Thermal stability studies of photosystem II complexes reconstituted into phosphatidylcholine liposomes View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2014-01

AUTHORS

F. Zhou, N. W. Qiu, Z. J. Gu, B. J. Zhang, C. Hua

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. More... »

PAGES

26-32

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s1021443714010191

DOI

http://dx.doi.org/10.1134/s1021443714010191

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031204005


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