Cited by 342Bacterial Genetics and BiotechnologyMetalloenzymes and iron-sulfur proteinsEnzyme Structure and Function

The DOI matches its Crossref record; 26 of the 27 references it cites were found in a registry or an index.

Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation: Roles of NapF, G and H in ubiquinol oxidation in E. coli

Open access

Brondijk, T. H. C., Fiegen, D., Richardson, D. J., Cole, J. A.·2002·Molecular Microbiology

DOI 10.1046/j.1365-2958.2002.02875.x

Open this paper in CoChat — free account Open PDF

Abstract

The nap operon of Escherichia coli K-12, encoding a periplasmic nitrate reductase (Nap), encodes seven proteins. The catalytic complex in the periplasm, NapA-NapB, is assumed to receive electrons from the quinol pool via the membrane-bound cytochrome NapC. Like NapA, B and C, a fourth polypeptide, NapD, is also essential for Nap activity. However, none of the remaining three polypeptides, NapF, G and H, which are predicted to encode non-haem, iron-sulphur proteins, are essential for Nap activity, and their function is currently unknown. The relative rates of growth and electron transfer from physiological substrates to Nap have been investigated using strains defective in the two membrane-bound nitrate reductases, and also defective in either ubiquinone or menaquinone biosynthesis. The data reveal that Nap is coupled more effectively to menaquinol oxidation than to ubiquinol oxidation. Conversely, parallel experiments with a second set of mutants revealed that nitrate reductase A couples more effectively with ubiquinol than with menaquinol. Three further sets of strains were constructed with combinations of in frame deletions of ubiCA, menBC, napC, napF and napGH genes. NapF, NapG and NapH were shown to play no role in electron transfer from menaquinol to the NapAB complex but, in the Ubi+Men- background, deletion of napF, napGH or napFGH all resulted in total loss of nitrate-dependent growth. Electron transfer from ubiquinol to NapAB was totally dependent upon NapGH, but not on NapF. NapC was essential for electron transfer from both ubiquinol and menaquinol to NapAB. The results clearly established that NapG and H, but not NapF, are essential for electron transfer from ubiquinol to NapAB. The decreased yield of biomass resulting from loss of NapF in a Ubi+Men+ strain implicates NapF in an energy- conserving role coupled to the oxidation of ubiquinol. We propose that NapG and H form an energy- conserving quinol dehydrogenase functioning as either components of a proton pump or in a Q cycle, as electrons are transferred from ubiquinol to NapC.

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 · 10.1046/j.1365-2958.2002.02875.x

Cites

26 of 26 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?

Self-check

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

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

One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products.
Datsenko, K., & Wanner, B. (2000) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.120163297 · Cited by 15,902
New method for generating deletions and gene replacements in Escherichia coli
Hamilton, C. M., Aldea, M., Washburn, B. K., Babitzke, P., & Kushner, S. R. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.9.4617-4622.1989 · Cited by 678
Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
Berks, B. C., Ferguson, S. J., Moir, J. W. B., & Richardson, D. J. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00092-5 · Cited by 596
Self-citation
Bacterial respiration: a flexible process for a changing environment 1999 Fleming Lecture (Delivered at the 144th meeting of the Society for General Microbiology, 8 September 1999)
Richardson, D. J. (2000) · Microbiology · doi:10.1099/00221287-146-3-551 · Cited by 544
Self-citation
Functional, biochemical and genetic diversity of prokaryotic nitrate reductases
Richardson, D. J., Berks, B. C., Russell, D. A., Spiro, S., & Taylor, C. J. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000845 · Cited by 477
Self-citation
Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction of iron(III), fumarate, and nitrate by Shewanella putrefaciens MR-1
Myers, C. R., & Myers, J. M. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.4.1143-1152.1997 · Cited by 297
Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci
Stewart, V. J., & MacGregor, C. H. (1982) · Journal of Bacteriology · doi:10.1128/jb.151.2.788-799.1982 · Cited by 257
Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA− menA− double quinone mutant
Wallace, B., & Young, I. G. (1977) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(77)90071-8 · Cited by 235
Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management
Søballe, B., & Poole, R. K. (1999) · Microbiology · doi:10.1099/13500872-145-8-1817 · Cited by 226
Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12
Rabin, R. S., & Stewart, V. J. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.11.3259-3268.1993 · Cited by 223

