Evidence map›Paper›PMID 22451105›Full record

ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2012

Structural basis for nitrous oxide generation by bacterial nitric oxide reductases.

Yoshitsugu Shiro, Hiroshi Sugimoto, Takehiko Tosha, Shingo Nagano, Tomoya Hino

Abstract read
In one paragraph

Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. One-Electron NO to NChemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Nitrosyl Linkage Isomers: NO Coupling to NJournal of the American Chemical Society · 2019
    Article
  11. OACS catalysis · 2018
    Article
  12. Article
  13. Heme redox potentials hold the key to reactivity differences between nitric oxide reductase and heme-copper oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Article
  16. Article
  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

5 authors.

Yoshitsugu ShiroRIKEN SPring-8 Center, Sayo, Hyogo, Japan. yshiro@riken.jp
Hiroshi Sugimoto
Takehiko Tosha
Shingo Nagano
Tomoya Hino

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crystal structure of the bacterial nitric oxide reductase (cNOR) from Pseudomonas aeruginosa is reported. Its overall structure is similar to those of the main subunit of aerobic and micro-aerobic cytochrome oxidases (COXs), in agreement with the hypothesis that all these enzymes are members of the haem-copper oxidase superfamily. However, substantial structural differences between cNOR and COX are observed in the catalytic centre and the delivery pathway of the catalytic protons, which should be reflected in functional differences between these respiratory enzymes. On the basis of the cNOR structure, we propose a possible reaction mechanism of nitric oxide reduction to nitrous oxide as a working hypothesis.

Indexed as

Crystallography, X-RayModels, MolecularNitric OxideNitrous OxideOxidoreductasesPseudomonas aeruginosaNitric Oxidenitric-oxide reductaseNitrous OxideOxidoreductases

Identifiers

PMID22451105
PMCPMC3306621

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.