A nocturnal inhibitor of carboxylation in leaves

Gutteridge, S. and Parry, M. A J and Burton, S. and Keys, A. J. and Mudd, A. and Feeney, J. and Servaites, J. C. and Pierce, J. (1986) A nocturnal inhibitor of carboxylation in leaves. Nature, 324 (6094). pp. 274-276. ISSN 0028-0836

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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.

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21 Oct 2015 05:04
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18 Sep 2023 00:55