Show all 27 references

Sorted by citations

Items 201–300 of 342

A highly conserved Sinorhizobium meliloti operon is induced microaerobically via the FixLJ system and by nitric oxide (NO) via NnrR
de Bruijn, F. J., Rossbach, S., Bruand, C., & Parrish, J. R. (2006) · Environmental Microbiology · doi:10.1111/j.1462-2920.2006.01030.x · Cited by 28
NifA is required for maximal expression of denitrification genes in Bradyrhizobium japonicum
Bueno, E., Mesa, S., Sánchez, C., Bedmar, E. J., & Delgado, M. J. (2009) · Environmental Microbiology · doi:10.1111/j.1462-2920.2009.02076.x · Cited by 28
Nitrification in Aquatic Systems
Ward, B. B. (2003) · Encyclopedia of Environmental Microbiology · doi:10.1002/0471263397.env287 · Cited by 28
Isolation of cold‐adapted nitrate‐reducing fungi that have potential to increase nitrate removal in woodchip bioreactors
Aldossari, N., & Ishii, S. (2020) · Journal of Applied Microbiology · doi:10.1111/jam.14939 · Cited by 27
NO 3 − removal efficiency in field denitrification beds: key controlling factors and main implications
Grießmeier, V., Leberecht, K., & Gescher, J. (2019) · Environmental Microbiology Reports · doi:10.1111/1758-2229.12758 · Cited by 27
Nitrate reductase from the magnetotactic bacteriumMagnetospirillum magnetotacticumMS-1: purification and sequence analyses
Taoka, A., Yoshimatsu, K., Kanemori, M., & Fukumori, Y. (2003) · Canadian Journal of Microbiology · doi:10.1139/w03-028 · Cited by 29
Detection of denitrification genes by in situ rolling circle amplification‐fluorescence in situ hybridization to link metabolic potential with identity inside bacterial cells
Hoshino, T., & Schramm, A. (2010) · Environmental Microbiology · doi:10.1111/j.1462-2920.2010.02224.x · Cited by 26
Characterization of the expression and activity of the periplasmic nitrate reductase of Paracoccus pantotrophus in chemostat cultures
Ellington, M. J., Sawers, R. G., Sears, H. J., Spiro, S., Richardson, D. J., & Ferguson, S. J. (2003) · Microbiology · doi:10.1099/mic.0.26277-0 · Cited by 26
Self-citation
Molybdopterin guanine dinucleotide cofactor in Synechococcus sp. nitrate reductase: identification of mobA and isolation of a putative moeB gene
Rubio, L. M., Flores, E., & Antonia Herrero, B. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01556-2 · Cited by 26
Iron‐ and aluminium‐induced depletion of molybdenum in acidic environments impedes the nitrogen cycle
Ge, X., Vaccaro, B. J., Thorgersen, M. P., Poole, F. L., Majumder, E. L. ‐., Zane, G. M., León, K. B. D., Lancaster, W. A., Moon, J., Paradis, C. J., et al. (2018) · Environmental Microbiology · doi:10.1111/1462-2920.14435 · Cited by 25
Post-translational flavinylation is associated with diverse extracytosolic redox functionalities throughout bacterial life
Méheust, R., Huang, S., Rivera‐Lugo, R., Banfield, J. F., & Light, S. H. (2021) · eLife · doi:10.7554/elife.66878 · Cited by 25
Menaquinone as Well as Ubiquinone as a Crucial Component in the Escherichia coli Respiratory Chain
Fujimoto, N., Kosaka, T., & Yam, M. (2012) · InTech eBooks · doi:10.5772/35809 · Cited by 25
A cytochrome c encoded by the nar operon is required for the synthesis of active respiratory nitrate reductase in Thermus thermophilus
Zafra, O., Ramı́rez, S., Castán, P., Moreno, R., Cava, F., Rapp, C. V., Caro, E., & Berenguer, J. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02953-8 · Cited by 25
Nitrate reduction to ammonium: a phylogenetic, physiological, and genetic aspects in Prokaryotes and eukaryotes
Kaviraj, M., Kumar, U., Snigdha, A., & Chatterjee, S. (2024) · Archives of Microbiology · doi:10.1007/s00203-024-04009-0 · Cited by 24
Microbial diversity and abundance vary along salinity, oxygen, and particle size gradients in the Chesapeake Bay
Cram, J. A., Hollins, A., McCarty, A. J., Martinez, G., Cui, M., Gomes, M. L., & Fuchsman, C. A. (2024) · Environmental Microbiology · doi:10.1111/1462-2920.16557 · Cited by 24
The nitrate‐sensing N as ST system regulates nitrous oxide reductase and periplasmic nitrate reductase in B radyrhizobium japonicum
