Regulation of nap Gene Expression and Periplasmic Nitrate Reductase Activity in the Phototrophic Bacterium Rhodobacter sphaeroides DSM158

Gavira, Mónica; Roldán, M. Dolores; Castillo, Francisco; Moreno-Vivián, Conrado

doi:10.1128/jb.184.6.1693-1702.2002

Cited by 55Bacterial Genetics and BiotechnologyWastewater Treatment and Nitrogen RemovalMetalloenzymes and iron-sulfur proteins

Regulation of nap Gene Expression and Periplasmic Nitrate Reductase Activity in the Phototrophic Bacterium Rhodobacter sphaeroides DSM158

Open access

Gavira, Mónica, Roldán, M. Dolores, Castillo, Francisco, Moreno-Vivián, Conrado·2002·Journal of Bacteriology

DOI 10.1128/jb.184.6.1693-1702.2002PMC PMC134877

Open this paper in CoChat — free account

Abstract

Bacterial periplasmic nitrate reductases (Nap) can play different physiological roles and are expressed under different conditions depending on the organism. Rhodobacter sphaeroides DSM158 has a Nap system, encoded by the napKEFDABC gene cluster, but nitrite formed is not further reduced because this strain lacks nitrite reductase. Nap activity increases in the presence of nitrate and oxygen but is unaffected by ammonium. Reverse transcription-PCR and Northern blots demonstrated that the napKEFDABC genes constitute an operon transcribed as a single 5.5-kb product. Northern blots and nap-lacZ fusions revealed that nap expression is threefold higher under aerobic conditions but is regulated by neither nitrate nor ammonium, although it is weakly induced by nitrite. On the other hand, nitrate but not nitrite causes a rapid enzyme activation, explaining the higher Nap activity found in nitrate-grown cells. Translational nap'-'lacZ fusions reveal that the napK and napD genes are not efficiently translated, probably due to mRNA secondary structures occluding the translation initiation sites of these genes. Neither butyrate nor caproate increases nap expression, although cells growing phototrophically on these reduced substrates show a very high Nap activity in vivo (nitrite accumulation is sevenfold higher than in medium with malate). Phototrophic growth on butyrate or caproate medium is severely reduced in the NapA(-) mutants. Taken together, these results indicate that nitrate reduction in R. sphaeroides is mainly regulated at the level of enzyme activity by both nitrate and electron supply and confirm that the Nap system is involved in redox balancing using nitrate as an ancillary oxidant to dissipate excess reductant.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1128/jb.184.6.1693-1702.2002

