Forster Resonance Energy Transfer Study of Cytochrome c-Lipid Interactions

被引:5
|
作者
Gorbenko, Galyna P. [1 ]
Trusova, Valeriya [1 ]
Molotkovsky, Julian G. [2 ]
机构
[1] Kharkov Natl Univ, Dept Nucl & Med Phys, 4 Svobody Sq, UA-61022 Kharkov, Ukraine
[2] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, 16-10 Miklukho Maklaya Str, Moscow 117997, Russia
关键词
Cytochrome c; Cardiolipin; Protein-lipid interactions; Forster resonance energy transfer; LOCALLY PLANAR SURFACES; BIOLOGICAL-MEMBRANES; P-31; NMR; CONFORMATIONAL-CHANGES; PHOSPHOLIPID-BILAYERS; ADSORPTION EQUILIBRIA; TRANSMEMBRANE HELIX; GLOBULAR-PROTEINS; FERRICYTOCHROME-C; CARDIOLIPIN;
D O I
10.1007/s10895-017-2176-1
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Specific interactions between a mitochondrial hemoprotein cytochrome c (cyt c) and cardiolipin, a lipid component of mitochondrial membrane, are crucial to electron shuttling and apoptotic activities of this protein. In the present study the Forster resonance energy transfer (FRET) between anthrylvinyl-labeled phosphatidylcholine as a donor and heme moiety of cyt c as an acceptor was employed to give a quantitative characterization of the protein binding to the model membranes from the mixtures of phosphatidylcholine (PC) with phosphatidylglycerol (PG), phosphatidylserine (PS) or cardiolipin (CL) in different molar ratios. The multiple arrays of the FRET data were globally analyzed in terms of the model of energy transfer in two-dimensional systems combined with the scaled particle adsorption model. The arguments in favor of the specificity of cyt c interactions with CL were obtained, including the higher adsorption potential and the deeper protein insertion in the lipid bilayer.
引用
收藏
页码:79 / 88
页数:10
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