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Cytochrome-c-lipid interactions studied by resonance Raman and p-31 NMR-spectroscopy - correlation between the conformational-changes of the protein and the lipid bilayer
Citation key ISI:A1991GF61400025
Author Heimburg, T and Hildebrandt, P and Marsh, D
Pages 9084-9089
Year 1991
ISSN 0006-2960
Address 1155 16TH ST, NW, WASHINGTON, DC 20036
Journal Biochemistry
Volume 30
Number 37
Month SEP 17
Abstract The interaction of cytochrome c with negatively charged lipids has been studied by resonance Raman spectroscopy of the protein heme group and P-31 NMR of the phospholipid headgroups. The gel-to-fluid-phase transition of dimyristoylphosphatidylglycerol induces shifts in the conformational and coordination equilibria of the bound cytochrome c, as recorded by the resonance Raman spectra in the fingerprint and marker band regions. Conformational and coordination shifts of the bound cytochrome are also induced on admixture of dioleoylglycerol or dioleoylphosphatidylcholine with dioleoylphosphatidylglycerol. In the case of dioleoylglycerol, significant changes take place even at levels as low as 5 mol \%. Binding of cytochrome c induces or increases the content of near isotropically diffusing lipid registered by the P-31 NMR spectra of the different lipids studied. Admixture of dioleoylglycerol also increases the bilayer curvature of dioleoylphosphatidylglycerol, inducing an inverted hexagonal phase at 50 mol \% concentration; the tendency to spontaneous curvature in the lipid appears to relax the conformational change detected in the protein.
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