Isolation and Characteristics of the PSI-LHCI-LHCII Supercomplex Under High Light

We developed a novel method for the isolation of the PSI‐LHCI‐LHCII complex from spinach leaves. The supercomplex was resolved into a core complex (CPI), LHCII trimers, LHCI dimers and LHCII monomers using green gel electrophoresis. We then investigate changes in the fluorescence and absorption spec...

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Bibliographic Details
Published inPhotochemistry and photobiology Vol. 87; no. 1; pp. 143 - 150
Main Authors Qin, Xiaochun, Wang, Wenda, Wang, Kebing, Xin, Yueyong, Kuang, Tingyun
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 01.01.2011
Subjects
Binding sites
Electrophoresis, Polyacrylamide Gel
Fluorescence
Leaves
Light
Photochemistry
Photosystem I Protein Complex - metabolism
Proteins
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
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Summary:We developed a novel method for the isolation of the PSI‐LHCI‐LHCII complex from spinach leaves. The supercomplex was resolved into a core complex (CPI), LHCII trimers, LHCI dimers and LHCII monomers using green gel electrophoresis. We then investigate changes in the fluorescence and absorption spectra of PSI‐LHCI‐LHCII under high light. In addition, we compared light‐induced denaturation of the core protein subunits in both PSI‐LHCI and PSI‐LHCI‐LHCII. Differences in denaturation and photochemical activity indicated that binding of LHCII increased the photosensitivity of the PSI core. Increased energy delivered to the PSI core during illumination accelerated damage to the core complex.
Bibliography:ark:/67375/WNG-RZG63FT2-K
istex:C1E2D19824128FBE252C8541C7276E9ED221B197
ArticleID:PHP830
These authors contributed equally to this work.
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0031-8655
1751-1097
DOI:10.1111/j.1751-1097.2010.00830.x