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The Mononuclear Molybdenum Enzymes
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ADVERTISEMENT RETURN TO ISSUEPREVReviewThe Mononuclear Molybdenum EnzymesRuss Hille*†, James Hall†, and Partha Basu*‡View Author Information† Department of Biochemistry, University of California, Riverside, Riverside, California 92521, United States‡ Department of Chemistry and Biochemistry, Duquesne University, Pittsburgh, Pennsylvania 15282, United States*E-mail: [email protected]*E-mail: [email protected]Cite this: Chem. Rev. 2014, 114, 7, 3963–4038Publication Date (Web):January 28, 2014Publication History Received13 August 2013Published online28 January 2014Published inissue 9 April 2014https://pubs.acs.org/doi/10.1021/cr400443zhttps://doi.org/10.1021/cr400443zreview-articleACS PublicationsCopyright © 2014 American Chemical SocietyRequest reuse permissionsArticle Views10413Altmetric-Citations493LEARN 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,Cluster chemistry,Molybdenum,Monomers,Peptides and proteins Get e-Alerts
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“Indeed, the expression and activation of bacterial nitrate reductases are tightly regulated via oxygen-dependent and nitrate-responsive mechanisms[77,256].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [256]
In the citing paper
“Conversely, NarZYW is constitutively expressed at low levels in the aerobic setting and only up-regulated in response to high nitrate concentrations, likely aiding in the transition from aerobic to anaerobic respiration [256,259,260].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [256]
In the citing paper
“Comparatively, while the DNRA nitrate reductase, nap, shares some regulatory elements with nar such as the oxygen-dependent FNR[77,256,261–264]”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [256]
In the citing paper
“The first, NarGHI, is highly oxygen-responsive, under primary transcriptional control via the oxygen sensor fumarate nitrate reductase regulator (FNR), and appears to be the major contributor to respiratory anaerobic activity[256–258].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [256]
In the citing paper
“For instance, the respiratory nitrate reductase, nar, expresses two major operons, NarGHI and NarZYW[77,256].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [256]
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Metadata
- Authors
- Hille, R., Hall, J., & Basu, P.
- Affiliations
- University of California, Riverside (US)
- Duquesne University (US)
- Corresponding author
- Hille, Russ
- Basu, Partha
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-01-28
- Volume
- 114
- Issue
- 7
- Pages
- 3963-4038
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- PMC
- PMC4080432
- OpenAlex
- W2045245826
- Cited by
- 1,738
- References
- 1,038
- Citations by year
- 2026: 41 · 2025: 55 · 2024: 64 · 2023: 65 · 2022: 63 · 2021: 79 · 2020: 72 · 2019: 65 · 2018: 70 · 2017: 69 · 2016: 77 · 2015: 72 · 2014: 80
- FWCI
- 3.75
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Chemical Reviews (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R15GM061555)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- molybdenum enzymes, molybdenum clusters, molybdenum cofactor, enzyme active site, metalloproteins, metalloenzymes
- MeSH terms
- Aldehyde Oxidoreductases, Formate Dehydrogenases, Iron-Sulfur Proteins, Molybdenum, Nitrate Reductases, Oxidoreductases, Xanthine Oxidase, Protein Structure, Tertiary, Sulfite Oxidase, Biocatalysis
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