Evidence map›Paper›PMID 23858452›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Characterization of the nitric oxide reductase from Thermus thermophilus.

Lici A Schurig-Briccio, Padmaja Venkatakrishnan, James Hemp, Carlos Bricio, José Berenguer, Robert B Gennis

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Insertion of the FeFEBS letters · 2025
    Article
  3. Diversity and evolution of nitric oxide reduction in bacteria and archaea.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Transferable denitrification capability of Thermus thermophilus.Applied and environmental microbiology · 2014
    Review
  10. Article
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

6 authors at 3 institutions in 2 countries.

Lici A Schurig-BriccioDepartment of Biochemistry, University of Illinois, Urbana, IL 61801, USA.
Padmaja Venkatakrishnan
James Hemp
Carlos Bricio
José Berenguer
Robert B Gennis
University of Illinois Urbana-Champaign · USConsejo Superior de Investigaciones Científicas · ESUniversidad Autónoma de Madrid · ES

Funding

PROTEIN/LIPID INTERACTIONSR01HL016101 · NHLBI · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GENNIS, ROBERT B · 1985 to 2015
$6.8M
PROTEIN/LIPID INTERACTIONSR37HL016101 · NHLBI · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GENNIS, ROBERT B. · 1993 to 2002
$1.5M
NHLBI NIH HHS HL16101NHLBI NIH HHS R01 HL016101NHLBI NIH HHS R37 HL016101
6 · The paper itself

Abstract

Nitrous oxide (N2O) is a powerful greenhouse gas implicated in climate change. The dominant source of atmospheric N2O is incomplete biological dentrification, and the enzymes responsible for the release of N2O are NO reductases. It was recently reported that ambient emissions of N2O from the Great Boiling Spring in the United States Great Basin are high, and attributed to incomplete denitrification by Thermus thermophilus and related bacterial species [Hedlund BP, et al. (2011) Geobiology 9(6)471-480]. In the present work, we have isolated and characterized the NO reductase (NOR) from T. thermophilus. The enzyme is a member of the cNOR family of enzymes and belongs to a phylogenetic clade that is distinct from previously examined cNORs. Like other characterized cNORs, the T. thermophilus cNOR consists of two subunits, NorB and NorC, and contains a one heme c, one Ca(2+), a low-spin heme b, and an active site consisting of a high-spin heme b and FeB. The roles of conserved residues within the cNOR family were investigated by site-directed mutagenesis. The most important and unexpected result is that the glutamic acid ligand to FeB is not essential for function. The E211A mutant retains 68% of wild-type activity. Mutagenesis data and the pattern of conserved residues suggest that there is probably not a single pathway for proton delivery from the periplasm to the active site that is shared by all cNORs, and that there may be multiple pathways within the T. thermophilus cNOR.

Indexed as

Amino Acid SubstitutionBacterial ProteinsCalciumHemeMutagenesis, Site-DirectedMutation, MissenseOxidoreductasesProtein SubunitsThermus thermophilusBacterial ProteinsCalciumHemenitric-oxide reductaseOxidoreductasesProtein Subunitsproton pathwaythermophilic

Identifiers

PMID23858452
PMCPMC3732958
OpenAlexW1971871683

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.