Evidence map›Paper›PMID 14563865›Full record

ArticleJournal of bacteriology2003

A mutant of Paracoccus denitrificans with disrupted genes coding for cytochrome c550 and pseudoazurin establishes these two proteins as the in vivo electron donors to cytochrome cd1 nitrite reductase.

Isobel V Pearson, M Dudley Page, Rob J M van Spanning, Stuart J Ferguson

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 61 citations in OpenAlex.

  1. Deep learning-drivenSynthetic and systems biotechnology · 2027
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  5. The crystal structure of the heme dActa crystallographica. Section D, Structural biology · 2020
    Article
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  8. Article
  9. Article
  10. Transferable denitrification capability of Thermus thermophilus.Applied and environmental microbiology · 2014
    Review
  11. Review
  12. The electron transfer complex between nitrous oxide reductase and its electron donors.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011
    Article
  13. Article
  14. Article
  15. Article
  16. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Isobel V PearsonDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
M Dudley Page
Rob J M van Spanning
Stuart J Ferguson
University of Oxford · GBUniversity of Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Paracoccus denitrificans, electrons pass from the membrane-bound cytochrome bc(1) complex to the periplasmic nitrite reductase, cytochrome cd(1). The periplasmic protein cytochrome c(550) has often been implicated in this electron transfer, but its absence, as a consequence of mutation, has previously been shown to result in almost no attenuation in the ability of the nitrite reductase to function in intact cells. Here, the hypothesis that cytochrome c(550) and pseudoazurin are alternative electron carriers from the cytochrome bc(1) complex to the nitrite reductase was tested by construction of mutants of P. denitrificans that are deficient in either pseudoazurin or both pseudoazurin and cytochrome c(550). The latter organism, but not the former (which is almost indistinguishable in this respect from the wild type), grows poorly under anaerobic conditions with nitrate as an added electron acceptor and accumulates nitrite in the medium. Growth under aerobic conditions with either succinate or methanol as the carbon source is not significantly affected in mutants lacking either pseudoazurin or cytochrome c(550) or both these proteins. We concluded that pseudoazurin and cytochrome c(550) are the alternative electron mediator proteins between the cytochrome bc(1) complex and the cytochrome cd(1)-type nitrite reductase. We also concluded that expression of pseudoazurin is mainly controlled by the transcriptional activator FnrP.

Indexed as

Genes, BacterialAnaerobiosisAzurinBase SequenceBiological TransportCloning, MolecularCytochrome c GroupCytochromesElectron TransportElectron Transport Complex IVMethanolMolecular Sequence DataNitrite ReductasesParacoccus denitrificansSequence AlignmentSuccinic AcidAzurincytochrome C-550Cytochrome c GroupCytochromesElectron Transport Complex IVMethanolnitrite reductase (NO-forming)Nitrite ReductasespseudoazurinSuccinic Acid

Identifiers

PMID14563865
PMCPMC219389
OpenAlexW2154755010

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.