ArticleThe Biochemical journal2004
NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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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.
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Who cites it
30 citing papers in PubMed, 85 citations in OpenAlex.
- A Cytochrome c-Containing Periplasmic Nitrate Reductase in the Acetogen Sporomusa ovata.Environmental microbiology · 2026Article
- Review
- Bacterial periplasmic nitrate and trimethylamine-N-oxide respiration coupled to menaquinol-cytochrome c reductase (Qcr): Implications for electrogenic reduction of alternative electron acceptors.Scientific reports · 2018Article
- Pressure-Regulated Gene Expression and Enzymatic Activity of the Two Periplasmic Nitrate Reductases in the Deep-Sea BacteriumFrontiers in microbiology · 2018Article
- All three quinone species play distinct roles in ensuring optimal growth under aerobic and fermentative conditions in E. coli K12.PloS one · 2018Article
- Transcriptomic profiles of Clostridium ljungdahlii during lithotrophic growth with syngas or HScientific reports · 2017Article
- Article
- CydDC-mediated reductant export in Escherichia coli controls the transcriptional wiring of energy metabolism and combats nitrosative stress.The Biochemical journal · 2016Article
- Proteomics of the organohalide-respiring Epsilonproteobacterium Sulfurospirillum multivorans adapted to tetrachloroethene and other energy substrates.Scientific reports · 2015Article
- The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.Biochimica et biophysica acta · 2015Review
- Identification of potential drug targets by subtractive genome analysis of Escherichia coli O157:H7: an in silico approach.Advances and applications in bioinformatics and chemistry : AABC · 2015Article
- A Metagenomics-Based Metabolic Model of Nitrate-Dependent Anaerobic Oxidation of Methane by Methanoperedens-Like Archaea.Frontiers in microbiology · 2015Article
- Assessment of the Carbon Monoxide Metabolism of the Hyperthermophilic Sulfate-Reducing Archaeon Archaeoglobus fulgidus VC-16 by Comparative Transcriptome Analyses.Archaea (Vancouver, B.C.) · 2015Article
- Inferring the relation between transcriptional and posttranscriptional regulation from expression compendia.BMC microbiology · 2014Article
- Nitrate and periplasmic nitrate reductases.Chemical Society reviews · 2014Review
- The MoxR ATPase RavA and its cofactor ViaA interact with the NADH:ubiquinone oxidoreductase I in Escherichia coli.PloS one · 2014Article
- Adaptive mutations and replacements of virulence traits in the Escherichia coli O104:H4 outbreak population.PloS one · 2013Article
- Bacterial adaptation of respiration from oxic to microoxic and anoxic conditions: redox control.Antioxidants & redox signaling · 2012Review
- Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide.Molecular microbiology · 2012Article
- Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB.Nature communications · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nap (periplasmic nitrate reductase) operons of many bacteria include four common, essential components, napD, napA, napB and napC (or a homologue of napC ). In Escherichia coli there are three additional genes, napF, napG and napH, none of which are essential for Nap activity. We now show that deletion of either napG or napH almost abolished Nap-dependent nitrate reduction by strains defective in naphthoquinone synthesis. The residual rate of nitrate reduction (approx. 1% of that of napG+ H+ strains) is sufficient to replace fumarate reduction in a redox-balancing role during growth by glucose fermentation. Western blotting combined with beta-galactosidase and alkaline phosphatase fusion experiments established that NapH is an integral membrane protein with four transmembrane helices. Both the N- and C-termini as well as the two non-haem iron-sulphur centres are located in the cytoplasm. An N-terminal twin arginine motif was shown to be essential for NapG function, consistent with the expectation that NapG is secreted into the periplasm by the twin arginine translocation pathway. A bacterial two-hybrid system was used to show that NapH interacts, presumably on the cytoplasmic side of, or within, the membrane, with NapC. As expected for a periplasmic protein, no NapG interactions with NapC or NapH were detected in the cytoplasm. An in vitro quinol dehydrogenase assay was developed to show that both NapG and NapH are essential for rapid electron transfer from menadiol to the terminal NapAB complex. These new in vivo and in vitro results establish that NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinone-ubiquinol couple via NapC and NapB to NapA.
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