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Förster Resonance Energy Transfer Study of Cytochrome c-Lipid Interactions
Galyna P Gorbenko1, Valeriya Trusova2, Julian G Molotkovsky3
1Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University, 4 Svobody Sq., Kharkiv, 61022, Ukraine. galyna.p.gorbenko@karazin.ua.
Journal of Fluorescence
|September 8, 2017
Summary
Cytochrome c (cyt c) specifically binds to cardiolipin in mitochondrial membranes. This interaction, studied using Förster resonance energy transfer (FRET), reveals higher adsorption and deeper insertion with cardiolipin, impacting electron transfer and apoptosis.
Area of Science:
- Biochemistry
- Biophysics
- Cell Biology
Background:
- Mitochondrial cytochrome c (cyt c) is vital for electron transport and apoptosis.
- Specific interactions between cyt c and cardiolipin (CL), a mitochondrial membrane lipid, are critical for its functions.
Purpose of the Study:
- To quantitatively characterize the binding of cyt c to model membranes composed of phosphatidylcholine (PC) mixed with other lipids (phosphatidylglycerol, phosphatidylserine, or CL).
- To investigate the specificity of cyt c interactions with cardiolipin using Förster resonance energy transfer (FRET).
Main Methods:
- Utilized Förster resonance energy transfer (FRET) with an anthrylvinyl-labeled phosphatidylcholine donor and the heme moiety of cyt c as the acceptor.
- Employed a model of energy transfer in two-dimensional systems combined with the scaled particle adsorption model for data analysis.
Main Results:
- Demonstrated specific binding of cyt c to cardiolipin-containing model membranes.
- Observed higher adsorption potential and deeper insertion of cyt c into lipid bilayers enriched with cardiolipin.
Conclusions:
- Cytochrome c exhibits specific interactions with cardiolipin, distinct from its interactions with other phospholipids.
- These specific interactions are crucial for the functional roles of cyt c within the mitochondria.
