, Volume 107, Issue 4, pp 469–477

Antioxidative protection in the inducible CAM plant Sedum album L. following the imposition of severe water stress and recovery

  • F. J. Castillo

DOI: 10.1007/BF00333937

Cite this article as:
Castillo, F.J. Oecologia (1996) 107: 469. doi:10.1007/BF00333937


The antioxidative protection during the C3-CAM shift induced by water stress was investigated in the temperate succulent Sedum album L. The C3-CAM shift was characterized in terms of CO2 exchange, titratable acidity and phosphoenolpyruvate carboxylase activity. Well-watered plants displayed C3-like patterns of gas exchange and exhibited a mild day-night acid fluctuation indicating that those plants were performing CAM-cycling metabolism. Imposed drought highly stimulated CAM cycling, decreasing the net CO2 uptake during the day, eliminating net CO2 efflux at night and stimulating tissue acid fluctuations. As water deficit developed, chlorophyll fluorescence measurements showed a decrease in the Fv/Fm ratio, indicating that photoinhibition could follow after severe drought. Protection might be performed by the increased activity of enzymes involved in the destruction of free radicals and oxidants, but their response depended on the water status of the plant. Ascorbate peroxidase and superoxide dismutase activities increased in plants subjected to mild stress but declined during severe water stress. Catalase activity, however, was quite stable under mild water stress and was clearly inhibited under severe water stress. At this stage, glutathione reductase and monodehydroascorbate reductase seemed to be very important in the protection against oxidants, both increasing considerably their activities under severe water stress. Even if recycling has been shown to alleviate photoinhibition, our results clearly demonstrate that antioxidative enzymes play an important role in the protection of plants from oxidants during the C3-CAM shift induced by water stress.

Key words

Crassulacean acid metabolism Sedum album Water stress Antioxidative enzymes 

Copyright information

© Springer-Verlag 1996

Authors and Affiliations

  • F. J. Castillo
    • 1
  1. 1.Departamento de Ciencias del Medio NaturalUniversidad Pública de NavarraPamplonaSpain

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