Evidence map›Paper›PMID 22079199›Full record

ReviewBiochimica et biophysica acta2012

Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatus.

Seda Ekici, Grzegorz Pawlik, Eva Lohmeyer, Hans-Georg Koch, Fevzi Daldal

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

62 citing papers in PubMed, 101 citations in OpenAlex.

  1. SLC25A3 exports mitochondrial copper to metalate cytochromeProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Cultivation driven transcriptomic changes in the wild-type and mutant strains ofComputational and structural biotechnology journal · 2024
    Article
  5. Article
  6. Article
  7. The structure of the diheme cytochrome cJournal of inorganic biochemistry · 2024
    Article
  8. Ubiquitous genome streamlinedISME communications · 2024
    Article
  9. Article
  10. Interaction of Terminal Oxidases with Amphipathic Molecules.International journal of molecular sciences · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Cryo-EM structures of engineered active bcNature communications · 2021
    Article

2 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 2 countries.

Seda EkiciUniversity of Pennsylvania, Department of Biology, Philadelphia, PA 19104, USA.
Grzegorz Pawlik
Eva Lohmeyer
Hans-Georg Koch
Fevzi Daldal
University of Freiburg · DEUniversity of Pennsylvania · US

Funding

Respiratory Complex III: Supercomplexes and ROS, from Bacteria to HumanR01GM038237 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DALDAL, M. FEVZI · 1987 to 2018
$5.9M
NIGMS NIH HHS GM38239NIGMS NIH HHS R01 GM038237
6 · The paper itself

Abstract

The cbb(3)-type cytochrome c oxidases (cbb(3)-Cox) constitute the second most abundant cytochrome c oxidase (Cox) group after the mitochondrial-like aa(3)-type Cox. They are present in bacteria only, and are considered to represent a primordial innovation in the domain of Eubacteria due to their phylogenetic distribution and their similarity to nitric oxide (NO) reductases. They are crucial for the onset of many anaerobic biological processes, such as anoxygenic photosynthesis or nitrogen fixation. In addition, they are prevalent in many pathogenic bacteria, and important for colonizing low oxygen tissues. Studies related to cbb(3)-Cox provide a fascinating paradigm for the biogenesis of sophisticated oligomeric membrane proteins. Complex subunit maturation and assembly machineries, producing the c-type cytochromes and the binuclear heme b(3)-Cu(B) center, have to be coordinated precisely both temporally and spatially to yield a functional cbb(3)-Cox enzyme. In this review we summarize our current knowledge on the structure, regulation and assembly of cbb(3)-Cox, and provide a highly tentative model for cbb(3)-Cox assembly and formation of its heme b(3)-Cu(B) binuclear center. This article is part of a Special Issue entitled: Biogenesis/Assembly of Respiratory Enzyme Complexes.

Indexed as

AnimalsBacterial ProteinsElectron Transport Complex IVGene Expression Regulation, BacterialHemeHumansMembrane LipidsProtein MultimerizationProtein Structure, QuaternaryProtein SubunitsRhodobacter capsulatusBacterial ProteinsElectron Transport Complex IVHemeMembrane LipidsProtein Subunits

Identifiers

PMID22079199
PMCPMC3304015
OpenAlexW2090800288

What OpenQuestion holds

Textmetadata
LicenceTDM
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.