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Elucidating the mechanism of

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The oxidation of ferrocytochrome c by peroxidized cardiolipin is explained by a Fenton-type reaction.

Our results indicate that this binding is not controlled by the specific sequence of the peptide, but rather by its conformational freedom in solution its freedom when it is in proximity to the substrate.In order to understand the mechansim of peptide–membrane binding, we modified the original peptide (cecropin B1: KWKVFKKIEKMGRNIRNGIV) by attaching a terminal tryptophan residue (cecropin B2: KWKVFKKIEKMGRNIRNGIVW).Both peptides show a large inhibition effect against a wide range of bacteria, compared to naturally occurring peptides. "Elucidating the mechanism of ferrocytochrome c heme disruption by peroxidized cardiolipin." Journal of Biological Inorganic Chemistry, 18, (2013) 137-144. The interaction of peroxidized cardiolipin with ferrocytochrome c induces two kinetically and chemically distinct processes.The first is a rapid oxidation of ferrocytochrome c, followed by a slower, irreversible disruption of heme c.Simultaneously with the heme c disruption, generation of hydroxyl radical is detected by EPR spectroscopy using the spin trapping technique.