Probing the Functional Relevance of the Tip-to-Tip Acrab-Tolc Structural Model

Abstract

the structural and dynamic changes affecting the protein as it associates with different types of lipid bilayers. We previously reported that the activation of lipid peroxidase activity occurs with the native fold largely preserved. Spectral signatures of the membrane-bound protein are clearly distinct from those of denatured cytochrome c. Remarkably, localized spectral changes indicate selective dynamics in the protein-lipid complex that respond to the membrane fluidity. Different dynamic modulations occur dependent on the lipid composition, in terms of acyl chain and headgroup type. Thus, lipids act not only as preferred substrates but also as crucial dynamic regulators of this lethal interplay of proteins and lipids at the mitochondrial inner membrane.