Effects of Glyoxylate on Photosynthesis by Intact Chloroplasts
Author(s) -
R. Michael Mulligan,
Barbara J. Wilson,
N. E. Tolbert
Publication year - 1983
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.72.2.415
Subject(s) - glyoxylate cycle , chloroplast , spinacia , photosynthesis , biochemistry , rubisco , carbon fixation , ribulose , chlorophyll , pyruvate carboxylase , chemistry , photorespiration , biology , metabolism , enzyme , botany , gene
Because glyoxylate inhibits CO(2) fixation by intact chloroplasts and purified ribulose bisphosphate carboxylase/oxygenase, glyoxylate might be expected to exert some regulatory effect on photosynthesis. However, ribulose bisphosphate carboxylase activity and activation in intact chloroplasts from Spinacia oleracea L. leaves were not substantially inhibited by 10 millimolar glyoxylate. In the light, the ribulose bisphosphate pool decreased to half when 10 millimolar glyoxylate was present, whereas this pool doubled in the control. When 10 millimolar glyoxylate or formate was present during photosynthesis, the fructose bisphosphate pool in the chloroplasts doubled. Thus, glyoxylate appeared to inhibit the regeneration of ribulose bisphosphate, but not its utilization.The fixation of CO(2) by intact chloroplasts was inhibited by salts of several weak acids, and the inhibition was more severe at pH 6.0 than at pH 8.0. At pH 6.0, glyoxylate inhibited CO(2) fixation by 50% at 50 micromolar, and glycolate caused 50% inhibition at 150 micromolar. This inhibition of CO(2) fixation seems to be a general effect of salts of weak acids.Radioactive glyoxylate was reduced to glycolate by chloroplasts more rapidly in the light than in the dark. Glyoxylate reductase (NADP(+)) from intact chloroplast preparations had an apparent K(m) (glyoxylate) of 140 micromolar and a V(max) of 3 micromoles per minute per milligram chlorophyll.
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