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- W2013947862 abstract "Cytochrome c is involved in triggering apoptosis in the mitochondria. In order to understand this initiation process of apoptosis, the interactions between cytochrome c and anionic lipid surfaces must be thoroughly characterized. It is well known that cytochrome c adopts partially unfolded conformations on cardiolipin containing liposomes. We examined the binding of cytochrome c to liposomes with different cardiolipin content by measuring the W59 fluorescence as a function of liposome concentration. Surprisingly, the thus obtained binding isotherms indicate a biphasic binding process, which are likely to correspond to different cardiolipin binding sites. Liposome concentrations associated with these binding sites were further investigated by far UV and visible CD as well as by absorption spectroscopy.The initial data obtained indicates that upon binding to cardiolipin complexes, cytochrome c adopts a nonnative state. This conformation is a low spin hexacoordinated state where the heme is ligated to H33 and H18. The far UV CD spectra shows that the protein retains its α-helical content regardless of CL binding, which is characteristic of native cytochrome c. The W59 signal in the near UV CD spectra disappears, indicating a more open protein conformation. This supports our fluorescence data which show an increase in fluorescence intensity as the W59 moves farther away from the heme. Soret band CD simulations also indicate an intermediate state upon protein binding to CL complexes. Data obtained from ultracentrifugation and gel electrophoresis experiments indicate a nonreversible mode of cytochrome c and liposome interactions, which might be due to the insertion of the lipids' hydrophobic tail into the protein crevice." @default.
- W2013947862 created "2016-06-24" @default.
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- W2013947862 date "2013-01-01" @default.
- W2013947862 modified "2023-09-27" @default.
- W2013947862 title "Cytochrome C Binding to Liposomal Surfaces" @default.
- W2013947862 doi "https://doi.org/10.1016/j.bpj.2012.11.3118" @default.
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