Sánchez, C., Itakura, M., Okubo, T., Matsumoto, T., Yoshikawa, H., Gotoh, A., Hidaka, M., Uchida, T., & Minamisawa, K. (2014) · Environmental Microbiology · doi:10.1111/1462-2920.12546 · Cited by 24
Resource effects on denitrification are mediated by community composition in tidal freshwater wetlands soils
Morrissey, E. M., & Franklin, R. B. (2014) · Environmental Microbiology · doi:10.1111/1462-2920.12575 · Cited by 26
Investigation on the anaerobic propionate degradation by Escherichia coli K12
Simonte, F. M., Dötsch, A., Galego, L., Arraiano, C. M., & Gescher, J. (2016) · Molecular Microbiology · doi:10.1111/mmi.13541 · Cited by 25
Ecology of Denitrification in Soils and Plant-Associated Bacteria
Bedmar, E. J., Bueno, E., Galeote, D. C., de Torres, M. A. R. R., Delgado, M. J., & Mesa, S. (2013) · CRC Press eBooks · doi:10.1201/b15251-9 · Cited by 25
A denitrifying community associated with a major, marine nitrogen fixer
Coates, C. J., & Wyman, M. (2017) · Environmental Microbiology · doi:10.1111/1462-2920.14007 · Cited by 24
Nitrous Oxide Emissions from Open‐Lot Cattle Feedyards: A Review
Waldrip, H. M., Todd, R. W., Parker, D. B., Cole, N. A., Rotz, C. A., & Casey, K. D. (2016) · Journal of Environmental Quality · doi:10.2134/jeq2016.04.0140 · Cited by 25
Met144Ala mutation of the copper‐containing nitrite reductase from Alcaligenes xylosoxidans reverses the intramolecular electron transfer
Farver, O., Eady, R. R., Sawers, R. G., Prudêncio, M., & Pecht, I. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00171-1 · Cited by 24
Nitric Oxide Signaling by Plant‐Associated Bacteria
Cohen, M. F., Lamattina, L., & Yamasaki, H. (2009) · doi:10.1002/9783527629138.ch11 · Cited by 24
Microbial community of nitrogen cycle‐related genes in aquatic plant rhizospheres of Lake Liangzi in winter
Yin, X., Liu, G., Lei, P., Hua, Y., Wan, X., Zhou, W., Zhao, J., & Zhu, D. (2018) · Journal of Basic Microbiology · doi:10.1002/jobm.201800220 · Cited by 23
A comprehensive model of simultaneous denitrification and methanogenic fermentation processes
Tuğtaş, A. E., Tezel, U., & Pavlostathis, S. G. (2009) · Biotechnology and Bioengineering · doi:10.1002/bit.22443 · Cited by 22
Diverse nitrogen cycling pathways across a marine oxygen gradient indicate nitrogen loss coupled to chemoautotrophic activity
Suter, E. A., Pachiadaki, M., Montes, E., Edgcomb, V. P., Scranton, M. I., Taylor, C. D., & Taylor, G. T. (2020) · Environmental Microbiology · doi:10.1111/1462-2920.15187 · Cited by 22
nir gene‐based co‐occurrence patterns reveal assembly mechanisms of soil denitrifiers in response to fire
Goberna, M., Donat, S., Pérez‐Valera, E., Hallin, S., & Verdú, M. (2020) · Environmental Microbiology · doi:10.1111/1462-2920.15298 · Cited by 22
Identification and functional analysis of a nitrate assimilation operon nasACKBDEF from Amycolatopsis mediterranei U32
Shao, Z., Gao, J., Ding, X., Wang, J., Chiao, J., & Zhao, G. (2011) · Archives of Microbiology · doi:10.1007/s00203-011-0690-0 · Cited by 22
Elucidation of Electron‐ Transfer Pathways in Copper and Iron Proteins by Pulse Radiolysis Experiments
Farver, O., & Pecht, I. (2007) · Progress in inorganic chemistry · doi:10.1002/9780470144428.ch1 · Cited by 22
A respiratory nitrate reductase active exclusively in resting spores of the obligate aerobe S treptomyces coelicolor A 3(2)
Fischer, M., Falke, D., & Sawers, R. G. (2013) · Molecular Microbiology · doi:10.1111/mmi.12344 · Cited by 21
The Radical SAM enzyme NirJ catalyzes the removal of two propionate side chains during heme d1 biosynthesis
Boß, L., Oehme, R., Billig, S., Birkemeyer, C., & Layer, G. (2017) · FEBS Journal · doi:10.1111/febs.14307 · Cited by 21
How does nitrous oxide reductase interact with its electron donors?—A docking study
Mattila, K., & Haltia, T. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20437 · Cited by 21
Cathodic supply of electrons to living microbial cells via cytocompatible redox-active polymers
Kaneko, M., Ishikawa, M., Song, J., Kato, S., Hashimoto, K., & Nakanishi, S. (2016) · Electrochemistry Communications · doi:10.1016/j.elecom.2016.12.002 · Cited by 20
The Prokaryotic Nitrate Reductases
