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- W2912973896 abstract "Fluorescence, visible circular dichroism, absorption and resonance Raman spectroscopy were combined to explore structural changes of ferricytochrome c upon its binding to cardiolipin containing liposomes (20% 1,1’,1,2’-tetraoleyolcardiolipin (TOCL) and 80% 1,2-deoleyol-sn-glycero-3-phosphocholine (DOPC)) at acidic pH (6.5). According to earlier work of Kawai et al., cytochrome c binding at this pH is governed by interactions between the phosphate head groups of cardiolipin and amino acid side chains of the so-called L-site which contains the charged residues K22, K25, K27 and potentially H26 and H33. We found that L-site binding causes a conformational change that involves a change of the protein's ligation and spin state. We measured spectroscopic responses to an increasing number of cardiolipin containing liposomes in the absence and presence of NaCl. The latter was found to mostly inhibit protein binding already with 50 mM concentration. The inhibition effect was quantitatively reproduced by applying the electrostatic theory of Heimburg and Marsh. A comparison with corresponding spectroscopic response data obtained at pH 7.4 reveal major differences in that the latter involves hydrophobic binding followed by a conformational change that is electrostatically driven, which we identify with the earlier proposed A-site binding." @default.
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- W2912973896 date "2019-02-01" @default.
- W2912973896 modified "2023-09-28" @default.
- W2912973896 title "pH Induced Switch between Different Modes of Cytochrome C Binding to Cardiolipin Containing Liposomes" @default.
- W2912973896 doi "https://doi.org/10.1016/j.bpj.2018.11.265" @default.
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