Association of ferri- and ferro-cytochrome c with lipid multilayers: a 31P solid-state NMR study

M. C. Waltham, B. A. Cornell, R. Smith

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Abstract

The 31P nuclear magnetic resonance anisotropies of dispersions of diacylphosphatidic acid and diacylphosphatidylserine were slightly increased in the presence of cytochrome c: no increase was observed with cardiolipin. However, the 31P spin-lattice relaxation times (T1) for all of these lipids were reduced markedly by the protein. As similar effects were observed with ferri-cytochrome c and with the reduced protein, which is diamagnetic, we suggest that the changes in T1 reflect a reduction in the spectral density of fast motions for the lipid headgroups attendant on binding of protein, rather than paramagnetic relaxation of the phosphorus nuclear spin.

Original languageEnglish
Pages (from-to)451-456
Number of pages6
JournalBiochimica et Biophysica Acta - Biomembranes
Volume862
Issue number2
DOIs
Publication statusPublished - 17 Nov 1986
Externally publishedYes

Keywords

  • P-NMR
  • Cardiolipin
  • Cytochrome c
  • Lipid-protein interaction
  • Phosphatidic acid
  • Phosphatidylserine

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