Richardson, D. J., van Spanning, R. J. M., & Ferguson, S. J. (2007) · Elsevier eBooks · doi:10.1016/b978-044452857-5.50003-5 · Cited by 22
Self-citation
Nitrogen‐cycling bacteria and archaea in the carbonate sediment of a coral reef
Rusch, A., & Gaidos, E. J. (2013) · Geobiology · doi:10.1111/gbi.12048 · Cited by 20
Reduktion von N2O an einem μ4‐sulfidverbrückten vierkernigen aktiven CuZ‐Zentrum
Chen, P., Gorelsky, S. I., Dey, S. G., & Solomon, E. I. (2004) · Angewandte Chemie · doi:10.1002/ange.200301734 · Cited by 20
Silver nanomaterials in the natural environment: An overview of their biosynthesis and kinetic behavior
Guo, Z. H., Cui, K., Zeng, G., Wang, J., & Guo, X.-P. (2018) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2018.06.302 · Cited by 18
NirF is a periplasmic protein that binds d1 heme as part of its essential role in d1 heme biogenesis
Bali, S., Warren, M. J., & Ferguson, S. J. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07899.x · Cited by 18
Reverse protein engineering of a novel 4‐domain copper nitrite reductase reveals functional regulation by protein–protein interaction
Sasaki, D., Watanabe, T. F., Eady, R. R., Garratt, R. C., Antonyuk, S. V., & Hasnain, S. S. (2020) · FEBS Journal · doi:10.1111/febs.15324 · Cited by 18
Fine‐tuned regulation of the dissimilatory nitrite reductase gene by oxygen and nitric oxide in P seudomonas aeruginosa
Kuroki, M., Igarashi, Y., Ishii, M., & Arai, H. (2014) · Environmental Microbiology Reports · doi:10.1111/1758-2229.12212 · Cited by 18
Structure–function relationship of assimilatory nitrite reductases from the leaf and root of tobacco based on high‐resolution structures
Nakano, S., Takahashi, M., Sakamoto, A., Morikawa, H., & Katayanagi, K. (2012) · Protein Science · doi:10.1002/pro.2025 · Cited by 17
The Ferredoxin-Like Proteins HydN and YsaA Enhance Redox Dye-Linked Activity of the Formate Dehydrogenase H Component of the Formate Hydrogenlyase Complex
Pinske, C. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01238 · Cited by 17
Intramolecular Electron Transfer in Nitrite Reductases
Wherland, S. E., Farver, O., & Pecht, I. (2005) · ChemPhysChem · doi:10.1002/cphc.200400353 · Cited by 17
Modeling the effect of copper availability on bacterial denitrification
Woolfenden, H. C., Gates, A. J., Bocking, C., Blyth, M. G., Richardson, D. J., & Moulton, V. (2013) · MicrobiologyOpen · doi:10.1002/mbo3.111 · Cited by 18
Self-citation
Rhodobacter capsulatus gains a competitive advantage from respiratory nitrate reduction during light–dark transitions
Ellington, M. J., Richardson, D. J., & Ferguson, S. J. (2003) · Microbiology · doi:10.1099/mic.0.26090-0 · Cited by 16
Self-citation
Targeted quantification of functional enzyme dynamics in environmental samples for microbially mediated biogeochemical processes
Li, M., Gao, Y., Qian, W., Shi, L., Liu, Y., Nelson, W. C., Nicora, C., Resch, C. T., Thompson, C. J., Yan, S., et al. (2017) · Environmental Microbiology Reports · doi:10.1111/1758-2229.12558 · Cited by 16
Community structure of denitrifying and total bacteria during nitrogen accumulation in an ammonia‐loaded biofilter
Yasuda, T., Waki, M., Fukumoto, Y., Hanajima, D., Kuroda, K., Suzuki, K., Matsumoto, T., & Uenishi, H. (2017) · Journal of Applied Microbiology · doi:10.1111/jam.13603 · Cited by 16
Functional Redundancy in Perchlorate and Nitrate Electron Transport Chains and Rewiring Respiratory Pathways to Alter Terminal Electron Acceptor Preference
Wang, O., Melnyk, R. A., Mehta‐Kolte, M. G., Youngblut, M. D., Carlson, H. K., & Coates, J. D. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00376 · Cited by 15
Denitrification in the Marine Environment
Joye, S. B. (2003) · Encyclopedia of Environmental Microbiology · doi:10.1002/0471263397.env141 · Cited by 16
Flavodiiron Proteins: Nitric Oxide and/or Oxygen Reductases
Vicente, J. B., Carrondo, M. A., Teixeira, M. S., & Frazão, C. (2004) · Handbook of Metalloproteins · doi:10.1002/0470028637.met218 · Cited by 15
Environmental controls on the distribution of archaeal lipids in T ibetan hot springs: insight into the application of organic proxies for biogeochemical processes
