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Electrochemistry of cytochrome c immobilized on cardiolipin-modified electrodes: a probe for protein – lipid interactions

Abstract : Electrochemistry of cytochrome c (cyt c) immobilized on a cardiolipin (CL) / phosphatidylcholine (PC) film supported on a glassy carbon electrode was investigated using variable-frequency AC voltammetry. At low ionic strength, we observed two redox-active subpopulations characterized by distinct values of potential (E1/2) and electron transfer rate constant (kET). At high ionic strength, only one subpopulation was detected, consistent with the existence of very stable cyt c – CL adducts, most probably formed by hydrophobic interactions between the protein and the fatty acid (FA) chains carried by CL. This subpopulation exhibits a comparatively high kET value (> 300 s−1) apparently changing with the structure of the FA chains of CL, i.e. 18:2(n-6) or 14:0. Our study suggests that electrochemistry can be a useful technique for probing protein − lipid interactions, and more particularly the role played by the specific structure of the FA chains of CL on cyt c binding.
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Antoine Perhirin, Edouard Kraffe, Yanic Marty, Francois Quentel, Philippe Elies, et al.. Electrochemistry of cytochrome c immobilized on cardiolipin-modified electrodes: a probe for protein – lipid interactions. BBA - Biochimica et Biophysica Acta, Elsevier, 2013, 1830 (3), pp.2798-2803. ⟨10.1016/j.bbagen.2012.12.009⟩. ⟨hal-01130700⟩

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