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Lipid specificity for membrane mediated partial unfolding of cytochrome c
Author(s) -
de Jongh Hh,
Tita Ritsema,
J. Antoinette Killian
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00115-p
Subject(s) - cardiolipin , chemistry , cytochrome c , cytochrome , biochemistry , membrane , hemeprotein , heme , inner mitochondrial membrane , membrane protein , biophysics , phospholipid , mitochondrion , biology , enzyme
In this study we investigated the lipid specificity for destabilization of the native structure of horse heart cytochrome c by model membranes. From (i) the enhanced release of deuterium from deuterium‐labelled cytochrome c and (ii) the increased proteolytic digestion of the protein in the presence of anionic lipids, it was concluded that these lipids are able to destabilize the native structure of cytochrome c . Changes in the absorbance at 695 nm indicated that the destabilization was accompanied by a diminished ligation of Met‐80 to the heme. Beef heart cardiolipin was found to be more effective than DOPS, DOPG or DOPA, while no protein destabilization was observed in the presence of the zwitterionic lipid DOPC or, surprisingly, in the presence of E. coli cardiolipin. Experimnts with mitoplasts showed that the protein can also be destabilized in its native structure by a biological membrane.