Evidence map›Paper›PMID 22266822›Full record

ArticleNature structural & molecular biology2012

Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus.

Yushi Matsumoto, Takehiko Tosha, Andrei V Pisliakov, Tomoya Hino, Hiroshi Sugimoto, Shingo Nagano, Yuji Sugita, Yoshitsugu Shiro

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Insertion of the FeFEBS letters · 2025
    Article
  5. Improving macromolecular structure refinement with metal-coordination restraints.Acta crystallographica. Section D, Structural biology · 2024
    Article
  6. 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
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Architecture of bacterial respiratory chains.Nature reviews. Microbiology · 2021
    Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

8 authors at 2 institutions in 1 country.

Yushi MatsumotoBiometal Science Laboratory, RIKEN SPring-8 Center, Sayo, Hyogo, Japan.
Takehiko Tosha
Andrei V Pisliakov
Tomoya Hino
Hiroshi Sugimoto
Shingo Nagano
Yuji Sugita
Yoshitsugu Shiro
SPring-8 · JPRIKEN Advanced Science Institute · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structure of quinol-dependent nitric oxide reductase (qNOR) from G. stearothermophilus, which catalyzes the reduction of NO to produce the major ozone-depleting gas N(2)O, has been characterized at 2.5 Å resolution. The overall fold of qNOR is similar to that of cytochrome c-dependent NOR (cNOR), and some structural features that are characteristic of cNOR, such as the calcium binding site and hydrophilic cytochrome c domain, are observed in qNOR, even though it harbors no heme c. In contrast to cNOR, structure-based mutagenesis and molecular dynamics simulation studies of qNOR suggest that a water channel from the cytoplasm can serve as a proton transfer pathway for the catalytic reaction. Further structural comparison of qNOR with cNOR and aerobic and microaerobic respiratory oxidases elucidates their evolutionary relationship and possible functional conversions.

Indexed as

Amino Acid SubstitutionCrystallography, X-RayGeobacillus stearothermophilusHydroquinonesModels, MolecularMolecular Dynamics SimulationMutagenesis, Site-DirectedMutant ProteinsNitric OxideNitrous OxideOxidoreductasesProtein ConformationHydroquinonesMutant ProteinsNitric Oxidenitric-oxide reductaseNitrous OxideOxidoreductases

Identifiers

PMID22266822
OpenAlexW2032020235

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.