Evidence map›Paper›PMID 22248670›Full record

ArticleBiochimica et biophysica acta2012

The roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa(3)-type and the cbb(3)-type cytochrome c oxidases.

Audie K Thompson, Jimmy Gray, Aimin Liu, Jonathan P Hosler

Abstract read
In one paragraph

Article 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 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-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

28 citing papers in PubMed, 63 citations in OpenAlex.

  1. AccA fromChemical science · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Diversity of CytochromeMicroorganisms · 2022
    Review
  6. The CopA2-Type PFrontiers in microbiology · 2021
    Article
  7. Review
  8. Article
  9. PCuThe Journal of biological chemistry · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The copper-deprivation stimulon ofThe Journal of biological chemistry · 2018
    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

4 authors at 1 institution in 1 country.

Audie K ThompsonDepartment of Biochemistry, The University of Mississippi Medical Center, Jackson, MS 39216, USA. akthompson@PVAMU.edu
Jimmy Gray
Aimin Liu
Jonathan P Hosler
University of Mississippi Medical Center · US

Funding

SUBUNIT III AND CYTOCHROME OXIDASE FUNCTIONR01GM056824 · NIGMS · UNIVERSITY OF MISSISSIPPI MEDICAL CENTER · PI HOSLER, JONATHAN P · 1998 to 2007
$1.6M
NIGMS NIH HHS GM 56824NIGMS NIH HHS R01 GM056824
6 · The paper itself

Abstract

The α proteobacter Rhodobacter sphaeroides accumulates two cytochrome c oxidases (CcO) in its cytoplasmic membrane during aerobic growth: a mitochondrial-like aa(3)-type CcO containing a di-copper Cu(A) center and mono-copper Cu(B), plus a cbb(3)-type CcO that contains Cu(B) but lacks Cu(A). Three copper chaperones are located in the periplasm of R. sphaeroides, PCu(A)C, PrrC (Sco) and Cox11. Cox11 is required to assemble Cu(B) of the aa(3)-type but not the cbb(3)-type CcO. PrrC is homologous to mitochondrial Sco1; Sco proteins are implicated in Cu(A) assembly in mitochondria and bacteria, and with Cu(B) assembly of the cbb(3)-type CcO. PCu(A)C is present in many bacteria, but not mitochondria. PCu(A)C of Thermus thermophilus metallates a Cu(A) center in vitro, but its in vivo function has not been explored. Here, the extent of copper center assembly in the aa(3)- and cbb(3)-type CcOs of R. sphaeroides has been examined in strains lacking PCu(A)C, PrrC, or both. The absence of either chaperone strongly lowers the accumulation of both CcOs in the cells grown in low concentrations of Cu(2+). The absence of PrrC has a greater effect than the absence of PCu(A)C and PCu(A)C appears to function upstream of PrrC. Analysis of purified aa(3)-type CcO shows that PrrC has a greater effect on the assembly of its Cu(A) than does PCu(A)C, and both chaperones have a lesser but significant effect on the assembly of its Cu(B) even though Cox11 is present. Scenarios for the cellular roles of PCu(A)C and PrrC are considered. The results are most consistent with a role for PrrC in the capture and delivery of copper to Cu(A) of the aa(3)-type CcO and to Cu(B) of the cbb(3)-type CcO, while the predominant role of PCu(A)C may be to capture and deliver copper to PrrC and Cox11. This article is part of a Special Issue entitled: Biogenesis/Assembly of Respiratory Enzyme Complexes.

Indexed as

Bacterial ProteinsCell MembraneCopperElectron Spin Resonance SpectroscopyElectron Transport Complex IVGene DeletionMolecular ChaperonesOxygenRhodobacter sphaeroidesBacterial ProteinsCopperElectron Transport Complex IVMolecular ChaperonesOxygen

Identifiers

PMID22248670
PMCPMC3336013
OpenAlexW2162393890

What OpenQuestion holds

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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.