Li, F., Zhang, C. L., Dong, H., Li, W., & Williams, A. J. (2013) · Environmental Microbiology Reports · doi:10.1111/1758-2229.12089 · Cited by 14
Bacterioplankton community variation in Bohai Bay (China) is explained by joint effects of environmental and spatial factors
Zhao, W., Wang, J., Xu, S., Yu, L., Yang, R., Shi, L., Wang, X., & Huang, Z. (2020) · MicrobiologyOpen · doi:10.1002/mbo3.997 · Cited by 14
Copper‐Containing Nitrite Reductase Employing Proton‐Coupled Spin‐Exchanged Electron‐Transfer and Multiproton Synchronized Transfer to Reduce Nitrite
Qin, X., Deng, L. P., Hu, C., Li, L., & Chen, X. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201703221 · Cited by 13
Electrocatalytic Nitrite Reduction to Nitrogen Oxide by a Synthetic Analogue of the Active Site of Cu‐Containing Nitrite Reductase Incorporated in Nafion Film
Migita, Y., Yokoyama, H., Minami, A., Mori, T., Nojiri, M., Suzuki, S., & Yamaguchi, K. (2009) · Electroanalysis · doi:10.1002/elan.200904700 · Cited by 13
Pseudomonas stutzeri soluble nitrate reductase αβ‐subunit is a soluble enzyme with a similar electronic structure at the active site as the inner membrane‐bound αβγ holoenzyme
Hettmann, T., Anemüller, S., Borcherding, H., Mathé, L., Steinrücke, P., & Diekmann, S. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03837-1 · Cited by 13
Impacts of maize hybrids with different nitrogen use efficiency on root‐associated microbiota based on distinct rhizosphere soil metabolites
Li, K., Chen, L., Shi, W., Hu, C., Sha, Y., Feng, G., Wang, E. T., Chen, W., Sui, X., & Mi, G. (2022) · Environmental Microbiology · doi:10.1111/1462-2920.16293 · Cited by 12
Differential protein expression during growth on model and commercial mixtures of naphthenic acids in Pseudomonas fluorescens Pf‐5
McKew, B. A., Johnson, R., Clothier, L., Skeels, K., Ross, M. S., Metodiev, M. V., Frenzel, M., Gieg, L. M., Martin, J. W., Hough, M. A., et al. (2021) · MicrobiologyOpen · doi:10.1002/mbo3.1196 · Cited by 12
Dissection of FixK 2 protein–DNA interaction unveils new insights into Bradyrhizobium diazoefficiens lifestyles control
Cabrera, J. J., Jiménez‐Leiva, A., Tomás‐Gallardo, L., Parejo, S., Casado, S., Torres, M. J., Bedmar, E. J., Delgado, M. J., & Mesa, S. (2021) · Environmental Microbiology · doi:10.1111/1462-2920.15661 · Cited by 12
Dissimilatory Nitrate Reductase
Romão, M. J., Dias, J. M. L., & Moura, I. (2004) · Wiley eBooks · doi:10.1002/0470028637.met178 · Cited by 12
Actinonin resistance of pathogenic Vibrio anguillarum in aquaculture
Yang, N., Song, F., Polyak, S. W., & Liu, J. (2021) · Aquaculture · doi:10.1016/j.aquaculture.2021.736850 · Cited by 11
Complex and flexible catabolism in Aromatoleum aromaticum pCyN1
Becker, P., Döhmann, A., Wöhlbrand, L., Thies, D., Hinrichs, C., Buschen, R., Wünsch, D., Neumann‐Schaal, M., Schomburg, D., Michael Winklhofer, A., et al. (2022) · Environmental Microbiology · doi:10.1111/1462-2920.16074 · Cited by 11
Paracoccus pantotrophus NapC can reductively activate cytochrome cd1 nitrite reductase
Zajicek, R. S., Allen, J. W. A., Cartron, M. L., Richardson, D. J., & Ferguson, S. J. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.03.072 · Cited by 11
Self-citation
Application of the Activated Sludge Model for Nitrogen to Elevated Nitrogen Conditions
Hiatt, W. C., & Grady, C. P. L. (2008) · Water Environment Research · doi:10.2175/106143008x304767 · Cited by 11
Mudflat reclamation causes changes of gene abundance in nitrogen cycle under long‐term rice cultivation
Zhang, Y., Li, Q., Chen, Y., Dai, Q., & Hu, J. (2019) · Journal of Basic Microbiology · doi:10.1002/jobm.201800660 · Cited by 11
Photophysical insights and guidelines for blue “turn‐on” fluorescent probes for the direct detection of nitric oxide (NO•) in biological systems
Olia, M. B. A., Hancock, A. N., Schiesser, C. H., Goerigk, L., & Wille, U. (2018) · Journal of Physical Organic Chemistry · doi:10.1002/poc.3896 · Cited by 10
Expression of nitrous oxide reductase from Pseudomonas stutzeri in transgenic tobacco roots using the root‐specific rolD promoter from Agrobacterium rhizogenes
