Electrochemistry of cytochrome c immobilized on cardiolipin-modified electrodes: A probe for protein–lipid interactions. Perhirin, A., Kraffe, E., Marty, Y., Quentel, F., Elies, P., & Gloaguen, F. Biochimica et Biophysica Acta (BBA)-General Subjects, 1830(3):2798--2803, 2013.
Electrochemistry of cytochrome c immobilized on cardiolipin-modified electrodes: A probe for protein–lipid interactions [link]Paper  doi  abstract   bibtex   
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 (E-1/2) and electron transfer rate constant (k(ET)). 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 k(ET) value (\textgreater300 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. (C) 2013 Elsevier B.V. All rights reserved.
@article{perhirin_electrochemistry_2013,
	title = {Electrochemistry of cytochrome c immobilized on cardiolipin-modified electrodes: {A} probe for protein–lipid interactions},
	volume = {1830},
	issn = {0304-4165},
	shorttitle = {Electrochemistry of cytochrome c immobilized on cardiolipin-modified electrodes},
	url = {http://www.sciencedirect.com/science/article/pii/S0304416512003558},
	doi = {10.1016/j.bbagen.2012.12.009},
	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 (E-1/2) and electron transfer rate constant (k(ET)). 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 k(ET) value ({\textgreater}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. (C) 2013 Elsevier B.V. All rights reserved.},
	number = {3},
	urldate = {2015-03-09TZ},
	journal = {Biochimica et Biophysica Acta (BBA)-General Subjects},
	author = {Perhirin, Antoine and Kraffe, Edouard and Marty, Yanic and Quentel, François and Elies, Philippe and Gloaguen, Frederic},
	year = {2013},
	keywords = {ACL, Cardiolipin, Cytochrome c, E1, E2, Electron transfer, Fatty acid chain, Lipid anchorage, Voltammetry, WOS},
	pages = {2798--2803}
}

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