Increased thermal stability of pigment-protein complexes of pea thylakoids following catalytic hydrogenation of membrane lipids

Peter G. Thomas, Peter J. Dominy, L. Vígh, Azad R. Mansourian, Peter J. Quinn, W. Patrick Williams

Research output: Contribution to journalArticle

82 Citations (Scopus)

Abstract

The membrane lipids of pea thylakoids were hydrogenated in situ using the homogeneous catalyst palladiumdi-(sodium alizazine monosulphonate). Following hydrogenation, particle-free patches corresponding to phase-separated gel-phase lipids were observed in the fracture-faces of thylakoid membranes. Freeze-fracture studies on samples of hydrogenated thylakoids incubated at elevated temperatures indicated that hydrogenation reduces the tendency of the heated membranes to destack and vesiculate at higher temperatures. Measurements of chlorophyll a fluorescence emission and the thermal properties of hydrogenated thylakoids suggest that the hydrogenation process also leads to an increase in the thermal stability of pigment-protein complexes of the Photosystem II light-harvesting apparatus.

Original languageEnglish
Pages (from-to)131-140
Number of pages10
JournalBBA - Bioenergetics
Volume849
Issue number1
DOIs
Publication statusPublished - Apr 2 1986

Fingerprint

Thylakoids
Hydrogenation
Protein Stability
Peas
Membrane Lipids
Pigments
Thermodynamic stability
Hot Temperature
Membranes
Proteins
Photosystem II Protein Complex
Temperature
Thermodynamic properties
Gels
Sodium
Fluorescence
Lipids
Catalysts
Light

Keywords

  • (Pea thylakoid)
  • Lipid hydrogenation
  • Pigment-protein complex
  • Thermal stability
  • Thylakoid membrane

ASJC Scopus subject areas

  • Biophysics

Cite this

Increased thermal stability of pigment-protein complexes of pea thylakoids following catalytic hydrogenation of membrane lipids. / Thomas, Peter G.; Dominy, Peter J.; Vígh, L.; Mansourian, Azad R.; Quinn, Peter J.; Williams, W. Patrick.

In: BBA - Bioenergetics, Vol. 849, No. 1, 02.04.1986, p. 131-140.

Research output: Contribution to journalArticle

Thomas, Peter G. ; Dominy, Peter J. ; Vígh, L. ; Mansourian, Azad R. ; Quinn, Peter J. ; Williams, W. Patrick. / Increased thermal stability of pigment-protein complexes of pea thylakoids following catalytic hydrogenation of membrane lipids. In: BBA - Bioenergetics. 1986 ; Vol. 849, No. 1. pp. 131-140.
@article{1e6e8791bfdb4a39b2372fdbebd03636,
title = "Increased thermal stability of pigment-protein complexes of pea thylakoids following catalytic hydrogenation of membrane lipids",
abstract = "The membrane lipids of pea thylakoids were hydrogenated in situ using the homogeneous catalyst palladiumdi-(sodium alizazine monosulphonate). Following hydrogenation, particle-free patches corresponding to phase-separated gel-phase lipids were observed in the fracture-faces of thylakoid membranes. Freeze-fracture studies on samples of hydrogenated thylakoids incubated at elevated temperatures indicated that hydrogenation reduces the tendency of the heated membranes to destack and vesiculate at higher temperatures. Measurements of chlorophyll a fluorescence emission and the thermal properties of hydrogenated thylakoids suggest that the hydrogenation process also leads to an increase in the thermal stability of pigment-protein complexes of the Photosystem II light-harvesting apparatus.",
keywords = "(Pea thylakoid), Lipid hydrogenation, Pigment-protein complex, Thermal stability, Thylakoid membrane",
author = "Thomas, {Peter G.} and Dominy, {Peter J.} and L. V{\'i}gh and Mansourian, {Azad R.} and Quinn, {Peter J.} and Williams, {W. Patrick}",
year = "1986",
month = "4",
day = "2",
doi = "10.1016/0005-2728(86)90104-0",
language = "English",
volume = "849",
pages = "131--140",
journal = "Biochimica et Biophysica Acta - Bioenergetics",
issn = "0005-2728",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Increased thermal stability of pigment-protein complexes of pea thylakoids following catalytic hydrogenation of membrane lipids

AU - Thomas, Peter G.

AU - Dominy, Peter J.

AU - Vígh, L.

AU - Mansourian, Azad R.

AU - Quinn, Peter J.

AU - Williams, W. Patrick

PY - 1986/4/2

Y1 - 1986/4/2

N2 - The membrane lipids of pea thylakoids were hydrogenated in situ using the homogeneous catalyst palladiumdi-(sodium alizazine monosulphonate). Following hydrogenation, particle-free patches corresponding to phase-separated gel-phase lipids were observed in the fracture-faces of thylakoid membranes. Freeze-fracture studies on samples of hydrogenated thylakoids incubated at elevated temperatures indicated that hydrogenation reduces the tendency of the heated membranes to destack and vesiculate at higher temperatures. Measurements of chlorophyll a fluorescence emission and the thermal properties of hydrogenated thylakoids suggest that the hydrogenation process also leads to an increase in the thermal stability of pigment-protein complexes of the Photosystem II light-harvesting apparatus.

AB - The membrane lipids of pea thylakoids were hydrogenated in situ using the homogeneous catalyst palladiumdi-(sodium alizazine monosulphonate). Following hydrogenation, particle-free patches corresponding to phase-separated gel-phase lipids were observed in the fracture-faces of thylakoid membranes. Freeze-fracture studies on samples of hydrogenated thylakoids incubated at elevated temperatures indicated that hydrogenation reduces the tendency of the heated membranes to destack and vesiculate at higher temperatures. Measurements of chlorophyll a fluorescence emission and the thermal properties of hydrogenated thylakoids suggest that the hydrogenation process also leads to an increase in the thermal stability of pigment-protein complexes of the Photosystem II light-harvesting apparatus.

KW - (Pea thylakoid)

KW - Lipid hydrogenation

KW - Pigment-protein complex

KW - Thermal stability

KW - Thylakoid membrane

UR - http://www.scopus.com/inward/record.url?scp=0000148853&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0000148853&partnerID=8YFLogxK

U2 - 10.1016/0005-2728(86)90104-0

DO - 10.1016/0005-2728(86)90104-0

M3 - Article

AN - SCOPUS:0000148853

VL - 849

SP - 131

EP - 140

JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

SN - 0005-2728

IS - 1

ER -