Cited by 99Metalloenzymes and iron-sulfur proteinsBacterial Genetics and BiotechnologyEnzyme Structure and Function

Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12

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POTTER, Laura C., COLE, Jeffrey A.·1999·Biochemical Journal

Abstract

The seven nap genes at minute 47 on the Escherichia coli K-12 chromosome encode a functional nitrate reductase located in the periplasm. The molybdoprotein, NapA, is known to be essential for nitrate reduction. We now demonstrate that the two c-type cytochromes, the periplasmic NapB and the membrane-associated NapC, as well as a fourth polypeptide, NapD, are also essential for nitrate reduction in the periplasm by physiological substrates such as glycerol, formate and glucose. None of the three iron-sulphur proteins, NapF, NapG or NapH, are essential, irrespective of whether the bacteria are grown anaerobically in the presence of nitrate or fumarate as a terminal electron acceptor, or by glucose fermentation. Mutation of napD resulted in the total loss of Methyl Viologen-dependent nitrate reductase activity of the molybdoprotein, NapA, consistent with an earlier suggestion by others that NapD might be required for post-translational modification of NapA.

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  • napB gene deletion mutants in R. sphaeroides and E. coli exhibit very little activity.

    “napB gene deletion mutants in R. sphaeroides215 and E. coli102 exhibit very little activity”

    From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [102]

  • Mutational studies on R. sphaeroides, E. coli, and Wolinella succinogenes have given insight into the significance of each auxiliary nap gene in nitrate reduction via Nap.

    “Mutational studies conducted on R. sphaeroides,215 E. coli,102 and Wolinella succinogenes105 have given insight into the significance of each auxiliary nap gene in nitrate reduction via Nap.”

    From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [102]

  • NapC is considered an essential component of electron transport to NapA in organisms in which it is found.

    “NapC, a tetra-heme transmembrane protein, is also considered to be an essential component of electron transport to NapA in organisms in which it is found.102”

    From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [102]

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Authors
POTTER, L. C., & COLE, J. A.
Affiliations
University of Birmingham (GB)
Venue
Biochemical Journal
Published
1999-11-08
Volume
344
Issue
1
Pages
69-76
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W1993696884
Cited by
93
References
38
Citations by year
2024: 3 · 2023: 2 · 2022: 1 · 2020: 1 · 2019: 4 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 4 · 2014: 4 · 2013: 3 · 2012: 1
FWCI
8.33
Type
journal article
Language
en
Open access
Locations
  • Biochemical Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Directorate for Biological Sciences
  • Medical Research Council
Topics
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
gene essentiality, post-translational modification, Escherichia coli K-12, glycerol, formate, glucose
MeSH terms
Bacterial Proteins, Base Sequence, Cytochrome c Group, Electron Transport, Escherichia coli, Fermentation, Fumarates, Genes, Bacterial, Glucose, Mutation, Nitrate Reductases, Oxidation-Reduction, Plasmids, Gene Deletion, DNA Primers, Nitric Acid, Periplasm, Escherichia coli Proteins, Nitrate Reductase

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