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A nocturnal inhibitor of carboxylation in leaves

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A nocturnal inhibitor of carboxylation in leaves. / Gutteridge, S.; Parry, M. A J; Burton, S. et al.
In: Nature, Vol. 324, No. 6094, 01.12.1986, p. 274-276.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Gutteridge, S, Parry, MAJ, Burton, S, Keys, AJ, Mudd, A, Feeney, J, Servaites, JC & Pierce, J 1986, 'A nocturnal inhibitor of carboxylation in leaves', Nature, vol. 324, no. 6094, pp. 274-276. https://doi.org/10.1038/324274a0

APA

Gutteridge, S., Parry, M. A. J., Burton, S., Keys, A. J., Mudd, A., Feeney, J., Servaites, J. C., & Pierce, J. (1986). A nocturnal inhibitor of carboxylation in leaves. Nature, 324(6094), 274-276. https://doi.org/10.1038/324274a0

Vancouver

Gutteridge S, Parry MAJ, Burton S, Keys AJ, Mudd A, Feeney J et al. A nocturnal inhibitor of carboxylation in leaves. Nature. 1986 Dec 1;324(6094):274-276. doi: 10.1038/324274a0

Author

Gutteridge, S. ; Parry, M. A J ; Burton, S. et al. / A nocturnal inhibitor of carboxylation in leaves. In: Nature. 1986 ; Vol. 324, No. 6094. pp. 274-276.

Bibtex

@article{3544dd90ec3344c881cc96e3176ef9aa,
title = "A nocturnal inhibitor of carboxylation in leaves",
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.",
author = "S. Gutteridge and Parry, {M. A J} and S. Burton and Keys, {A. J.} and A. Mudd and J. Feeney and Servaites, {J. C.} and J. Pierce",
year = "1986",
month = dec,
day = "1",
doi = "10.1038/324274a0",
language = "English",
volume = "324",
pages = "274--276",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6094",

}

RIS

TY - JOUR

T1 - A nocturnal inhibitor of carboxylation in leaves

AU - Gutteridge, S.

AU - Parry, M. A J

AU - Burton, S.

AU - Keys, A. J.

AU - Mudd, A.

AU - Feeney, J.

AU - Servaites, J. C.

AU - Pierce, J.

PY - 1986/12/1

Y1 - 1986/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0001560447&partnerID=8YFLogxK

U2 - 10.1038/324274a0

DO - 10.1038/324274a0

M3 - Journal article

AN - SCOPUS:0001560447

VL - 324

SP - 274

EP - 276

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6094

ER -