Lipid specificity for membrane mediated partial unfolding of cytochrome c.
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. Experiments with mitoplasts showed that the protein can also be destabilized in its native structure by a biological membrane.
de Jongh
H H
HH
Department of Biochemistry of Membranes, University of Utrecht, The Netherlands.
Ritsema
T
T
Killian
J A
JA
D000818:Animals; D003574:Cytochrome c Group / Q000737:chemistry*; D003903:Deuterium / Q000737:chemistry; D006736:Horses; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008563:Membrane Lipids / Q000737:chemistry*; D008928:Mitochondria / Q000378:metabolism; D010084:Oxidation-Reduction; D010449:Peptide Mapping; D011489:Protein Denaturation; D013057:Spectrum Analysis; D013820:Thermolysin / Q000494:pharmacology
D003574:Cytochrome c Group; D008563:Membrane Lipids; D003903:Deuterium; D013820:Thermolysin