Carotenoid composition and down regulation of photosystem II in three conifer species during the winter

1994 ◽  
Vol 92 (3) ◽  
pp. 451-458 ◽  
Author(s):  
William W. Adams III ◽  
Barbara Demmig-Adams
2001 ◽  
Vol 28 (10) ◽  
pp. 1023 ◽  
Author(s):  
Congming Lu ◽  
Qingtao Lu ◽  
Jianhua Zhang ◽  
Qide Zhang ◽  
Tingyun Kuang

Photosynthesis, the xanthophyll cycle, light energy dissipation and down-regulation of photosystem II (PSII) in senescent leaves of wheat plants grown in the field were investigated. With the progress of senescence, maximal efficiency of PSII photochemistry decreased only slightly early in the morning but substantially at midday. Actual PSII efficiency, photochemical quenching, efficiency of excitation capture by open PSII centres, and the I–P phase of fluorescence induction curves decreased significantly and such decreases were much more evident at midday than in the morning. At the same time, non-photochemical quenching, thermal dissipation and de-epoxidation status of the xanthophyll cycle increased, with much greater increases at midday than in the morning. These results suggest that the xanthophyll cycle played a role in photoprotection of PSII in senescent leaves by dissipating excess excitation energy. Taking into account the substantial decrease in photosynthetic capacity in senescent leaves, our data seem to support the view that the decrease in actual PSII efficiency in senescent leaves may represent a mechanism to down-regulate photosynthetic electron transport to match the decreased CO2 assimilation capacity and avoid photodamage of PSII from excess excitation energy.


Author(s):  
Kathleen M. Marr ◽  
Mary K. Lyon

Photosystem II (PSII) is different from all other reaction centers in that it splits water to evolve oxygen and hydrogen ions. This unique ability to evolve oxygen is partly due to three oxygen evolving polypeptides (OEPs) associated with the PSII complex. Freeze etching on grana derived insideout membranes revealed that the OEPs contribute to the observed tetrameric nature of the PSIl particle; when the OEPs are removed, a distinct dimer emerges. Thus, the surface of the PSII complex changes dramatically upon removal of these polypeptides. The atomic force microscope (AFM) is ideal for examining surface topography. The instrument provides a topographical view of individual PSII complexes, giving relatively high resolution three-dimensional information without image averaging techniques. In addition, the use of a fluid cell allows a biologically active sample to be maintained under fully hydrated and physiologically buffered conditions. The OEPs associated with PSII may be sequentially removed, thereby changing the surface of the complex by one polypeptide at a time.


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