A nocturnal inhibitor of carboxylation in leaves.

A - Papers appearing in refereed journals

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

AuthorsGutteridge, S., Parry, M. A. J., Burton, S., Keys, A. J., Mudd, A., Feeney, J., Servaites, J. and Pierce, J.
Abstract

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. 

KeywordsRRES175; 175_Plant sciences; 175_Biochemistry
Year of Publication1986
JournalNature
Journal citation324 (6094), pp. 274-276
Digital Object Identifier (DOI)doi:10.1038/324274a0
Open accessPublished as non-open access
Output statusPublished
Publication dates
Online20 Nov 1986
Publication process dates
Accepted24 Sep 1986
ISSN14764687
PublisherSpringer Nature
Copyright licensePublisher copyright

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