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

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

doi:10.1016/0005-2736(86)90250-6

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

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

Research output: Contribution to journal › Article › Research › peer-review

19 Citations (Scopus)

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 language	English
Pages (from-to)	451-456
Number of pages	6
Journal	BBA Biomembranes
Volume	862
Issue number	2
DOIs	https://doi.org/10.1016/0005-2736(86)90250-6
Publication status	Published - 17 Nov 1986
Externally published	Yes

Keywords

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

Access to Document

10.1016/0005-2736(86)90250-6

Cite this

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

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.",

keywords = "P-NMR, Cardiolipin, Cytochrome c, Lipid-protein interaction, Phosphatidic acid, Phosphatidylserine",

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T1 - Association of ferri- and ferro-cytochrome c with lipid multilayers

T2 - a 31P solid-state NMR study

AU - Waltham, M. C.

AU - Cornell, B. A.

AU - Smith, R.

PY - 1986/11/17

Y1 - 1986/11/17

N2 - 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.

AB - 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.

KW - P-NMR

KW - Cardiolipin

KW - Cytochrome c

KW - Lipid-protein interaction

KW - Phosphatidic acid

KW - Phosphatidylserine

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DO - 10.1016/0005-2736(86)90250-6

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AN - SCOPUS:0023051994

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