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

Brondijk, T. H. C.; Fiegen, D.; Richardson, D. J.; Cole, J. A.

doi:10.1046/j.1365-2958.2002.02875.x

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

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

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

DOI 10.1046/j.1365-2958.2002.02875.x

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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.

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Ubiquinone electron transfer from NapGH to NapABC is more efficient than ubiquinol transfer directly from NapC to NapAB.
“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]
NapF is not considered essential for NapA maturation, although it aids in [4Fe-4S] insertion.
“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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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
Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Physical Sciences › Materials Science › Materials Chemistry › 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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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

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