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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 accessAbstract
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.
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“Ubiquinone electron transfer from NapGH to NapABC is more efficient than ubiquinol transfer directly from NapC to NapAB.258”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [258]
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“NapF is not considered to be essential for NapA maturation, although it does aid in [4Fe–4S] insertion. 105,258,274”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [258]
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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
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-citationRichardson, D. J. (2000) · Microbiology · doi:10.1099/00221287-146-3-551 · Cited by 544
Self-citationFunctional, 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-citationMyers, 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
Wallace, B., & Young, I. G. (1977) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(77)90071-8 · Cited by 235
Søballe, B., & Poole, R. K. (1999) · Microbiology · doi:10.1099/13500872-145-8-1817 · Cited by 226
Rabin, R. S., & Stewart, V. J. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.11.3259-3268.1993 · Cited by 223
Myers, J. M., & Myers, C. R. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.1.67-75.2000 · Cited by 203
Simon, J., Groß, R., Einsle, O., Kroneck, P. M. H., Kröger, A., & Klimmek, O. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01742.x · Cited by 155
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
Self-citationNitrate reduction in the periplasm of gram-negative bacteria
Potter, L., Angove, H., Richardson, D., & Cole, J. (2001) · Advances in Microbial Physiology · doi:10.1016/s0065-2911(01)45002-8 · Cited by 152
Self-citationDissimilatory nitrate reductases in bacteria
Philippot, L., & Højberg, O. (1999) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(99)00072-x · Cited by 143
Wang, H., Tseng, C., & Gunsalus, R. P. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.17.5303-5308.1999 · Cited by 137
Wissenbach, U., Kr�ger, A., & Unden, G. (1990) · Archives of Microbiology · doi:10.1007/bf00249179 · Cited by 113
POTTER, L. C., & COLE, J. A. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440069 · Cited by 93
Self-citationWissenbach, U., Ternes, D. J., & Unden, G. (1992) · Archives of Microbiology · doi:10.1007/bf00249068 · Cited by 92
The Fermentation of Lactulose by Colonic Bacteria
Sahota, S. S., Bramley, P. M., & Menzies, I. S. (1982) · Microbiology · doi:10.1099/00221287-128-2-319 · Cited by 87
POPE, N. R., & Cole, J. A. (1982) · Microbiology · doi:10.1099/00221287-128-1-219 · Cited by 62
Self-citationAnaerobically expressed Escherichia coli genes identified by operon fusion techniques
Choe, M., & Reznikoff, W. S. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.19.6139-6146.1991 · Cited by 60
REYES, F., GAVIRA, M., CASTILLO, F., & MORENO-VIVIÁN, C. (1998) · Biochemical Journal · doi:10.1042/bj3310897 · Cited by 56
Tyson, K. L., Metheringham, R. L., Griffiths, L., & Cole, J. A. (1997) · Archives of Microbiology · doi:10.1007/s002030050515 · Cited by 30
Self-citationballe, B. S., & Poole, R. K. (1998) · Microbiology · doi:10.1099/00221287-144-2-361 · Cited by 30
POTTER, L. C., MILLINGTON, P., GRIFFITHS, L., THOMAS, G. H., & COLE, J. A. (1999) · Biochemical Journal · doi:10.1042/bj3440077 · Cited by 2
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Metadata
- 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.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2002-04-20
- Volume
- 44
- Issue
- 1
- Pages
- 245-255
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- 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
- 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
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