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An investigation of ribulosebisphosphate carboxylase activity by high resolution 1H NMR

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An investigation of ribulosebisphosphate carboxylase activity by high resolution 1H NMR. / Gutteridge, Steven; Parry, Martin A J; Schmidt, C. N Godfrey et al.
In: FEBS Letters, Vol. 170, No. 2, 21.05.1984, p. 355-359.

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

Harvard

Gutteridge, S, Parry, MAJ, Schmidt, CNG & Feeney, J 1984, 'An investigation of ribulosebisphosphate carboxylase activity by high resolution 1H NMR', FEBS Letters, vol. 170, no. 2, pp. 355-359. https://doi.org/10.1016/0014-5793(84)81343-5

APA

Gutteridge, S., Parry, M. A. J., Schmidt, C. N. G., & Feeney, J. (1984). An investigation of ribulosebisphosphate carboxylase activity by high resolution 1H NMR. FEBS Letters, 170(2), 355-359. https://doi.org/10.1016/0014-5793(84)81343-5

Vancouver

Gutteridge S, Parry MAJ, Schmidt CNG, Feeney J. An investigation of ribulosebisphosphate carboxylase activity by high resolution 1H NMR. FEBS Letters. 1984 May 21;170(2):355-359. doi: 10.1016/0014-5793(84)81343-5

Author

Gutteridge, Steven ; Parry, Martin A J ; Schmidt, C. N Godfrey et al. / An investigation of ribulosebisphosphate carboxylase activity by high resolution 1H NMR. In: FEBS Letters. 1984 ; Vol. 170, No. 2. pp. 355-359.

Bibtex

@article{d0f34addab21440f88c948d7075cbe45,
title = "An investigation of ribulosebisphosphate carboxylase activity by high resolution 1H NMR",
abstract = "The reactions catalysed by ribulosebisphosphate carboxylase/oxygenase have been studied by high resolution proton NMR spectroscopy. The protons of the substrate ribulose-P2 and the products of the carboxylase and oxygenase reactions are readily assigned to the various carbon centres. Half of the 3-phosphoglycerate molecules generated during carboxylase turnover of ribulose-P2 in saturating CO2 concentrations acquire deuterium from the solution at the C2 position, whereas the other 3-phosphoglycerate molecules and also the 3-phosphoglycerate produced as a result of the oxygenase activity contain no deuterium of this type. However, the addition of activated enzyme (i.e., in the presence of an effector) to a solution of ribulose-P2 in the near absence of either CO2 or O2 catalyses the exchange of the C3 proton with the deuterium of the solution.",
keywords = "Enediol, NMR, Proton/deuterium exchange, Ribulose bisphosphate, Ribulosebisphosphate carboxylase/oxygenase",
author = "Steven Gutteridge and Parry, {Martin A J} and Schmidt, {C. N Godfrey} and Jim Feeney",
year = "1984",
month = may,
day = "21",
doi = "10.1016/0014-5793(84)81343-5",
language = "English",
volume = "170",
pages = "355--359",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - An investigation of ribulosebisphosphate carboxylase activity by high resolution 1H NMR

AU - Gutteridge, Steven

AU - Parry, Martin A J

AU - Schmidt, C. N Godfrey

AU - Feeney, Jim

PY - 1984/5/21

Y1 - 1984/5/21

N2 - The reactions catalysed by ribulosebisphosphate carboxylase/oxygenase have been studied by high resolution proton NMR spectroscopy. The protons of the substrate ribulose-P2 and the products of the carboxylase and oxygenase reactions are readily assigned to the various carbon centres. Half of the 3-phosphoglycerate molecules generated during carboxylase turnover of ribulose-P2 in saturating CO2 concentrations acquire deuterium from the solution at the C2 position, whereas the other 3-phosphoglycerate molecules and also the 3-phosphoglycerate produced as a result of the oxygenase activity contain no deuterium of this type. However, the addition of activated enzyme (i.e., in the presence of an effector) to a solution of ribulose-P2 in the near absence of either CO2 or O2 catalyses the exchange of the C3 proton with the deuterium of the solution.

AB - The reactions catalysed by ribulosebisphosphate carboxylase/oxygenase have been studied by high resolution proton NMR spectroscopy. The protons of the substrate ribulose-P2 and the products of the carboxylase and oxygenase reactions are readily assigned to the various carbon centres. Half of the 3-phosphoglycerate molecules generated during carboxylase turnover of ribulose-P2 in saturating CO2 concentrations acquire deuterium from the solution at the C2 position, whereas the other 3-phosphoglycerate molecules and also the 3-phosphoglycerate produced as a result of the oxygenase activity contain no deuterium of this type. However, the addition of activated enzyme (i.e., in the presence of an effector) to a solution of ribulose-P2 in the near absence of either CO2 or O2 catalyses the exchange of the C3 proton with the deuterium of the solution.

KW - Enediol

KW - NMR

KW - Proton/deuterium exchange

KW - Ribulose bisphosphate

KW - Ribulosebisphosphate carboxylase/oxygenase

UR - http://www.scopus.com/inward/record.url?scp=0005651561&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(84)81343-5

DO - 10.1016/0014-5793(84)81343-5

M3 - Journal article

AN - SCOPUS:0005651561

VL - 170

SP - 355

EP - 359

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2

ER -