Cites

44 of 44 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The DNRA nitrate reductase nap shares some regulatory elements with nar such as the oxygen-dependent FNR.
“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 [264]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572 · see citing works
Experiments in molecular genetics
Miller, J. H. (1972) · Medical Entomology and Zoology · Cited by 27,157 · see citing works
A Broad Host Range Mobilization System for In Vivo Genetic Engineering: Transposon Mutagenesis in Gram Negative Bacteria
Simon, R., Priefer, U. B., & Pühler, A. (1983) · Nature Biotechnology · doi:10.1038/nbt1183-784 · Cited by 7,342 · see citing works
The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
Vieira, J., & Messing, J. W. (1982) · Gene · doi:10.1016/0378-1119(82)90015-4 · Cited by 6,127 · see citing works
Anoxygenic Photosynthetic Bacteria
Blankenship, R. E., Bauer, C. E., & Madigan, M. T. (1995) · Advances in photosynthesis and respiration · doi:10.1007/0-306-47954-0 · Cited by 1,912 · see citing works
Colorimetric Methods of Analyses
Snell, F. D., & Snell, C. T. (1950) · Soil Science · doi:10.1097/00010694-195002000-00009 · Cited by 1,415 · see citing works
Prokaryotic Nitrate Reduction: Molecular Properties and Functional Distinction among Bacterial Nitrate Reductases
Moreno‐Vivián, C., Cabello, P., Martínez‐Luque, M., Blasco, R., & del Castillo, F. J. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.21.6573-6584.1999 · Cited by 593 · see citing works
Self-citation
Reverse transcription and DNA amplification by a Thermus thermophilus DNA polymerase
Myers, T. W., & Gelfand, D. H. (1991) · Biochemistry · doi:10.1021/bi00245a001 · Cited by 471 · see citing works
Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods
Dias, J. M., Than, M. E., Humm, A., Huber, R., Bourenkov, G. P., Bartunik, H. D., Bursakov, S., Calvete, J., Caldeira, J., Carneiro, C., et al. (1999) · Structure · doi:10.1016/s0969-2126(99)80010-0 · Cited by 286 · see citing works
A new family of RSF1010-derived expression and lac-fusion broad-host-range vectors for Gram-negative bacteria
Labes, M., Pühler, A., & Simon, R. (1990) · Gene · doi:10.1016/0378-1119(90)90203-4 · Cited by 243 · see citing works
Periplasmic and membrane‐bound respiratory nitrate reductases in Thiosphaera pantotropha
Bell, L. C., Richardson, D. J., & Ferguson, S. J. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80889-q · Cited by 241 · see citing works
Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16
Siddiqui, R. A., Warnecke‐Eberz, U., Hengsberger, A., Schneider, B., Kostka, S., & Friedrich, B. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.18.5867-5876.1993 · Cited by 175 · see citing works
Expression of regulatory nif genes in Rhodobacter capsulatus
Hübner, P., Willison, J. C., Vignais, P. M., et al. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.9.2993-2999.1991 · Cited by 162 · see citing works
Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: does Nap confer a selective advantage during nitrate-limited growth?
POTTER, L. C., MILLINGTON, P., GRIFFITHS, L., THOMAS, G. H., & COLE, J. A. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440077 · Cited by 160 · see citing works
Escherichia coli K‐12 genes essential for the synthesis of c‐type cytochromes and a third nitrate reductase located in the periplasm
Grove, J. I., Tanapongpipat, S., Thomas, G. H., Griffiths, L., Crooke, H., & Cole, J. A. (1996) · Molecular Microbiology · doi:10.1046/j.1365-2958.1996.383914.x · Cited by 153 · see citing works
The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha
Berks, B. C., Richardson, D. J., Reilly, A., Willis, A. C., & Ferguson, S. J. (1995) · Biochemical Journal · doi:10.1042/bj3090983 · Cited by 138 · see citing works
The napF and narG Nitrate Reductase Operons in Escherichia coli Are Differentially Expressed in Response to Submicromolar Concentrations of Nitrate but Not Nitrite
Wang, H., Tseng, C., & Gunsalus, R. P. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.17.5303-5308.1999 · Cited by 137 · see citing works
The Periplasmic Nitrate Reductase in Pseudomonas sp. Strain G-179 Catalyzes the First Step of Denitrification
Bedzyk, L. A., Wang, T., & Ye, R. W. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.9.2802-2806.1999 · Cited by 127 · see citing works
Spectroscopic Characterization of a Novel Multihemec-Type Cytochrome Widely Implicated in Bacterial Electron Transport
Roldán, M. D., Sears, H. J., Cheesman, M. R., Ferguson, S. J., THOMSON, A. J., Berks, B. C., & Richardson, D. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.44.28785 · Cited by 124 · see citing works
A family of high-copy-number plasmid vectors with single end-label sites for rapid nucleotide sequencing
Arnold, W., & Pühler, A. (1988) · Gene · doi:10.1016/0378-1119(88)90115-1 · Cited by 112 · see citing works
The role of auxiliary oxidants in maintaining redox balance during phototrophic growth of Rhodobacter capsulatus on propionate or butyrate
Richardson, D. J., King, G. F., Kelly, D. J., McEwan, A. G., Ferguson, S. J., & JACKSON, J. B. (1988) · Archives of Microbiology · doi:10.1007/bf00425152 · Cited by 105 · see citing works
The influence of carbon substrate on the activity of the periplasmic nitrate reductase in aerobically grown Thiosphaera pantotropha
Richardson, D. J., & Ferguson, S. J. (1992) · Archives of Microbiology · doi:10.1007/bf00276774 · Cited by 97 · see citing works
Detection of genes for periplasmic nitrate reductase in nitrate respiring bacteria and in community DNA
