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Excitation-energy redistribution in the cryptomonad alga Cryptomonas ovata

Authors :
Ursula K. Snyder
John Biggins
Source :
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 892:48-55
Publication Year :
1987
Publisher :
Elsevier BV, 1987.

Abstract

We have studied the redistribution of excitation energy in the cryptomonad alga Cryptomonas ovata . Low-temperature fluorescence emission spectra from cells preilluminated with light 1 and light 2 show that preferential excitation of Photosystem II (PS II) leads to decreased fluorescence emission from chlorophyll (Chl) a associated with PS II relative to the emission following the preferential excitation of Photosystem I (PS I). The fluorescence change is indicative of a light-state transition by the cells. However, comparision of measurements of the kinetics of P-700 photooxidation by cells fixed with glutaraldehyde following illumination with light 1 or light 2 shows that the relative activity of PS I is lower in cells fixed in light 2. This is in contrast to the expectation for cells in State 2. Excitation spectra for the fluorescence emission from PS II Chl a show that preferential excitation of PS II leads to a decreased probability for energy transfer from phycoerythrin and Chl c 2 to PS II when compared to cells in which PS I is preferentially excited. This result is in accordance with recent picosecond time-resolved fluorescence studies (Bruce, D., Biggins, J., Charbonneau, S. and Thewalt, M. (1987) in Progress in Photosynthesis Research (Biggins, J., ed.), Vol. II, pp. 777–780, Martinus Nijhoff, Dordrecht) and we, therefore, suggest that C. ovata does not undergo a classical light-state transition. However, preferential excitation of PS II or PS I appears to cause pigment-protein conformational changes which change the probability for energy transfer from phycoerythrin to PS II, and we suggest that this may be a mechanism for photoprotection of PS II. Studies of the kinetics of excitation-energy redistribution, and of the effects of electron-transport inhibitors and uncouplers of photophosphorylation indicate that the mechanism for excitation-energy redistribution in C. ovata and phycobilisome-containing organisms may be similar.

Details

ISSN :
00052728
Volume :
892
Database :
OpenAIRE
Journal :
Biochimica et Biophysica Acta (BBA) - Bioenergetics
Accession number :
edsair.doi...........475b6fe25cebad2c6ef4c73ba7bdbe85