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. 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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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.","number":"3","urldate":"2015-03-09TZ","journal":"Biochimica et Biophysica Acta (BBA)-General Subjects","author":[{"propositions":[],"lastnames":["Perhirin"],"firstnames":["Antoine"],"suffixes":[]},{"propositions":[],"lastnames":["Kraffe"],"firstnames":["Edouard"],"suffixes":[]},{"propositions":[],"lastnames":["Marty"],"firstnames":["Yanic"],"suffixes":[]},{"propositions":[],"lastnames":["Quentel"],"firstnames":["François"],"suffixes":[]},{"propositions":[],"lastnames":["Elies"],"firstnames":["Philippe"],"suffixes":[]},{"propositions":[],"lastnames":["Gloaguen"],"firstnames":["Frederic"],"suffixes":[]}],"year":"2013","keywords":"ACL, Cardiolipin, Cytochrome c, E1, E2, Electron transfer, Fatty acid chain, Lipid anchorage, Voltammetry, WOS","pages":"2798--2803","bibtex":"@article{perhirin_electrochemistry_2013,\n\ttitle = {Electrochemistry of cytochrome c immobilized on cardiolipin-modified electrodes: {A} probe for protein–lipid interactions},\n\tvolume = {1830},\n\tissn = {0304-4165},\n\tshorttitle = {Electrochemistry of cytochrome c immobilized on cardiolipin-modified electrodes},\n\turl = {http://www.sciencedirect.com/science/article/pii/S0304416512003558},\n\tdoi = {10.1016/j.bbagen.2012.12.009},\n\tabstract = {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. 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