Flanagan, D., Gregory, L. G., Carter, J. P., Karakas-Sen, A., Richardson, D. J., & Spiro, S. (1999) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1999.tb13742.x · Cited by 97 · see citing works
Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: structural and functional differences among prokaryotic nitrate reductases
Reyes, F., Roldán, M. D., Klipp, W., del Castillo, F. J., & Moreno‐Vivián, C. (1996) · Molecular Microbiology · doi:10.1111/j.1365-2958.1996.tb02475.x · Cited by 95 · see citing works
Self-citation
Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12
POTTER, L. C., & COLE, J. A. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440069 · Cited by 93 · see citing works
Control of periplasmic nitrate reductase gene expression (napEDABC) from Paracoccus pantotrophus in response to oxygen and carbon substrates
Sears, H. J., Sawers, G., Berks, B. C., Ferguson, S. J., & Richardson, D. J. (2000) · Microbiology · doi:10.1099/00221287-146-11-2977 · Cited by 76 · see citing works
Open reading frame 5 (ORF5), encoding a ferredoxinlike protein, and nifQ are cotranscribed with nifE, nifN, nifX, and ORF4 in Rhodobacter capsulatus
Moreno‐Vivián, C., Hennecke, S., Pühler, A., & Klipp, W. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.5.2591-2598.1989 · Cited by 75 · see citing works
Promoters controlling expression of the alternative nitrogenase and the molybdenum uptake system in Rhodobacter capsulatus are activated by NtrC, independent of sigma54, and repressed by molybdenum
Kutsche, M., Leimkühler, S., Angermüller, S., et al. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.7.2010-2017.1996 · Cited by 73 · see citing works
Structure and Sequence of the Photosynthesis Gene Cluster
Alberti, M., Burke, D. H., & Hearst, J. E. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-47954-0_50 · Cited by 72 · see citing works
DNA sequence and genetic analysis of the Rhodobacter capsulatus nifENX gene region: Homology between NifX and NifB suggests involvement of NifX in processing of the iron-molybdenum cofactor
Moreno‐Vivián, C., Schmehl, M., Masepohl, B., Arnold, W., & Klipp, W. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00334376 · Cited by 68 · see citing works
Fnr, NarP, and NarL Regulation of Escherichia coli K-12 napF (Periplasmic Nitrate Reductase) Operon Transcription In Vitro
Darwin, A. J., Ziegelhoffer, E. C., Kiley, P. J., & Stewart, V. J. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.16.4192-4198.1998 · Cited by 68 · see citing works
Chlorate and nitrate reduction in the phototrophic bacteriaRhodobacter capsulatus andRhodobacter sphaeroides
Roldán, M. D., Reyes, F., Moreno‐Vivián, C., et al. (1994) · Current Microbiology · doi:10.1007/bf01570161 · Cited by 65 · see citing works
Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12
POTTER, L. C., & Cole, J. A. (1999) · Biochemical Journal · doi:10.1042/bj3440069 · Cited by 63 · see citing works
Periplasmic nitrate-reducing system of the phototrophic bacterium Rhodobacter sphaeroides DSM 158: transcriptional and mutational analysis of the napKEFDABC gene cluster
REYES, F., GAVIRA, M., CASTILLO, F., & MORENO-VIVIÁN, C. (1998) · Biochemical Journal · doi:10.1042/bj3310897 · Cited by 56 · see citing works
Self-citation
Effect of carbon substrate and aeration on nitrate reduction and expression of the periplasmic and membrane-bound nitrate reductases in carbon-limited continuous cultures of Paracoccus denitrificans Pd1222
Sears, H. J., Spiro, S. G., & Richardson, D. J. (1997) · Microbiology · doi:10.1099/00221287-143-12-3767 · Cited by 54 · see citing works
Involvement in Denitrification of thenapKEFDABCGenes Encoding the Periplasmic Nitrate Reductase System in the Denitrifying Phototrophic BacteriumRhodobacter sphaeroidesf. sp.denitrificans
Hui-Ping, L. I. U., Takio, S., Satoh, T., & Yamamoto, I. (1999) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.63.530 · Cited by 37 · see citing works
Nitrate reductase from Rhodopseudomonas sphaeroides
Kerber, N. L., & Cárdenas, J. (1982) · Journal of Bacteriology · doi:10.1128/jb.150.3.1091-1097.1982 · Cited by 23 · see citing works
Nitrite uptake system in photosynthetic bacterium Rhodopseudomonas capsulata E1F1
Caballero, F. J., Moreno‐Vivián, C., Castillo, F. J., et al. (1986) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(86)90155-6 · Cited by 23 · see citing works
Self-citation
Overproduction, purification and novel redox properties of the dihaem cytochrome c, NapB, from Haemophilus influenzae
BRIGÉ, A., COLE, J. A., HAGEN, W. R., GUISEZ, Y., & Van BEEUMEN, J. J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560851 · Cited by 23 · see citing works
In vivo short-term inhibition of nitrogenase by nitrate inRhodopseudomonas capsulataE1F1
Moreno‐Vivián, C., CÃ¡rdenas, J., & del Castillo, F. J. (1986) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1986.tb01358.x · Cited by 18 · see citing works
Self-citation
Effect of carbon and nitrogen metabolism on nitrate reductase activity of Rhodobacter capsulatus E1F1
Dobao, M. M., Martínez‐Luque, M., Moreno‐Vivián, C., et al. (1994) · Canadian Journal of Microbiology · doi:10.1139/m94-102 · Cited by 15 · see citing works
Overproduction, purification and novel redox properties of the dihaem cytochrome c, NapB, from Haemophilus influenzae
Brigé, A., Cole, J. A., Hagen, W. R., et al. (2001) · Biochemical Journal · doi:10.1042/bj3560851 · Cited by 15 · see citing works
Isolation and characterization of transposon Tn5 mutants ofRhodobacter sphaeroidesdeficient in both nitrate and chlorate reduction.
Moreno‐Vivián, C., RoldÃ¡n, M. D., Reyes, F., et al. (1994) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1994.tb06651.x · Cited by 9 · see citing works

