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

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 value...

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Published inBiochimica et biophysica acta Vol. 1830; no. 3; pp. 2798 - 2803
Main Authors Perhirin, Antoine, Kraffe, Edouard, Marty, Yanic, Quentel, François, Elies, Philippe, Gloaguen, Frederic
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.03.2013
Elsevier
Subjects
Analytical chemistry
Biochemistry, Molecular Biology
Biodiversity and Ecology
Carbon - chemistry
Cardiolipin
Cardiolipins - chemistry
Chemical Sciences
Cytochrome c
Cytochromes c - chemistry
Electrochemical Techniques
electrochemistry
Electrodes
Electron transfer
Electron Transport
Environmental Sciences
Fatty acid chain
fatty acids
glassy carbon electrode
Hydrophobic and Hydrophilic Interactions
hydrophobic bonding
Immobilized Proteins - chemistry
ionic strength
Kinetics
Life Sciences
Lipid anchorage
Microscopy, Atomic Force
Osmolar Concentration
Oxidation-Reduction
phosphatidylcholines
Phosphatidylcholines - chemistry
proteins
Surface Properties
Voltammetry
Cytochrome c
Electron transfer
Lipid anchorage
Voltammetry
Cardiolipin
Fatty acid chain
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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 (>300s−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. ► PC/CL supported films were used to study electrochemistry of immobilized cyt c. ► AC voltammetry experiments showed two subpopulations of immobilized cyt c. ► At high ionic strength, only hydrophobically bound cyt c is detected. ► Redox behavior of cyt c depends on the structure of the FA chains carried by CL.
AbstractList 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 (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 (> 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.
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 (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 (> 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.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 (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 (> 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.
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 (>300s−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.
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 (>300s⁻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.
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.
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 (>300s−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. ► PC/CL supported films were used to study electrochemistry of immobilized cyt c. ► AC voltammetry experiments showed two subpopulations of immobilized cyt c. ► At high ionic strength, only hydrophobically bound cyt c is detected. ► Redox behavior of cyt c depends on the structure of the FA chains carried by CL.
Author Quentel, François
Elies, Philippe
Perhirin, Antoine
Marty, Yanic
Kraffe, Edouard
Gloaguen, Frederic
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  fullname: Gloaguen, Frederic
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Issue 3
Keywords Cytochrome c
Electron transfer
Lipid anchorage
Voltammetry
Cardiolipin
Fatty acid chain
Language English
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Snippet Electrochemistry of cytochrome c (cyt c) immobilized on a cardiolipin (CL)/phosphatidylcholine (PC) film supported on a glassy carbon electrode was...
Electrochemistry of cytochrome c (cyt c) immobilized on a cardiolipin (CL) / phosphatidylcholine (PC) film supported on a glassy carbon electrode was...
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SubjectTerms Analytical chemistry
Biochemistry, Molecular Biology
Biodiversity and Ecology
Carbon - chemistry
Cardiolipin
Cardiolipins - chemistry
Chemical Sciences
Cytochrome c
Cytochromes c - chemistry
Electrochemical Techniques
electrochemistry
Electrodes
Electron transfer
Electron Transport
Environmental Sciences
Fatty acid chain
fatty acids
glassy carbon electrode
Hydrophobic and Hydrophilic Interactions
hydrophobic bonding
Immobilized Proteins - chemistry
ionic strength
Kinetics
Life Sciences
Lipid anchorage
Microscopy, Atomic Force
Osmolar Concentration
Oxidation-Reduction
phosphatidylcholines
Phosphatidylcholines - chemistry
proteins
Surface Properties
Voltammetry
Title Electrochemistry of cytochrome c immobilized on cardiolipin-modified electrodes: A probe for protein–lipid interactions
URI https://dx.doi.org/10.1016/j.bbagen.2012.12.009
https://www.ncbi.nlm.nih.gov/pubmed/23266496
https://www.proquest.com/docview/1351607339
https://www.proquest.com/docview/2000082887
https://hal.univ-brest.fr/hal-01130700
Volume 1830
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