ReviewChemical Society reviews2014
Nitrate and periplasmic nitrate reductases.
Review in Chemical Society reviews, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
139 citing papers in PubMed, 391 citations in OpenAlex.
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- Structure and function of periplasmic nitrate reductase.Biochemical Society transactions · 2026Review
- A parsimonious preoperative prediction model for postoperative sepsis following upper urinary tract calculi surgery.Urolithiasis · 2026Article
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- Gut Microbial Nitrate Reduction to Ammonia: A Possible Pathway of Biological Nitrogen Provisioning in Freshwater Insects.Microbial ecology · 2026Article
- Bioremediation of enrofloxacin and modulation of nitrogen cycling in a simulated aquaculture system by the fungus Cladosporium cladosporioides 11.World journal of microbiology & biotechnology · 2026Article
- Nitrogen metabolic characteristics and adaptive mechanisms of Paracoccus sp. QD-21 under complex nitrogenous environments.Biodegradation · 2026Article
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- Structure and substrate promiscuity of Campylobacter jejuni periplasmic nitrate reductase (Nap) and phylogenetic analysis of Nap homologs.The Journal of biological chemistry · 2025Article
- Flavomycin inhibits plasmid-mediated conjugative transfer of antibiotic resistance genes by disrupting energy metabolism and pilus assembly.Zoological research · 2025Article
- Red seaweed supplementation suppresses methanogenesis in the rumen, revealing potentially advantageous traits among hydrogenotrophic bacteria.Microbiome · 2025Article
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- Influence of a 7 T magnetic field on growth, biomineralization, and denitrification metabolism inApplied and environmental microbiology · 2025Article
79 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The nitrate anion is a simple, abundant and relatively stable species, yet plays a significant role in global cycling of nitrogen, global climate change, and human health. Although it has been known for quite some time that nitrate is an important species environmentally, recent studies have identified potential medical applications. In this respect the nitrate anion remains an enigmatic species that promises to offer exciting science in years to come. Many bacteria readily reduce nitrate to nitrite via nitrate reductases. Classified into three distinct types--periplasmic nitrate reductase (Nap), respiratory nitrate reductase (Nar) and assimilatory nitrate reductase (Nas), they are defined by their cellular location, operon organization and active site structure. Of these, Nap proteins are the focus of this review. Despite similarities in the catalytic and spectroscopic properties Nap from different Proteobacteria are phylogenetically distinct. This review has two major sections: in the first section, nitrate in the nitrogen cycle and human health, taxonomy of nitrate reductases, assimilatory and dissimilatory nitrate reduction, cellular locations of nitrate reductases, structural and redox chemistry are discussed. The second section focuses on the features of periplasmic nitrate reductase where the catalytic subunit of the Nap and its kinetic properties, auxiliary Nap proteins, operon structure and phylogenetic relationships are discussed.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.