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Cited by 152Bacterial Genetics and BiotechnologyMetalloenzymes and iron-sulfur proteinsWastewater Treatment and Nitrogen Removal

Nitrate reduction in the periplasm of gram-negative bacteria

Potter, Laura, Angove, Hayley, Richardson, David, Cole, Jeff·2001·Advances in Microbial Physiology
DOI 10.1016/s0065-2911(01)45002-8
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Abstract

In contrast to the bacterial assimilatory and membrane-associated, respiratory nitrate reductases that have been studied for many years, it is only recently that periplasmic nitrate reductases have attracted growing interest. Recent research has shown that these soluble proteins are widely distributed, but vary greatly between species. All of those so far studied include four essential components: the periplasmic molybdoprotein, NapA, which is associated with a small, di-haem cytochrome, NapB; a putative quinol oxidase, NapC; and a possible pathway-specific chaperone, NapD. At least five other components have been found in different species. Other variations between species include the location of the nap genes on chromosomal or extrachromosomal DNA, and the environmental factors that regulate their expression. Despite the relatively small number of bacteria so far screened, striking correlations are beginning to emerge between the organization of the nap genes, the physiology of the host, the conditions under which the nap genes are expressed, and even the fate of nitrite, the product of Nap activity. Evidence is emerging that Nap fulfills a novel role in nitrate scavenging by some pathogenic bacteria.

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  • The loss of potential energy from lower ATP generation by Nap may be compensated by the higher affinity for nitrate typically found in periplasmic nitrate reductases.

    “Although the gradient may be less than that generated by the cytoplasmic-facing Nar complex, the loss of potential energy may be compensated by the higher affinity for nitrate typically found in periplasmic nitrate reductases.”

    From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [97]

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Authors
Potter, L., Angove, H., Richardson, D., & Cole, J.
Affiliations
  • University of Birmingham (GB)
  • University of East Anglia (GB)
ORCID
Richardson, David
Venue
Advances in Microbial Physiology
Publisher
Elsevier
Published
2001
Volume
45
Pages
51-112
ISSN
0065-2911 (ISSN-L)
DOI
10.1016/s0065-2911(01)45002-8
OpenAlex
W1756037023
Cited by
152
References
205
Citations by year
2026: 4 · 2025: 1 · 2024: 3 · 2023: 2 · 2022: 4 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 7 · 2017: 5 · 2016: 5 · 2015: 7 · 2014: 7 · 2013: 11 · 2012: 5
FWCI
14.50
Type
book chapter
Language
en
Open access
closed
Locations
  • Advances in microbial physiology/Advances in Microbial Physiology (publishedVersion)
  • PubMed (publishedVersion)
  • University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
  • UEA Digital Repository (University of East Anglia) (submittedVersion)
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 › Environmental Science › Pollution › Wastewater Treatment and Nitrogen Removal
Keywords
periplasmic nitrate reductase, napA, quinol oxidase, gene expression regulation, pathogenic bacteria, Gram-negative bacteria
MeSH terms
Amino Acid Sequence, Base Sequence, Gram-Negative Bacteria, Models, Chemical, Molecular Sequence Data, Nitrate Reductases, Nitrates, Oxidation-Reduction, Gene Expression Regulation, Bacterial, Sequence Alignment, Sequence Homology, Amino Acid, Periplasm

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