Resistance of Photosynthesis to Hydrogen Peroxide in Algae : ENVIRONMENTAL AND STRESS RESPONSES : PROTEINS, ENZYMES AND METABOLISM :
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- Takeda,Toru
- Department of Food and Nutrition, Kinki University
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- Yokota,Akiho
- Research Institute of Innovative Technology for the Earth(RITE)
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- Shigeoka,Shigeru
- Department of Food and Nutrition, Kinki University
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Abstract
The effects of H_2O_2 On the photosynthetic fixation of CO_2 and on thiol-modulated enzymes involved in the photosynthetic reduction of carbon in algae were studied in a comparison with those in chloroplasts isolated from spinach leaves. In both systems, H_2O_2-scavenging enzymes were inhibited by addition of 0.1 mM NaN_3 1 h prior to the addition of H_2O_2・ A concentration (10^<-4> M) of H_2O_2 caused strong inhibition of the CO_2 fixation by intact spinach chloroplasts, as observed by Kaiser [(1976) Biochim. Biophys. Acta 440: 476] , but not that by Euglena and Chlamydomonas cells. The same results were also obtained with cells of the cyanobacteria Synechococcus PCC 7942 and Synechocystis PCC 6803 in the presence of 1 mM hydroxylamine. These results indicate that algal photosynthesis is rather resistant to H_2O_2. The insusceptibility to H_2O_2 Of thiol-modulated enzymes, namely, fructose-1,6-bisphosphatase, NADP-glyceraldehyde-3-phosphate dehydrogenase, and ribulose-5-phosphate kinase, was also observed in the chloroplasts of Euglena and Chlamydomonas and in cyanobacterial cells. It seems likely that the resistance of photosynthesis to H_2O_2 is due in part to the insusceptibility of the algal thiol-modulated enzymes to H_2O_2.
Journal
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- Plant and cell physiology
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Plant and cell physiology 36 (6), 1089-1095,
Japanese Society of Plant Physiologists
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Details 詳細情報について
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- CRID
- 1540854195337374592
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- NII Article ID
- 110003720703
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- NII Book ID
- AA0077511X
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- Text Lang
- en
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- Data Source
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- NDL-Digital
- CiNii Articles