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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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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. © 1986 Nature Publishing Group.

Item Type: Article
Journal or Publication Title: Nature
Subjects:
Departments: Faculty of Science and Technology > Lancaster Environment Centre
ID Code: 76063
Deposited By: ep_importer_pure
Deposited On: 21 Oct 2015 06:04
Refereed?: Yes
Published?: Published
Last Modified: 20 Nov 2017 11:45
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/76063

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