Protection from photoinhibition by low temperature in Synechocystis 6714 and in Chlamydomonas reinhardtii: detection of an intermediary state
- 4 September 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (35) , 8100-8106
- https://doi.org/10.1021/bi00487a016
Abstract
Photoinhibition was induced in a cyanobacterium strain, Synechocystis 6714, and a green alga, Chlamydomonas reinhardtii, by exposing them to light intensities from 1000 to 4000 .mu.E/(m2 .cntdot. s) at various temperatures. The photoinhibition process was followed by measurements of chlorophyll fluorescence and oxygen evolution. During exposure to high light, fluorescent active reaction centers II became low fluorescent inactive centers. This process involved several reversible and irreversible steps. The pathway from the active state to the inactive low fluorescent state was different in Synechocystis and Chlamydomonas. In the latter there was a reversible intermediary step characterized by an increase of Fo. This state was stable at 5.degree.C and slowly reversible at room temperature. The high Fo fluorescence level corresponded to a state of photosystem II centers that were inactive for oxygen evolution. An FO decrease occurred in the dark in the absence of protein synthesis and was correlated to a restoration of oxygen evolution. Further experiments suggested that the existence of the intermediate fluorescent state is due to modified closed centers in which the reduced primary acceptor is less acessible to reoxidation. In cyanobacteria this reversible state was not detected. In both organisms, the decrease of Fmax reflected an irreversible damage of photosystem II centers. These centers need replacement of proteins in order to be active again. The quenching of Fmax and the irreversible inhibition of oxygen evolution were slowed down in both organisms by decreasing the temperature of the photoinhibitory treatment from 34 to 5.degree.C. We conclude that low temperature protected the reaction center II from irreversible photodamage.This publication has 17 references indexed in Scilit:
- Photoinhibition of photosynthesis in intact bean leaves: role of light and temperature, and requirement for chloroplast-protein synthesis during recoveryPlanta, 1986
- Photoinactivation of chloroplasts already inhibited on the oxidizing side of Photosystem IIBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1986
- Mechanism of photoinhibition: photochemical reaction center inactivation in system II of chloroplastsPhotosynthesis Research, 1986
- Membrane protein damage and repair: removal and replacement of inactivated 32-kilodalton polypeptides in chloroplast membranes.The Journal of cell biology, 1984
- Membrane protein damage and repair: Selective loss of a quinone-protein function in chloroplast membranesProceedings of the National Academy of Sciences, 1984
- Quenching of the System II chlorophyll fluorescence by the plastoquinone poolBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1979
- A polarographic method for detection of oxygen production and reduction of Hill reagent by isolated chloroplastsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1968
- Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardi.Proceedings of the National Academy of Sciences, 1965
- Effect of growth temperature on the fatty acid composition of a blue-green algaPhytochemistry, 1964
- COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARISPlant Physiology, 1949