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super(1)H-n.m.r. evaluation of the ferricytochrome c-cardiolipin interaction. Effect of superoxide radicals

The interaction between ferricytochrome c and cardiolipin was investigated by super(1)H.n.m.r. at 270 MHz. Peroxidation of cardiolipin by superoxide radical ions drastically decreases the protein binding to this phospholipid. The implications of this finding, and the likelihood of the ternary cytoch...

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Bibliographic Details
Published in:Biochemical journal 1990-01, Vol.265 (1), p.227-232
Main Authors: Soussi, B, Bylund-Fellenius, A-C, Schersten, T, Aangstroem, J
Format: Article
Language:English
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Summary:The interaction between ferricytochrome c and cardiolipin was investigated by super(1)H.n.m.r. at 270 MHz. Peroxidation of cardiolipin by superoxide radical ions drastically decreases the protein binding to this phospholipid. The implications of this finding, and the likelihood of the ternary cytochrome c-cardiolipin-cytochrome c oxidase complex, for the binding of cytochrome c to cytochrome c oxidase in vivo, are discussed in relation to peroxidative damage following ischaemia and reperfusion.
ISSN:0264-6021