University of Hertfordshire

Standard

Preferential association of apocytochrome c with negatively charged phospholipids in mixed model membranes. / Rietveld, A.; Berkhout, Theo; Roenhorst, A.; Marsh, D.; de Kruijff, Ben.

In: Biochimica et Biophysica Acta - Biomembranes, Vol. 858, No. 1, 13.06.1986, p. 38-46.

Research output: Contribution to journalArticle

Harvard

APA

Vancouver

Author

Rietveld, A. ; Berkhout, Theo ; Roenhorst, A. ; Marsh, D. ; de Kruijff, Ben. / Preferential association of apocytochrome c with negatively charged phospholipids in mixed model membranes. In: Biochimica et Biophysica Acta - Biomembranes. 1986 ; Vol. 858, No. 1. pp. 38-46.

Bibtex

@article{8b1f370b49cc42478bfb3f3cdc3fa0bd,
title = "Preferential association of apocytochrome c with negatively charged phospholipids in mixed model membranes",
abstract = "The mitochondrial precursor protein, apocytochrome c, binds to model membranes containing negatively charged phospholipids (Rietveld, A., Sijens, R., Verkleij, A.J. and Kruijff, B. (1983) EMBO J. 2, 907-913). In the present paper the effect of apocytochrome c on the lipid distribution in model membranes, consisting of neutral and acidic phospholipids, is examined. Both ESR and fluorescence energy transfer experiments show that the protein preferentially interacts with the negatively charged phospholipid in the mixed model membranes. Semi-quantitative analysis of the fluorescence energy transfer from the single tryptophan in apocytochrome c to the parinaric acid in phosphatidylserine or phosphatidylcholine in mixed bovine brain phosphatidylserine/egg phosphatidylcholine vesicles reveals and average donor-acceptor distance of 22-26 A and 26-30 A for phosphatidylserine and phosphatidylcholine, respectively. In addition, these experiments demonstrate that this preferential interaction does not induce the separation of large domains enriched in complexes of apocytochrome c with negatively charged phospholipids and domains enriched in neutral lipids.",
keywords = "Apoproteins, Biological Transport, Cytochrome c Group, Cytochromes c, Electron Spin Resonance Spectroscopy, Energy Transfer, Membrane Fluidity, Membrane Lipids, Phosphatidylcholines, Phosphatidylglycerols, Phosphatidylserines, Phospholipids, Spectrometry, Fluorescence, Tryptophan",
author = "A. Rietveld and Theo Berkhout and A. Roenhorst and D. Marsh and {de Kruijff}, Ben",
year = "1986",
month = "6",
day = "13",
doi = "10.1016/0005-2736(86)90289-0",
language = "English",
volume = "858",
pages = "38--46",
journal = "Biochimica et Biophysica Acta - Biomembranes",
issn = "0005-2736",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Preferential association of apocytochrome c with negatively charged phospholipids in mixed model membranes

AU - Rietveld, A.

AU - Berkhout, Theo

AU - Roenhorst, A.

AU - Marsh, D.

AU - de Kruijff, Ben

PY - 1986/6/13

Y1 - 1986/6/13

N2 - The mitochondrial precursor protein, apocytochrome c, binds to model membranes containing negatively charged phospholipids (Rietveld, A., Sijens, R., Verkleij, A.J. and Kruijff, B. (1983) EMBO J. 2, 907-913). In the present paper the effect of apocytochrome c on the lipid distribution in model membranes, consisting of neutral and acidic phospholipids, is examined. Both ESR and fluorescence energy transfer experiments show that the protein preferentially interacts with the negatively charged phospholipid in the mixed model membranes. Semi-quantitative analysis of the fluorescence energy transfer from the single tryptophan in apocytochrome c to the parinaric acid in phosphatidylserine or phosphatidylcholine in mixed bovine brain phosphatidylserine/egg phosphatidylcholine vesicles reveals and average donor-acceptor distance of 22-26 A and 26-30 A for phosphatidylserine and phosphatidylcholine, respectively. In addition, these experiments demonstrate that this preferential interaction does not induce the separation of large domains enriched in complexes of apocytochrome c with negatively charged phospholipids and domains enriched in neutral lipids.

AB - The mitochondrial precursor protein, apocytochrome c, binds to model membranes containing negatively charged phospholipids (Rietveld, A., Sijens, R., Verkleij, A.J. and Kruijff, B. (1983) EMBO J. 2, 907-913). In the present paper the effect of apocytochrome c on the lipid distribution in model membranes, consisting of neutral and acidic phospholipids, is examined. Both ESR and fluorescence energy transfer experiments show that the protein preferentially interacts with the negatively charged phospholipid in the mixed model membranes. Semi-quantitative analysis of the fluorescence energy transfer from the single tryptophan in apocytochrome c to the parinaric acid in phosphatidylserine or phosphatidylcholine in mixed bovine brain phosphatidylserine/egg phosphatidylcholine vesicles reveals and average donor-acceptor distance of 22-26 A and 26-30 A for phosphatidylserine and phosphatidylcholine, respectively. In addition, these experiments demonstrate that this preferential interaction does not induce the separation of large domains enriched in complexes of apocytochrome c with negatively charged phospholipids and domains enriched in neutral lipids.

KW - Apoproteins

KW - Biological Transport

KW - Cytochrome c Group

KW - Cytochromes c

KW - Electron Spin Resonance Spectroscopy

KW - Energy Transfer

KW - Membrane Fluidity

KW - Membrane Lipids

KW - Phosphatidylcholines

KW - Phosphatidylglycerols

KW - Phosphatidylserines

KW - Phospholipids

KW - Spectrometry, Fluorescence

KW - Tryptophan

U2 - 10.1016/0005-2736(86)90289-0

DO - 10.1016/0005-2736(86)90289-0

M3 - Article

C2 - 3011094

VL - 858

SP - 38

EP - 46

JO - Biochimica et Biophysica Acta - Biomembranes

JF - Biochimica et Biophysica Acta - Biomembranes

SN - 0005-2736

IS - 1

ER -