Flagged first, then by citations

Research works printed but not linked: 4

[20]Moreno-Vivián, C., J. Cárdenas, and F. Castillo. 1986. In vivo short-term regulation of nitrogenase by nitrate in Rhodopseudomonas capsulata E1F1. FEMS Microbiol. Lett. 34:105-109. [Google Scholar]
[23]Moreno-Vivián, C., M. D. Roldán, F. Reyes, and F. Castillo. 1994. Isolation and characterization of transposon Tn 5 mutants of Rhodobacter sphaeroides deficient in both nitrate and chlorate reduction. FEMS Microbiol. Lett. 115:279-284. [Google Scholar]
[34]Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
[40]Snell, F. D., and C. T. Snell. 1949. Colorimetric methods of analysis, 3rd ed., vol. 2, p. 804-805. D. van Nostrand Reinhold, New York, N.Y.

Sorted by citations

The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738 · see citing works
Nitrate and periplasmic nitrate reductases
Sparacino-Watkins, C., Stolz, J. F., & Basu, P. (2014) · Chem. Soc. Rev. · doi:10.1039/c3cs60249d · Cited by 426 · see citing works
Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health
Koch, C. D., Gladwin, M. T., Freeman, B. A., Lundberg, J. O., Weitzberg, E., & Morris, A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.015 · Cited by 186 · see citing works
The Periplasmic Nitrate Reductase Nap Is Required for Anaerobic Growth and Involved in Redox Control of Magnetite Biomineralization in Magnetospirillum gryphiswaldense
Li, Y., Katzmann, E., Borg, S., & Schüler, D. (2012) · Journal of Bacteriology · doi:10.1128/jb.00903-12 · Cited by 117 · see citing works
EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774
González, P. J., Rivas, M. G., Brondino, C. D., Bursakov, S. A., Moura, I., & Moura, J. J. G. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0110-0 · Cited by 45 · see citing works
NapF Is a Cytoplasmic Iron-Sulfur Protein Required for Fe-S Cluster Assembly in the Periplasmic Nitrate Reductase
Olmo-Mira, M. F., Gavira, M., Richardson, D. J., Castillo, F., Moreno-Vivián, C., & Roldán, M. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406502200 · Cited by 44 · see citing works
Self-citation

