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Cited by 178Hemoglobin structure and functionBacterial Genetics and BiotechnologyRedox biology and oxidative stress

Nitric Oxide Formation by Escherichia coli

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Corker, Hazel, Poole, Robert K.·2003·Journal of Biological Chemistry
DOI 10.1074/jbc.m303282200
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Abstract

Nitric oxide (NO) is a key signaling and defense molecule in biological systems. The bactericidal effects of NO produced, for example, by macrophages are resisted by various bacterial NO-detoxifying enzymes, the best understood being the flavohemoglobins exemplified by Escherichia coli Hmp. However, many bacteria, including E. coli, are reported to produce NO by processes that are independent of denitrification in which NO is an obligatory intermediate. We demonstrate using an NO-specific electrode that E. coli cells, grown anaerobically with nitrate as terminal electron acceptor, generate significant NO on adding nitrite. The periplasmic cytochrome c nitrite reductase (Nrf) is shown, by comparing Nrf+ and Nrf- mutants, to be largely responsible for NO generation. Surprisingly, an hmp mutant did not accumulate more NO but, rather, failed to produce detectable NO. Anaerobic growth of the hmp mutant was not stimulated by nitrate, and the mutant failed to produce periplasmic cytochrome(s) c, leading to the hypothesis that accumulating NO in the absence of Hmp inactivates the global anaerobic regulator Fnr by reaction with the [4Fe-4S]2+ cluster (Cruz-Ramos, H., Crack, J., Wu, G., Hughes, M. N., Scott, C., Thomson, A. J., Green, J., and Poole, R. K. (2002) EMBO J. 21, 3235-3244). Fnr thus failed to up-regulate nitrite reductase. The model is supported by the inability of an fnr mutant to generate NO and by the restoration of NO accumulation to hmp mutants upon introducing a plasmid encoding Fnr* (D154A) known to confer activity in the presence of oxygen. A cytochrome bd-deficient mutant retained NO-generating activity. The present study reveals a critical balance between NO-generating and -detoxifying activities during anaerobic growth.

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  • Several following studies have proposed different mechanisms of bacterial NO formation independent of respiratory denitrification, such as arginine-dependent bacterial NOS activity, DNRA, and non-enzymatic processes.

    “However, several following studies on bacterial NO formation have proposed different mechanisms independent of respiratory denitrification such as arginine dependent bacterial NOS enzymatic activity, DNRA and non-enzymatic processes [15,32–34].”

    From Nitrate reduction to nitrite, nitric oxide and ammonia by gut bacteria under physiological conditions (2015) · cites this paper as [33]

  • Respiratory denitrification can generate small but relevant amounts of NO as an intermediate product and has been implicated in bacterial NO production in the gut.

    “Respiratory denitrification can also generate small but relevant amounts of NO as an intermediate product and has been implicated in the bacterial NO production in the gut [32,33].”

    From Nitrate reduction to nitrite, nitric oxide and ammonia by gut bacteria under physiological conditions (2015) · cites this paper as [33]

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Research works printed but not linked: 4

  1. Gardner, P. R., Gardner, A. M., Martin, L. A., and Salzman, A. L. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 10378 -10383
  2. Hausladen, A., Gow, A. J., and Stamler, J. S. (1998) Proc. Natl. Acad. Sci.
  3. Wu, G., Wainwright, L. M., and Poole, R. K. (2003) Adv. Microb. Physiol. 47, in press
  4. Hausladen, A., Gow, A. J., and Stamler, J. S. (2001) Proc. Natl. Acad. Sci.

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Authors
Corker, H., & Poole, R. K.
Affiliations
University of Sheffield (GB)
Corresponding author
Poole, Robert K.
ORCID
Poole, Robert K.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2003-08
Volume
278
Issue
34
Pages
31584-31592
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.m303282200
OpenAlex
W2087747384
Cited by
178
References
65
Citations by year
2026: 3 · 2025: 2 · 2024: 9 · 2023: 6 · 2022: 3 · 2021: 8 · 2020: 8 · 2019: 5 · 2018: 8 · 2017: 5 · 2016: 15 · 2015: 9 · 2014: 11 · 2013: 10 · 2012: 8
FWCI
2.55
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • Directorate for Biological Sciences
  • Biotechnology and Biological Sciences Research Council (P18939)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords
nitric oxide production, Escherichia coli, cytochrome c nitrite reductase, flavohemoglobin, Hmp, FNR, [4Fe-4S] cluster, nitrite reductase, anaerobic growth, cytochrome bd, nitric oxide detoxification
MeSH terms
Dihydropteridine Reductase, Escherichia coli, Hemeproteins, Iron-Sulfur Proteins, Mutation, NADH, NADPH Oxidoreductases, Nitric Oxide, Nitrite Reductases, Sensitivity and Specificity, Escherichia coli Proteins

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