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Light‐Induced Phosphate Binding in Relation to Photophosphorylation and Levels of ATP, ADP and AMP in the Green Alga Scenedesmus
Author(s) -
LARSSON C.M.,
TILLBERG J.E.,
HALLMÉN G.
Publication year - 1978
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1978.tb01624.x
Subject(s) - photophosphorylation , dcmu , adenylate kinase , biophysics , energy charge , tetrahymena pyriformis , atp synthase , phosphate , scenedesmus , biochemistry , biology , adenosine triphosphate , light intensity , chloroplast , photosynthesis , chemistry , algae , photosystem ii , botany , enzyme , physics , tetrahymena , gene , optics
Synchronous cultures of Scenedesmus obtusiusculus Chod. were starved for phosphorus for 48 h. Such cells develop an efficient mechanism for phosphate binding which is very sensitive to metabolic inhibitions. Phosphate binding, fluctuations in the ATP pool during dark‐light‐dark transitions, and steady state levels of ATP, ADP and AMP were studied. The experiments were carried out in a CO 2 ‐free N 2 atmosphere. DCMU, phloridzin and 2,5‐dibromo‐3‐methyl‐6‐isopropyl‐ p ‐benzoquinone (DBMIB) were used as inhibitors of photophosphorylation. Light‐induced phosphate uptake was inhibited to various extents by all the inhibitions. The dark‐light‐dark transition experiments show that neither the light‐induced increment in ATP nor the decrease at darkening are affected by DCMU, but DBMIB and phloridzin inhibit both processes. DCMU seems to affect the regulation of the ATP pool size. The steady state levels of the adenylate pools were almost the same in the light as in the dark, and they were also little sensitive to the inhibitors. In unpoisoned cells in the light the steady state ATP/ADP ratio was 1.7 and the energy charge was 0.66. The rates of phosphate binding are not correlated to any of the adenylate parameters studied. This is probably due to the diverse effects of the inhibitors on light‐stimulated production of reducing equivalents, photophosphorylation and transfer of energy from the chloroplast to the cytoplasm.