Evidence map›Paper›PMID 17614790›Full record

ArticleThe Biochemical journal2007

Cytochrome c impaled: investigation of the extended lipid anchorage of a soluble protein to mitochondrial membrane models.

Erta Kalanxhi, Carmichael J A Wallace

Abstract read
In one paragraph

Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Binding of S. cerevisiae iso-1 cytochrome c and its surface lysine-to-alanine variants to cardiolipin: charge effects and the role of the lipid to protein ratio.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. The key role played by charge in the interaction of cytochrome c with cardiolipin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017
    Article
  12. Role of Cardiolipin in Mitochondrial Signaling Pathways.Frontiers in cell and developmental biology · 2017
    Review
  13. Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons.Journal of the American Chemical Society · 2016
    Article
  14. The nitrite reductase activity of horse heart carboxymethylated-cytochrome c is modulated by cardiolipin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Article
  15. Review
  16. Article
  17. Article
  18. Cardiolipin Interactions with Proteins.Biophysical journal · 2015
    Article
  19. Immobilized cytochrome c bound to cardiolipin exhibits peculiar oxidation state-dependent axial heme ligation and catalytically reduces dioxygen.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    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

2 authors.

Erta KalanxhiDepartment of Biochemistry and Molecular Biology, Dalhousie University, Halifax, NS, Canada B3H1X5.
Carmichael J A Wallace

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyt c (cytochrome c) has been traditionally envisioned as rapidly diffusing in two dimensions at the surface of the mitochondrial inner membrane when not engaged in redox reactions with physiological partners. However, the discovery of the extended lipid anchorage (insertion of an acyl chain of a bilayer phospholipid into the protein interior) suggests that this may not be exclusively the case. The physical and structural factors underlying the conformational changes that occur upon interaction of ferrous cyt c with phospholipid membrane models have been investigated by monitoring the extent of the spin state change that result from this interaction. Once transiently linked by electrostatic forces between basic side chains and phosphate groups, the acyl chain entry may occur between two parallel hydrophobic polypeptide stretches that are surrounded by positively charged residues. Alteration of these charges, as in the case of non-trimethylated (TML72K) yeast cyt c and Arg91Nle horse cyt c (where Nle is norleucine), led to a decline in the binding affinity for the phospholipid liposomes. The electrostatic association was sensitive to ionic strength, polyanions and pH, whereas the hydrophobic interactions were enhanced by conformational changes that contributed to the loosening of the tertiary structure of cyt c. In addition to proposing a mechanistic model for the extended lipid anchorage of cyt c, we consider what, if any, might be the physiological relevance of the phenomenon.

Indexed as

Models, BiologicalAnimalsCytochromes cHydrophobic and Hydrophilic InteractionsMembrane ProteinsMitochondrial MembranesModels, MolecularPhospholipidsProtein BindingProtein ConformationSolubilityStatic ElectricityYeastsCytochromes cMembrane ProteinsPhospholipids

Identifiers

PMID17614790
PMCPMC2049027

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.