Cited by 68Microbial Fuel Cells and BioremediationMetalloenzymes and iron-sulfur proteinsBacterial Genetics and Biotechnology

Nitrate reduction by Desulfovibrio desulfuricans: A periplasmic nitrate reductase system that lacks NapB, but includes a unique tetraheme c-type cytochrome, NapM

Marietou, Angeliki, Richardson, David, Cole, Jeff, Mohan, Sudesh·2005·FEMS Microbiology Letters

Abstract

Many sulphate reducing bacteria can also reduce nitrite, but relatively few isolates are known to reduce nitrate. Although nitrate reductase genes are absent from Desulfovibrio vulgaris strain Hildenborough, for which the complete genome sequence has been reported, a single subunit periplasmic nitrate reductase, NapA, was purified from Desulfovibrio desulfuricans strain 27774, and the structural gene was cloned and sequenced. Chromosome walking methods have now been used to determine the complete sequence of the nap gene cluster from this organism. The data confirm the absence of a napB homologue, but reveal a novel six-gene organisation, napC-napM-napA-napD-napG-napH. The NapC polypeptide is more similar to the NrfH subgroup of tetraheme cytochromes than to NapC from other bacteria. NapM is predicted to be a tetra-heme c-type cytochrome with similarity to the small tetraheme cytochromes from Shewanella oneidensis. The operon is located close to a gene encoding a lysyl-tRNA synthetase that is also found in D. vulgaris. We suggest that electrons might be transferred to NapA either from menaquinol via NapC, or from other electron donors such as formate or hydrogen via the small tetraheme cytochrome, NapM. We also suggest that, despite the absence of a twin-arginine targeting sequence, NapG might be located in the periplasm where it would provide an alternative direct electron donor to NapA.

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Crossref · 10.1016/j.femsle.2005.05.042

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  • Organisms lacking the napB gene, such as Desulfovibrio desulfuricans, encode alternative iron cofactor redox partners such as NapM or NapC.

    “Organisms lacking the napB gene, such as Desulfovibrio desulfuricans, encode alternative iron cofactor redox partners, such as NapM or NapC.249,250”

    From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [249]

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Authors
Marietou, A., Richardson, D., Cole, J., & Mohan, S.
Affiliations
  • University of Birmingham (GB)
  • University of East Anglia (GB)
Corresponding author
Cole, Jeff
Venue
FEMS Microbiology Letters
Published
2005-07
Volume
248
Issue
2
Pages
217-225
ISSN
  • 0378-1097 (ISSN-L)
  • 1574-6968
OpenAlex
W2075673568
Cited by
68
References
23
Citations by year
2026: 3 · 2025: 2 · 2024: 1 · 2023: 5 · 2022: 3 · 2021: 4 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 2 · 2016: 3 · 2015: 3 · 2014: 2 · 2013: 4 · 2012: 8
FWCI
5.58
Type
journal article
Language
en
Open access
closed
Locations
  • FEMS Microbiology Letters (publishedVersion)
  • PubMed (publishedVersion)
  • University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
  • UEA Digital Repository (University of East Anglia) (submittedVersion)
Funders
Directorate for Biological Sciences
Topics
  • Physical Sciences › Environmental Science › Environmental Engineering › Microbial Fuel Cells and Bioremediation
  • 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
Keywords
Desulfovibrio desulfuricans, nitrate reduction, periplasmic nitrate reductase, napA, electron transfer, sulfate-reducing bacteria, lysyl-tRNA synthetase
MeSH terms
Amino Acid Sequence, Bacterial Proteins, Multigene Family, Molecular Sequence Data, Nitrate Reductases, Nitrates, Operon, Oxidation-Reduction, Quinone Reductases, Sequence Alignment, Periplasm, Desulfovibrio desulfuricans, Cytochromes c, Nitrate Reductase

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