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• W2004037237 abstract "We attempted to evaluate the affinity of the anionic phospholipids to cytochrome c by means of surface plasmon resonance (SPR) technique and to correlate it with the cytochrome c active site alterations and peroxidase activity. Our experiments showed a strong interdependence between the phospholipid fatty acid saturation degree, the active site structure alterations and peroxidase activity of the cytochrome c phospholipid complex. Cytochrome c peroxidase activity and Trp59 fluorescence increase in the sequence of phosphatidyl choline (PC) → phosphatidylserine (PS) → cardiolipin (CL) → phosphatidic acid (PA). The association constant ( K a ) increased in the sequence PC → PA → PS → CL. The SPR spectroscopy data shows that K a is independent of lipid saturation degree, but correlates with phospholipid negative charge value." @default.
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• W2004037237 date "2008-12-04" @default.
• W2004037237 modified "2023-10-10" @default.
• W2004037237 title "Evaluation of cytochrome<i>c</i>affinity to anionic phospholipids by means of surface plasmon resonance" @default.
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• W2004037237 doi "https://doi.org/10.1016/j.febslet.2008.11.029" @default.
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