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• W2085754089 abstract "Cytochrome c exhibits peroxidase activity on diphenylacetaldehyde (DPAA) and 3-methylacetoacetone (MAA), which is greatly affected by the presence and nature of charged liposome or micelle interfaces interacting with the enzyme. The ferricytochrome c reaction with DPAA is accelerated when the enzyme is attached to negatively charged interfaces. Whatever the medium, bulk solution or negatively charged dicetylphosphate (DCP), phosphatidylcoline/phosphatidylethanolamine/cardiolipin (PC/PE/CL) liposomes, this chemiluminescent reaction is accompanied by reduction of cytochrome c to its ferrous form. In turn, MAA is oxidized by cytochrome c exclusively when bound to DCP liposomes. Contrary to DPAA oxidation, the MAA reaction is followed by bleaching of cytochrome c, reflecting damage to the hemeprotein chromophore. The cytochrome-c-catalyzed oxidation of either DPAA or MAA leads to concomitant disappearance of the enzyme charge transfer absorption band at 695 nm. This suggests that the peroxidase activity of cytochrome c involves substrate-induced loss of the methionine ligand at the iron sixth coordination position, which is favored by interaction of cytochrome c with negatively charged interfaces. Accordingly, a decrease and blue shift of the charge transfer band could be observed in cytochrome-c-containing negatively charged DCP, PC/PE/CL liposomes or lysophosphatidylethanolamine micelles in the presence of DPAA or MAA." @default.
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• W2085754089 date "1998-09-01" @default.
• W2085754089 modified "2023-10-18" @default.
• W2085754089 title "Liposome effect on the cytochrome c-catalyzed peroxidation of carbonyl substrates to triplet species" @default.
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• W2085754089 doi "https://doi.org/10.1016/s0891-5849(98)00082-3" @default.
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