Evidence map›Paper›PMID 16565064›Full record

ArticleBiophysical journal2006

Cytochrome C interaction with cardiolipin/phosphatidylcholine model membranes: effect of cardiolipin protonation.

Galyna P Gorbenko, Julian G Molotkovsky, Paavo K J Kinnunen

Abstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Review
  2. The Increase in the Peroxidase Activity of the CytochromeInternational journal of molecular sciences · 2024
    Article
  3. Article
  4. Composition of the CytochromeMolecules (Basel, Switzerland) · 2023
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Magic angle spinningBiochimica et biophysica acta. Biomembranes · 2017
    Article
  13. Article
  14. Article
  15. Article
  16. Versatility of non-native forms of human cytochrome c: pH and micellar concentration dependence.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013
    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

3 authors.

Galyna P GorbenkoDepartment of Biological and Medical Physics, V.N. Karazin Kharkiv National University, Kharkiv, Ukraine.
Julian G Molotkovsky
Paavo K J Kinnunen

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Resonance energy transfer between anthrylvinyl-labeled phosphatidylcholine as a donor and heme moiety of cytochrome c (cyt c) as an acceptor has been employed to explore the protein binding to model membranes, composed of phosphatidylcholine and cardiolipin (CL). The existence of two types of protein-lipid complexes has been hypothesized where either deprotonated or partially protonated CL molecules are responsible for cyt c attachment to bilayer surface. To quantitatively describe cyt c membrane binding, the adsorption model based on scaled particle and double layer theories has been employed, with potential-dependent association constants being treated as a function of acidic phospholipid mole fraction, degree of CL protonation, ionic strength, and surface coverage. Multiple arrays of resonance energy transfer data obtained under conditions of varying pH, ionic strength, CL content, and protein/lipid molar ratio have been analyzed in terms of the model of energy transfer in two-dimensional systems combined with the adsorption model allowing for area exclusion and electrostatic effects. The set of recovered model parameters included effective protein charge, intrinsic association constants, and heme distance from the bilayer midplane for both types of protein-lipid complexes. Upon increasing CL mole fraction from 10 to 20 mol % (the value close to that characteristic of the inner mitochondrial membrane), the binding equilibrium dramatically shifted toward cyt c association with partially protonated CL species. The estimates of heme distance from bilayer center suggest shallow bilayer location of cyt c at physiological pH, whereas at pH below 6.0, the protein tends to insert into membrane core.

Indexed as

Models, BiologicalCardiolipinsCytochromes cFluorescence Resonance Energy TransferFluorescent DyesHydrogen-Ion ConcentrationLipid BilayersOsmolar ConcentrationPhosphatidylcholinesProtonsCardiolipinsCytochromes cFluorescent DyesLipid BilayersPhosphatidylcholinesProtons

Identifiers

PMID16565064
PMCPMC1459516

What OpenQuestion holds

Textmetadata
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.