Wan, S., Johnson, A. M., & Altosaar, I. (2011) · Ecology and Evolution · doi:10.1002/ece3.74 · Cited by 10
Distribution of carbon and nitrogen cycle microbes along permafrost peatland profile in Northeast China
Jiang, L., Song, Y., Sun, L., Ma, X., Wang, X., Song, C., Hou, A., & Wang, L. (2021) · Environmental Progress & Sustainable Energy · doi:10.1002/ep.13707 · Cited by 10
Biogeographic distribution patterns and assembly processes of nirS‐ type and nirK ‐type denitrifiers across the black soil zone in Northeast China
Hu, X., Gu, H., Liu, J., Liu, Z., Li, L., Du, S., Yu, Z., Li, Y., Jin, J., Liu, X., et al. (2021) · Soil Science Society of America Journal · doi:10.1002/saj2.20345 · Cited by 10
Copper Nitrite Reductase
Adman, E. T., & Murphy, M. E. P. (2004) · Handbook of Metalloproteins · doi:10.1002/0470028637.met201 · Cited by 10
Active Intermediates in Copper Nitrite Reductase Reactions Probed by a Cryotrapping‐Electron Paramagnetic Resonance Approach
Hedison, T. M., Shanmugam, M., Heyes, D. J., Edge, R., & Scrutton, N. S. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202005052 · Cited by 9
Identification of a Novel Gene for Biosynthesis of a Bacteroid-Specific Electron Carrier Menaquinone
Xie, F., Cheng, G., Xu, H., Wang, Z., Lei, L., & Li, Y. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028995 · Cited by 9
nir S‐type denitrifying bacterial assemblages respond to environmental conditions of a shallow estuary
Lisa, J. A., Jayakumar, A., Ward, B. B., & Song, B. (2017) · Environmental Microbiology Reports · doi:10.1111/1758-2229.12594 · Cited by 9
Rhodobacterales use a unique L‐threonine kinase for the assembly of the nucleotide loop of coenzyme B12
Tavares, N. K., VanDrisse, C. M., & Escalante‐Semerena, J. C. (2018) · Molecular Microbiology · doi:10.1111/mmi.14100 · Cited by 9
Proposed mechanism of inactivatingEscherichia coliO157:H7 by ultra-high pressure in combination withtert-butylhydroquinone
Malone, A. S., Chung, Y.-K., & Yousef, A. E. (2008) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2008.03973.x · Cited by 9
Nitric Oxide Synthase‐Like Activities in Plants
Yamasaki, H., Itoh, R. D., Bouchard, J. N., Dghim, A. A., Hossain, K. K., Gurung, S., & Cohen, M. F. (2010) · Wiley eBooks · doi:10.1002/9781444328608.ch5 · Cited by 9
Copper nitrite reductase from Sinorhizobium meliloti 2011: Crystal structure and interaction with the physiological versus a nonmetabolically related cupredoxin‐like mediator
Ramírez, C. S., Tolmie, C., Opperman, D. J., González, P. J., Rivas, M. G., Brondino, C. D., & Ferroni, F. M. (2021) · Protein Science · doi:10.1002/pro.4195 · Cited by 8
Metabolism
Wünschiers, R., Jahn, M., Jahn, D., Schomburg, I., Peifer, S., Heinzle, E., BURTSCHER, H. J., Garbe, J., Steen, A., Schobert, M., et al. (2012) · Wiley eBooks · doi:10.1002/9781118657072.ch3 · Cited by 8
Spectroscopic Characterization and Competitive Inhibition Studies of Azide Binding to a Functional NOR Model
Yang, Y., Dey, A., & Decréau, R. A. (2010) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201000566 · Cited by 6
Q-Site Occupancy Defines Heme Heterogeneity in Escherichia coli Nitrate Reductase A (NarGHI)
Fedor, J. G., Rothery, R. A., Giraldi, K. S., & Weiner, J. H. (2014) · Biochemistry · doi:10.1021/bi500121x · Cited by 6
„Brot aus Luft“ und andere chemische Beiträge zur Welternährung
Fischer, P. J., & Kühn, F. E. (2019) · Chemie in unserer Zeit · doi:10.1002/ciuz.201800848 · Cited by 6
An integrated strategy for the discovery of drug targets by the analysis of protein–protein interactions
Peltier, J. M., Ašković, S., Becklin, R. R., Chepanoske, C. L., Ho, Y.-S. J., Kéry, V., Lai, S., Mujtaba, T., Pyne, M., Robbins, P. B., et al. (2004) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2003.12.039 · Cited by 6
Nitrogen Cycling in Aquatic Environments
Ward, B. B. (2007) · doi:10.1128/9781555815882.ch42 · Cited by 6
Cytochrome cd 1Nitrite Reductase
Allen, J. W. A., Ferguson, S. J., & Fülöp, V. (2004) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc0557 · Cited by 6
Physiological and kinetic evaluation of ampicillin oxidation as unique electron source by a denitrifying sludge
