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Becoming a peroxidase: cardiolipin-induced unfolding of cytochrome c. | LitMetric

Becoming a peroxidase: cardiolipin-induced unfolding of cytochrome c.

J Phys Chem B

Department of Chemistry, Dartmouth College, Hanover, New Hampshire 03755, United States.

Published: October 2013

Interactions of cytochrome c (cyt c) with a unique mitochondrial glycerophospholipid cardiolipin (CL) are relevant for the protein's function in oxidative phosphorylation and apoptosis. Binding to CL-containing membranes promotes cyt c unfolding and dramatically enhances the protein's peroxidase activity, which is critical in early stages of apoptosis. We have employed a collection of seven dansyl variants of horse heart cyt c to probe the sequence of steps in this functional transformation. Kinetic measurements have unraveled four distinct processes during CL-induced cyt c unfolding: rapid protein binding to CL liposomes; rearrangements of protein substructures with small unfolding energies; partial insertion of the protein into the lipid bilayer; and extensive protein restructuring leading to "open" extended structures. While early rearrangements depend on a hierarchy of foldons in the native structure, the later process of large-scale unfolding is influenced by protein interactions with the membrane surface. The opening of the cyt c structure exposes the heme group, which enhances the protein's peroxidase activity and also frees the C-terminal helix to aid in the translocation of the protein through CL membranes.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3979359PMC
http://dx.doi.org/10.1021/jp402104rDOI Listing

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