On the role of the light‐harvesting B880 in the correct insertion of the reaction center of Rhodobacter capsulatus and Rhodobacter sphaeroides
Jackson, W. J., Kiley, P. J., Haith, C. E., et al. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80135-7 · Cited by 22 · see citing works
Complete Genome Sequence of Rhodobacter sphaeroides Strain HJ, a Purple Nonsulfur Bacterium with the Ability To Produce High Levels of Hydrogen from Acetate
Kobayashi, J., & Kondo, A. (2019) · Microbiology Resource Announcements · doi:10.1128/mra.00652-19 · Cited by 1 · see citing works
Complete Genome Sequence of Rhodobacter sphaeroides KD131
Lim, S., Kim, S. J., Cha, S. H., Oh, Y., Rhee, H.-J., Kim, M.-S., & Lee, J. K. (2008) · Journal of Bacteriology · doi:10.1128/jb.01565-08 · Cited by 29 · see citing works
Methylation-independent and methylation-dependent chemotaxis in Rhodobacter sphaeroides and Rhodospirillum rubrum
Sockett, R. E., Armitage, J. P., & Evans, M. C. W. (1987) · Journal of Bacteriology · doi:10.1128/jb.169.12.5808-5814.1987 · Cited by 37 · see citing works
Accumulation of poly-(hydroxybutyrate) by a non-sulfur photosynthetic bacterium, Rhodobacter sphaeroides RV at different pH
Suzuki, T., Tsygankov, A. A., Miyake, J., et al. (1995) · Biotechnology Letters · doi:10.1007/bf00130796 · Cited by 40 · see citing works

Authors: Gavira, M., Roldán, M. D., Castillo, F., & Moreno-Vivián, C.
Affiliations: Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Campus Universitario de Rabanales, Universidad de Córdoba, 14071 Córdoba, Spain
University of Córdoba (ES)
ORCID: Castillo, Francisco
Venue: Journal of Bacteriology
Publisher: American Society for Microbiology
Published: 2002-03-15
Volume: 184
Issue: 6
Pages: 1693-1702
ISSN: 0021-9193 (ISSN-L)
1098-5530
DOI: 10.1128/jb.184.6.1693-1702.2002
PMC: PMC134877
OpenAlex: W2101848131
Cited by: 55
References: 44
Citations by year: 2025: 2 · 2023: 1 · 2022: 1 · 2020: 2 · 2018: 3 · 2017: 1 · 2016: 4 · 2015: 2 · 2014: 1 · 2013: 6 · 2012: 3
FWCI: 1.77
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Bacteriology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Physical Sciences › Environmental Science › Pollution › Wastewater Treatment and Nitrogen Removal
Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Keywords: periplasmic nitrate reductase, napA, Rhodobacter sphaeroides, gene expression regulation, nitrate reduction, nitrite accumulation, aerobic conditions, mRNA secondary structure, translation initiation, butyrate, caproate, phototrophic growth, redox balancing, enzyme activation
MeSH terms: Quaternary Ammonium Compounds, Dose-Response Relationship, Drug, Enzyme Activation, Genes, Bacterial, Multigene Family, Nitrate Reductases, Nitrates, Nitrites, Plant Proteins, Recombinant Fusion Proteins, Rhodobacter sphaeroides, Transcription, Genetic, Protein Biosynthesis, Gene Expression Regulation, Bacterial, Periplasm, Arabidopsis Proteins, Nitrate Reductase

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Regulation of nap Gene Expression and Periplasmic Nitrate Reductase Activity in the Phototrophic Bacterium Rhodobacter sphaeroides DSM158

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks