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A nocturnal inhibitor of carboxylation in leaves

Research output: Contribution to Journal/MagazineJournal articlepeer-review

  • S. Gutteridge
  • M. A J Parry
  • S. Burton
  • A. J. Keys
  • A. Mudd
  • J. Feeney
  • J. C. Servaites
  • J. Pierce
<mark>Journal publication date</mark>1/12/1986
Issue number6094
Number of pages3
Pages (from-to)274-276
Publication StatusPublished
<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.