Evidence map›Paper›PMID 34145390›Full record

ArticleThe ISME journal2021

Evolution of the cytochrome bd oxygen reductase superfamily and the function of CydAA' in Archaea.

Ranjani Murali, Robert B Gennis, James Hemp

Open access · bronzeAbstract read
In one paragraph

Article in The ISME journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Review
  3. Effect of Ammonia onAntioxidants (Basel, Switzerland) · 2026
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  7. TheProceedings of the National Academy of Sciences of the United States of America · 2026
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  12. Unusual Plastoquinones in Non-Phototrophic Nitrifying Bacteria.Environmental microbiology reports · 2025
    Article
  13. Carbon Monoxide and Prokaryotic Energy Metabolism.International journal of molecular sciences · 2025
    Review
  14. A cytochromeApplied and environmental microbiology · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Membrane-Bound Redox Enzyme CytochromeInternational journal of molecular sciences · 2024
    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

3 authors at 3 institutions in 1 country.

Ranjani MuraliDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, USA. m.ranjani@gmail.com.ORCID http://orcid.org/0000-0003-4073-9910
Robert B GennisDepartment of Biochemistry, University of Illinois, Urbana-Champaign, Urbana, IL, USA.
James HempThe Metrodora Institute, Salt Lake City, UT, USA. james.hemp@metrodora.org.
California Institute of Technology · USThe Metropolitan Opera (United States) · USUniversity of Illinois Urbana-Champaign · US

Funding

The molecular mechanism linking respiratory NADH oxidation and virulence in Staphylococcus aureusR01AI148160 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI GENNIS, ROBERT B · 2020 to 2024
$2.6M
NIAID NIH HHS R01 AI148160
6 · The paper itself

Abstract

Cytochrome bd-type oxygen reductases (cytbd) belong to one of three enzyme superfamilies that catalyze oxygen reduction to water. They are widely distributed in Bacteria and Archaea, but the full extent of their biochemical diversity is unknown. Here we used phylogenomics to identify three families and several subfamilies within the cytbd superfamily. The core architecture shared by all members of the superfamily consists of four transmembrane helices that bind two active site hemes, which are responsible for oxygen reduction. While previously characterized cytochrome bd-type oxygen reductases use quinol as an electron donor to reduce oxygen, sequence analysis shows that only one of the identified families has a conserved quinol binding site. The other families are missing this feature, suggesting that they use an alternative electron donor. Multiple gene duplication events were identified within the superfamily, resulting in significant evolutionary and structural diversity. The CydAA' cytbd, found exclusively in Archaea, is formed by the co-association of two superfamily paralogs. We heterologously expressed CydAA' from Caldivirga maquilingensis and demonstrated that it performs oxygen reduction with quinol as an electron donor. Strikingly, CydAA' is the first isoform of cytbd containing only b-type hemes shown to be active when isolated from membranes, demonstrating that oxygen reductase activity in this superfamily is not dependent on heme d.

Indexed as

OxidoreductasesArchaeaArchaeal ProteinsCytochrome b GroupElectron Transport Chain Complex ProteinsEvolution, MolecularOxidation-ReductionOxygenArchaeal ProteinsCytochrome b GroupElectron Transport Chain Complex ProteinsOxidoreductasesOxygen

Identifiers

PMID34145390
PMCPMC8630170
OpenAlexW3172878846

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.