Thermal stability studies of photosystem II complexes reconstituted into phosphatidylcholine liposomes

Thermal stability studies of photosystem II complexes reconstituted into phosphatidylcholine... Light-harvesting II complexes (LHCII) and photosystem II core complexes (PSIICC) were isolated from spinach (Spinacia oleracea L.) and reconstituted into phosphatidylcholine liposomes and, under heat stress, PSIICC-LHCII proteoliposomes were found to exhibit significantly higher oxygen evolution activity than PSIICC proteoliposomes lacking LHCII. In the presence of LHCII, the temperature of a 10-min heat stress that caused semi-inactivation of oxygen-evolving activity in these liposomes increased from 34 to ∼37°C and the total inactivation temperature increased from ∼50 to ∼60°C. Moreover, with heat stress, decreases in the absorbance and fluorescence spectra of PSIICC-LHCII proteoliposomes were smaller than in LHCII-lacking PSIICC proteoliposomes. These results demonstrated that reconstitution of PSII into liposomes with LHCII increased the antenna size and light harvesting cross-section of PSII and thus, under heat stress, enhanced PSII photochemical activity and thermal stability. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Thermal stability studies of photosystem II complexes reconstituted into phosphatidylcholine liposomes

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Publisher
Springer Journals
Copyright
Copyright © 2014 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Plant Physiology; Plant Sciences
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1134/S1021443714010191
Publisher site
See Article on Publisher Site

Abstract

Light-harvesting II complexes (LHCII) and photosystem II core complexes (PSIICC) were isolated from spinach (Spinacia oleracea L.) and reconstituted into phosphatidylcholine liposomes and, under heat stress, PSIICC-LHCII proteoliposomes were found to exhibit significantly higher oxygen evolution activity than PSIICC proteoliposomes lacking LHCII. In the presence of LHCII, the temperature of a 10-min heat stress that caused semi-inactivation of oxygen-evolving activity in these liposomes increased from 34 to ∼37°C and the total inactivation temperature increased from ∼50 to ∼60°C. Moreover, with heat stress, decreases in the absorbance and fluorescence spectra of PSIICC-LHCII proteoliposomes were smaller than in LHCII-lacking PSIICC proteoliposomes. These results demonstrated that reconstitution of PSII into liposomes with LHCII increased the antenna size and light harvesting cross-section of PSII and thus, under heat stress, enhanced PSII photochemical activity and thermal stability.

Journal

Russian Journal of Plant PhysiologySpringer Journals

Published: Dec 28, 2013

References

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