Research output: Contribution to Journal/Magazine › Journal article › peer-review
<mark>Journal publication date</mark> | 1/12/1986 |
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<mark>Journal</mark> | Nature |
Issue number | 6094 |
Volume | 324 |
Number of pages | 3 |
Pages (from-to) | 274-276 |
Publication Status | Published |
<mark>Original language</mark> | English |
The diurnal variation in the activity of ribulose-l,5-bisphosphate carboxylase (RuBPCase), the major CO2-fixing enzyme in plants, has been shown to result from the influx and efflux of Mg2+ ions into and out of the chloroplast stroma. A recent re-examination of the phenomenon indicates that the inactivation of the enzyme, rather than being due to the efflux of Mg2+, is correlated in some plant species with an increase in the concentration of an organic phosphate ester in the chloroplast in the dark1-3. We have purified this potent inhibitor from dark-treated potato (Solanum tuberosum) leaves, and established that its structure is 2-carboxy-D-arabinitol-1-phosphate, a molecule that closely resembles an intermediate in the carboxylase reaction of RuBPCase.