The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications
Abstract
Ribulose-1,5-bisphosphate carboxylase was activated by incubation with CO2 and Mg2++, and inactivated upon removal of CO2 and Mg2+ by gel filtration. The activation process involved CO2 rather than HCO3-. The activity of the enzyme was dependent upon the preincubation concentrations of CO2 and Mg2+ and upon the preincubation pH, indicating that activation involved the reversible formation of an equilibrium complex of enzyme-CO2-Mg. The initial rate of activation was linearly dependent upon the CO2 concentration but independent of the Mg2+ concentration. Kinetic analyses indicated that the enzyme reacted first with CO2 in a rate-determining and reversible step, followed by a rapid reaction with Mg2+ to form an active ternary complex (see eq 1 in text). The pseudo-first order rate constant, kobsd, for the activation process at constant pH was derived: kobsd=k1[CO2] + (k2k4/k3[Mg2+]). Experimentally, kobsd was shown to be linearly dependent upon the CO2 concentration and inversely dependent upon the Mg2+ concentration. The activity of the enzyme after preincubation to equilibrium at constant concentrations of CO2 and Mg2+ increased as the preincubation pH was raised, indicating that CO2 reacted with an enzyme group whose pK was distinctly alkaline. It is proposed that the activation of ribulose-1, 5-biphosphate carboxylane involves the formation of a carbamate.
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Citations
Cites
Statistical estimations in enzyme kinetics
WILKINSON, G. (1961) · Biochemical Journal · doi:10.1042/bj0800324 · Cited by 3,552
Laing, W. A., Ogren, W. L., & Hageman, R. H. (1974) · Plant Physiology · doi:10.1104/pp.54.5.678 · Cited by 662
Phosphoglycolate production catalyzed by ribulose diphosphate carboxylase
Bowes, G., Ogren, W. L., & Hageman, R. H. (1971) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(71)90475-x · Cited by 549
Heldt, H. W., Werdan, K., Milovancev, M., & Geller, G. (1973) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(73)90137-0 · Cited by 469
Oxygen Inhibition and Other Properties of Soybean Ribulose 1,5-Diphosphate Carboxylase
Bowes, G., & Ogren, W. L. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45507-5 · Cited by 245
The Active Species of “CO2” Utilized by Ribulose Diphosphate Carboxylase
Cooper, T., Filmer, D. L., Wishnick, M. M., et al. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91899-5 · Cited by 241
Ribulose diphosphate oxygenase. II. Further proof of reaction products and mechanism of action
Lorimer, G. H., Andrews, T. J., & Tolbert, N. E. (1973) · Biochemistry · doi:10.1021/bi00725a004 · Cited by 225
Self-citationBadger, M. R., & Andrews, T. J. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(74)90192-2 · Cited by 164
Self-citationThe Carboxylation of Phosphoenolpyruvate and Pyruvate
Cooper, T., Tchen, T. T., Wood, H. G., et al. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)92022-3 · Cited by 142
Determination of the Rate of Hexokinase-Glucose Dissociation by the Isotope-trapping Method
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Cited by
Mechanism of Rubisco: the carbamate as general base
Cleland, W. W., Andrews, T. J., Gutteridge, S., Hartman, F. C., & Lorimer, G. H. (1998) · Chemical Reviews · doi:10.1021/cr970010r · Cited by 430
Self-citationEffect of carbon dioxide on yeast growth and fermentation
Jones, R. P., & Greenfield, P. F. (1982) · Enzyme and Microbial Technology · doi:10.1016/0141-0229(82)90034-5 · Cited by 320
Zhang, N., Kallis, R. P., Ewy, R. G., & Portis, A. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042529999 · Cited by 214
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10568 · Cited by 190
The activity of Rubisco’s molecular chaperone, Rubisco activase, in leaf extracts.
Carmo-Silva, A. E., & Salvucci, M. E. (2011) · Photosynthesis Research · doi:10.1007/s11120-011-9667-8 · Cited by 86
Metadata
- Authors
- Lorimer, G. H., Badger, M. R., & Andrews, T. J.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1976-02-10
- Volume
- 15
- Issue
- 3
- Pages
- 529-536
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2030642428
- Cited by
- 555
- References
- 14
- FWCI
- 16.61
- Type
- journal article
- Language
- en
- Open access
- closed
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- Lorimer, G. H., Badger, M. R., & Andrews, T. J. (1976). The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications. Biochemistry. https://doi.org/10.1021/bi00648a012
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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