Light inhibition of mitochondrial respiration in a mutant of Chlamydomonas reinhardtii devoid of ribulose-1,5-bisphosphate carboxylase/oxygenase activity.
The effect of light on mitochondrial respiration has been investigated in Chlamydomonas reinhardtii rcl-u-1-10-6C, a mutant devoid of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activity. No CO2 uptake was observed in the light, confirming that there was no Rubisco activity, but the CO2 evolution rate was diminished by 65 to 80%. This inhibition was ascribable to a decrease in the tricarboxylic acid cycle (Krebs cycle) activity. At the same time, O2 evolution associated with stimulation of the O2 uptake appears. Darkness or addition of DCMU fully reversed the effect of light, indicating that the inhibitory process is linked to photosystem activities. Levels of pyridine nucleotides (NAD(H) and NADP(H)) and adenine nucleotides (ATP and ADP), the most probable mediators of the interaction between photosynthesis and respiration, were measured in dark and in light. During a dark to light transition the level of NADPH increased significantly whereas the NAD(H) pool remained almost fully oxidized. The level of ADP was always extremely low. These results suggest that the inhibition of Krebs cycle activity is due to a competition for cytosolic ADP between chloroplastic photophosphorylations and oxidative phosphorylations.
Gans
P
P
Department de Biologie, C.E.N. de Cadarache, Saint-Paul-lez-Durance, France.
Rebeille
F
F
D002696:Chlamydomonas / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D002952:Citric Acid Cycle; D008027:Light; D008928:Mitochondria / Q000378:metabolism*; D009154:Mutation; D009711:Nucleotides / Q000378:metabolism; D010101:Oxygen Consumption; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*
D009711:Nucleotides; D012273:Ribulose-Bisphosphate Carboxylase