| Autor: |
Kramer, David M., Wise, Robert R., Frederick, James R., Alm, David M., Hesketh, John D., Ort, Donald R., Crofts, Antony R. |
| Zdroj: |
Photosynthesis Research; December 1990, Vol. 26 Issue: 3 p213-222, 10p |
| Abstrakt: |
Simultaneous, non-invasive measurements were made of the rate of photosynthetic CO2 fixation and the state of activation of the chloroplast CF1CF0-ATP synthase (CF) in field-grown sunflower (Helianthus annuus L.) during the dark-to-light transition at sunrise. CO2 fixation showed a linear response with light intensity from zero to about 500–700 µE m-2 s-1. However, at light intensities of only 5–22 µE m-2 s-1, the energetic threshold for activation of the CF was found to be significantly lowered (as compared to the pre-dawn state), presumably through reduction of the regulatory sulfhdryl groups of the ?-subunit of the CF. When these studies were extended to chamber-grown plants, it was found that as little as 5 seconds of illumination at 4 µE m-2 s-1 caused apparently full CF reduction. It is clear, therefore, that the catalytic activation of CF is not rate limiting to the induction of carbon assimilation under field conditions during a natural dark-to-light transition at sunrise. A model, based on the redox properties of the regulatory sulfhydryls, was developed to examine the significance of sulfhydryl midpoint potential in explaining the differences in light sensitivity and oxidation and reduction kinetics, between the CF and other thioredoxin-modulated chloroplast enzymes. Computer simulations of the light-induced regulation of three representative thioredoxin-modulated enzymes are presented. |
| Databáze: |
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