期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 283, 期 42, 页码 28380-28391出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M710465200
关键词
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资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan [18570042, 20570039]
- Ministry of Education, Youth and Sports of the Czech Republic [6198959215]
- Grant Agency of the Czech Republic [522/06/0979]
- Grants-in-Aid for Scientific Research [18570042, 20570039] Funding Source: KAKEN
Moderate heat stress (40 degrees C for 30 min) on spinach thylakoid membranes induced cleavage of the reaction center-binding D1 protein of photosystem II, aggregation of the D1 protein with the neighboring polypeptides D2 and CP43, and release of three extrinsic proteins, PsbO, -P, and -Q. These heat-induced events were suppressed under anaerobic conditions or by the addition of sodium ascorbate, a general scavenger of reactive oxygen species. In accordance with this, singlet oxygen and hydroxyl radicals were detected in spinach photosystem II membranes incubated at 40 C for 30 min with electron paramagnetic resonance spin-trapping spectroscopy. The moderate heat stress also induced significant lipid peroxidation under aerobic conditions. We suggest that the reactive oxygen species are generated by heat-induced inactivation of a water-oxidizing manganese complex and through lipid peroxidation. Although occurring in the dark, the damages caused by the moderate heat stress to photosystem II are quite similar to those induced by excessive illumination where reactive oxygen species are involved.
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