Soriano, Y. R. B., Texier, A., & Cuervo-López, F. M. (2021) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.7014 · Cited by 5
Critical role of His369 in the reactivity of Pseudomonas aeruginosa cytochrome cd1 nitrite reductase with oxygen
Centola, F., Rinaldo, S., Brunori, M., & Cutruzzolà, F. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05455.x · Cited by 5
Syntheses, Characterization, and Reactivities of (μ‐η2:η2‐Disulfido)dicopper(II) Complexes with N‐Alkylated cis,cis‐1,3,5‐Triaminocyclohexane Derivatives
Kajita, Y., Matsumoto, J., Takahashi, I., Hirota, S., Funahashi, Y., Ozawa, T., & Masuda, H. (2008) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.200701358 · Cited by 5
Rate of denitrification and stoichiometry of its products in fluvo‐aquic Cambisols for sterilized and unsterilized incubations
Wang, Y., Cao, W., Zhang, X., & Guo, J. (2018) · European Journal of Soil Science · doi:10.1111/ejss.12763 · Cited by 5
Functional roles of norCB in Pseudomonas aeruginosa ATCC 9027 under aerobic conditions
Zhou, G., Wang, Y., Peng, H., Shen, P., Xie, X., & Shi, Q. (2019) · Journal of Basic Microbiology · doi:10.1002/jobm.201900267 · Cited by 5
Does Diapirism Influence Greenhouse Gas Production on Patterned Ground in the High Arctic?
Brummell, M. E., Guy, A. L., & Siciliano, S. D. (2015) · Soil Science Society of America Journal · doi:10.2136/sssaj2015.01.0026 · Cited by 5
A comparison of nitrate removal and denitrifying bacteria populations among three wetland plant communities
Gordon, B. A., Lenhart, C., & LaPara, T. M. (2020) · Journal of Environmental Quality · doi:10.1002/jeq2.20004 · Cited by 5
Mitigation of Laughing Gas Emissions by Nitrous Oxide Respiring Microorganisms
Simon, J. (2020) · Springer eBooks · doi:10.1007/978-3-030-58315-6_7 · Cited by 5
Nitric Oxide Synthase‐Like Activities in Plants
Yamasaki, H., Itoh, R. D., Bouchard, J. N., Dghim, A. A., Hossain, K. K., Gurung, S., & Cohen, M. F. (2017) · Wiley eBooks · doi:10.1002/9781119312994.apr0452 · Cited by 5
Metabolic versatility and nitrate reduction pathways of a new thermophilic bacterium of the Deferrivibrionaceae: Deferrivibrio metallireducens sp. nov isolated from hot sediments of Vulcano Island, Italy
Galès, G., Hennart, M., Hannoun, M., Postec, A., & Erauso, G. (2025) · PLoS ONE · doi:10.1371/journal.pone.0315093 · Cited by 4
Active Intermediates in Copper Nitrite Reductase Reactions Probed by a Cryotrapping‐Electron Paramagnetic Resonance Approach
Hedison, T. M., Shanmugam, M., Heyes, D. J., Edge, R., & Scrutton, N. S. (2020) · Angewandte Chemie · doi:10.1002/ange.202005052 · Cited by 4
Phylogenomic analysis of Citrobacter sp. strain AAK_AS5 and its metabolic capabilities to support nitrogen removal behavior
Gupta, R. K., Singh, A. K., Bajaj, A., Khardenavis, A. A., & Purohit, H. J. (2022) · Journal of Basic Microbiology · doi:10.1002/jobm.202200323 · Cited by 4
Investigating the role of organic carbon amendments and microbial denitrification gene abundance in nitrogen removal from experimental agricultural drainage ditches with low‐grade weirs
Faust, D. R., Kröger, R., Baker, B. H., Brooks, J. P., Cox, M. S., & Rush, S. A. (2019) · Water Environment Research · doi:10.1002/wer.1284 · Cited by 4
Crystal structure of NirF: insights into its role in heme d 1 biosynthesis
Klünemann, T., Nimtz, M., Jänsch, L., Layer, G., & Blankenfeldt, W. (2020) · FEBS Journal · doi:10.1111/febs.15323 · Cited by 4
Refined Distances Between Paramagnetic Centers of a Multi‐Copper Nitrite Reductase Determined by Pulsed EPR (iDEER) Spectroscopy
van Wonderen, J. H., Kostrz, D. N., Dennison, C., & MacMillan, F. (2013) · Angewandte Chemie · doi:10.1002/ange.201208166 · Cited by 4
The role of conserved proteins DrpA and DrpB in nitrate respiration of Thermus thermophilus
Chahlafi, Z., Álvarez, L., Cava, F., & Berenguer, J. (2018) · Environmental Microbiology · doi:10.1111/1462-2920.14400 · Cited by 4
Carbon sink reduction by fruit removal triggers respiration but not nitrous oxide emissions from the root zone of cucumber
Nett, L., Hauschild, I., & Kläring, H. ‐. (2019) · Annals of Applied Biology · doi:10.1111/aab.12516 · Cited by 4

