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A mitochondria‐targeted antioxidant can inhibit peroxidase activity of cytochrome c by detachment of the protein from liposomes
Author(s) -
Firsov Alexander M.,
Kotova Elena A.,
Orlov Viktor N.,
Antonenko Yuri N.,
Skulachev Vladimir P.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12319
Subject(s) - cardiolipin , cytochrome c , cytochrome c peroxidase , liposome , chemistry , mitochondrion , peroxidase , antioxidant , biochemistry , coenzyme q – cytochrome c reductase , cytochrome , cytochrome c1 , inner mitochondrial membrane , enzyme , membrane , phospholipid
Interaction of cytochrome c with cardiolipin converts this respiratory chain electron‐transfer protein into a peroxidase, supposedly involved in mitochondria‐mediated apoptosis initiation. Liposome membrane permeabilization provoked by peroxidase activity of the cytochrome c /cardiolipin complex has been previously shown to be suppressed by conventional antioxidants. Here, the mitochondria‐targeted antioxidant SkQ1 (plastoquinonyl‐decyl‐triphenylphosphonium) was found to strongly inhibit both cytochrome c /cardiolipin peroxidase activity and the permeabilization of liposomes composed of phosphatidylcholine and cardiolipin. A number of binding assays revealed a significant inhibiting effect of SkQ1 on cytochrome c binding to liposomes, thus suggesting that SkQ1‐mediated protection of liposomes from the cytochrome c /H 2 O 2 ‐induced permeabilization involved distortion of the cytochrome c ‐membrane binding. It is suggested that antioxidant and antiapoptotic effects of alkyltriphenylphosphonium cations can be related to the prevention of cytochrome c /cardiolipin interaction.