The Puzzling Problem of Cardiolipin Membrane-Cytochrome c Interactions: A Combined Infrared and Fluorescence Study

The interaction of cytochrome c (cyt c) with natural and synthetic membranes is known to be a complex phenomenon, involving both protein and lipid conformational changes. In this paper, we combined infrared and fluorescence spectroscopy to study the structural transformation occurring to the lipid network of cardiolipin-containing large unilamellar vesicles (LUVs). The data, collected at increasing protein/lipid ratio, demonstrate the existence of a multi-phase process, which is characterized by: (i) the interaction of cyt c with the lipid polar heads; (ii) the lipid anchorage of the protein on the membrane surface; and (iii) a long-distance order/disorder transition of the cardiolipin acyl chains. Such effects have been quantitatively interpreted introducing specific order parameters and discussed in the frame of the models on cyt c activity reported in literature.

Automated summary

This study used infrared and fluorescence spectroscopy to investigate the interaction of cytochrome c with cardiolipin, revealing a multi-phase process involving protein-lipid interaction, protein anchorage on the membrane surface, and a long-distance order/disorder transition of cardiolipin acyl chains. These effects were quantitatively interpreted with specific order parameters and discussed in the context of previous models on cytochrome c activity.