Title
The role of enzyme activation state in limiting carbon assimilation under variable light conditions
Recommended Citation
Postprint version. Published in Photosynthesis Research, Volume 41, Issue 2, August 1, 1994, pages 295-302.
NOTE: At the time of publication, the author Scott Steinmaus was not yet affiliated with Cal Poly.
The definitive version is available at https://doi.org/10.1007/BF00019407.
Abstract
The mechanisms regulating transient photosynthesis by soybean (Glycine max) leaves were examined by comparing photosynthetic rates and carbon reduction cycle enzyme activities under flashing (saturating 1 s lightflecks separated by low photon flux density (PFD) periods of different durations) and continuous PFD. At the same mean PFD, the mean photosynthetic rates were reduced under flashing as compared to continuous light. However, as the duration of the low PFD period lengthened, the CO2 assimilation attributable to a lightfleck increased. This enhanced lightfleck CO2 assimilation was accounted for by a greater postillumination CO2 fixation occurring after the lightfleck. The induction state of photosynthesis, ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco), fructose 1,6-bisphosphatase (FBPase) and ribulose 5-phosphate kinase (Ru5P kinase) activities all responded similarly and were all lower under flashing as compared to constant PFD of the same integrated mean value. However, the fast phase of induction and FBPase and Ru5P kinase activities were reduced more than were the slow phase of induction and rubisco activity. This was consistent with the role of the former enzymes in the fast induction component that limited RuBP regeneration. Competition for reducing power between carbon metabolism and thioredoxin-mediated enzyme activation may have resulted in lower enzyme activation states and hence lower induction states under flashing than continuous PFD, especially at low lightfleck frequencies (low mean PFD).
Disciplines
Biology
Copyright
1994 Springer.
URL: https://digitalcommons.calpoly.edu/bio_fac/76