Authors: Brondijk, T. H. C., Fiegen, D., Richardson, D. J., & Cole, J. A.
Affiliations: University of Birmingham (GB)
University of East Anglia (GB)
Corresponding author: Cole, J. A.
ORCID: Brondijk, T. H. C.
Fiegen, D.
Richardson, D. J.
Cole, J. A.
Venue: Molecular Microbiology
Publisher: Wiley
Published: 2002-04-20
Volume: 44
Issue: 1
Pages: 245-255
ISSN: 0950-382X (ISSN-L)
1365-2958
DOI: 10.1046/j.1365-2958.2002.02875.x
OpenAlex: W1925458372
Cited by: 342
References: 27
Citations by year: 2026: 3 · 2025: 5 · 2024: 3 · 2023: 4 · 2022: 6 · 2021: 17 · 2020: 16 · 2019: 14 · 2018: 16 · 2017: 20 · 2016: 14 · 2015: 14 · 2014: 17 · 2013: 22 · 2012: 16
FWCI: 9.02
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: doi.wiley.com/10.1002/tdm_license_1.1 (tdm, 4882 d)
Locations: Molecular Microbiology (publishedVersion)
PubMed (publishedVersion)
University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
UEA Digital Repository (University of East Anglia) (submittedVersion)
Funders: Biotechnology and Biological Sciences Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: periplasmic nitrate reductase, Napf, ubiquinol oxidation, electron transfer, Q-cycle, proton pump, energy conservation, Escherichia coli K-12, iron-sulfur proteins, menaquinone biosynthesis, ubiquinone biosynthesis
MeSH terms: Energy Metabolism, Escherichia coli, Kinetics, Nitrate Reductases, Nitrates, Operon, Oxidation-Reduction, Ubiquinone, Vitamin K, Gene Deletion, Protein Subunits, Escherichia coli 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

Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation: Roles of NapF, G and H in ubiquinol oxidation in E. coli

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks