Resistance to photoinhibition of photosystem II and catalase and antioxidative protection in high mountain plants

• Published in: Plant, Cell & Environment
• Main Authors: STREB, P., FEIERABEND, J., BLIGNY, R.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 1997
• Subjects: Ranunculus glacialis
• Online Access: http://dx.doi.org/10.1111/j.1365-3040.1997.tb00679.x; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1365-3040.1997.tb00679.x; https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1365-3040.1997.tb00679.x

ABSTRACT In leaves of three alpine high mountain plants, Homogyne alpina, Ranunculus glacialis and Soldanella alpina , both photosystem II (PSII) and the enzyme catalase appeared to he highly resistant to photoinactivation under natural field conditions. While the Dl protein of PSII and catalase have a rapid turnover in light and require continuous new protein synthesis in non‐adapted plants, little apparent photoinactivation of PSII or catalase was induced in the alpine plants by translation inhibitors or at low temperature, suggesting that turnover of the Dl protein and catalase was slow in these leaves. In vitro PSII was rapidly inactivated in light in isolated thylakoids from H. alpina and R. glacialis. In isolated intact chloroplasts from R. glacialis , photoinactivation of PSII was slower than in thylakoids. Partially purified catalase from R. glacialis and S. alpina was as sensitive to photoinactivation in vitro as catalases from other sources. Catalase from H. alpina had, however, a 10‐fold higher stability in light. The levels of xanthophyll cycle carotenoids, of the antioxidants ascorbate and glulathione, and of the activities of catalase, superoxide dismutase and glutathione reductase were very high in S. alpina , intermediate in H. alpina , but very low in R. glacialis. However, isolated chloroplasts from all three alpine species contained much higher concentrations of ascorbate and glutathione than chloroplasts from lowland plants.