cr950061thttps://doi.org/10.1021/cr950061tresearch-articleACS PublicationsCopyright © 1996 American Chemical SocietyRequest reuse permissionsArticle Views6503Altmetric-Citations1396LEARN 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:Anions,Electron paramagnetic resonance spectroscopy,Molybdenum,Peptides and proteins,Redox reactions Get e-Alerts
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Dissimilatory NRs Nar and Nap, as well as prokaryotic assimilatory nitrate reductase (Nas), belong to the DMSOR family.
“Dissimilatory NRs, Nar and Nap, as well as prokaryotic assimilatory nitrate reductase (Nas) belong to the DMSOR family.”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [113]
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Reassessing the Strategies for Trapping Catalytic Intermediates during Nitrate Reductase Turnover
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- Authors
- Hille, R.
- Affiliations
- The Ohio State University (US)
- Corresponding author
- Hille, Russ
- ORCID
- Hille, Russ
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 1996-01-01
- Volume
- 96
- Issue
- 7
- Pages
- 2757-2816
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W4245399940
- Cited by
- 1,501
- References
- 413
- Citations by year
- 2026: 14 · 2025: 19 · 2024: 30 · 2023: 33 · 2022: 26 · 2021: 27 · 2020: 30 · 2019: 27 · 2018: 40 · 2017: 39 · 2016: 49 · 2015: 50 · 2014: 70 · 2013: 55 · 2012: 59
- FWCI
- 2.83
- 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
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- molybdenum enzymes, molybdenum cofactor, enzyme active site, electron spin resonance, redox reactions, negative ions, metalloproteins
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