The Response of Antioxidant Enzymes in Cellular Organelles in Cucumber (Cucumis sativus L.) Leaves to Methyl Viologen-induced Photo-oxidative Stress
The Response of Antioxidant Enzymes in Cellular Organelles in Cucumber (Cucumis sativus L.) Leaves to Methyl Viologen-induced Photo-oxidative Stress
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DOI:
10.1007/s10725-006-0023-5
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发表时间:
2006-05
影响因子:
4.2
通讯作者:
X. Song;Chun Lan Tiao;K. Shi;W. Mao;J. Ogweno;Y. Zhou;Jingquan Yu
中科院分区:
文献类型:
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作者:
X. Song;Chun Lan Tiao;K. Shi;W. Mao;J. Ogweno;Y. Zhou;Jingquan Yu
In order to clarify the response of antioxidant systems in various cellular organelles to photo-oxidative stress, the activities of superoxide dismutase (SOD) and enzymes of the ascorbate–glutathione (AsA-GSH) cycle were investigated in chloroplasts, mitochondria and cytosol of cucumber leaves subjected to methyl viologen (MV) treatment. Photo-oxidation by MV resulted in significant reductions in net photosynthetic rate (Pn) and increases in the ratio of the quantum efficiency of photosystem II (PSII), ΦPSIIto that of the quantum efficiency of CO2fixation (ΦCO2), followed by increased activities of SOD, and a general increase of AsA-GSH cycle enzymes in chloroplasts, mitochondria and cytosol. These increases were however, most significant in chloroplasts. There were also significant increases in dehydroascorbate (DHA), reduced glutathione (GSH), and oxidized glutathione (GSSG) except that the content of ascorbate (AsA) in chloroplasts and cytosol was slightly decreased and little effected, respectively. However, GSSG in mitochondria and GSH in cytosol were little influenced by the MV treatment. The activity of ascorbate oxidase (AO) in these organelles was independent of the MV treatment while the activity ofl-galactono-1,4- lactone dehydrogenase (GLDH) in mitochondria was slightly inhibited by MV treatment. These results indicate that disturbance of electron transport in chloroplasts by MV influenced the metabolism of whole cell by a crosstalk signaling system and that the AsA-GSH cycle played a primary role in sustaining the levels of AsA.