Abstract
Ribulose biphosphate oxygenase/carboxylase is a very interesting enzyme in several respects. It is the enzyme that provides the glycolate associated with photorespiration in C3 plants by catalyzing the reaction of the substrate with molecular oxygen (Metzler, 1977). If carbon dioxide is encountered instead of dioxygen, the product of the reaction is 3-phosphoglycerate (2 equivalents), which enters the Calvin cycle via reduction to glyceraldehyde-3-phosphate (Figure 17–1). This enzyme thus accounts for all light-dependent carbon fixation as well as the substrate for photorespiration. Since the purpose of photorespiration is not understood, the competing reactions of this enzyme are fascinating.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Andrews, T. J., Lorimer, G. H., and Tolbert, N. E., 1973. Ribulose diphosphate oxygenase. I. Synthesis of phosphoglycolate by fraction-1 protein of leaves, Biochemistry12: 11–18.
Gleason, W. B., and Barker, R., 1971a. Oxidation of pentoses in alkaline solution, Can. J. Chem49: 1423–1432.
Gleason, W. B., and Barker, R., 1971b. Evidence for a hydride shift in the alkaline rearrangement of D-ribose, Can. J. Chem49: 1433–1440.
Jensen, R. G., and Bahr, J. T., 1977. Ribulose 1, 5-bisphosphate carboxylase oxygenase, Annu. Rev. Plant Physiol28: 379–400.
Lorimer, G. H., Andrews, T. J., and Tolbert, N. E., 1973. Ribulose diphosphate oxygenase. II. Further proof of reaction products and mechanism of action, Biochemistry12: 18–23.
McFadden, B. A., 1980. A perspective of ribulose bisphosphate carboxylase/oxygenase, the key catalyst in photosynthesis and photorespiration, Acc. Chem. Res13: 394–399.
Metzler, D. E. (ed.), 1977. Biochemistry: The Chemical Reactions of Living Cells, Academic Press, New York, pp. 419–420.
Miziorko, H. M., 1979. Ribulose-1, 5-bisphosphate carboxylase: Evidence in support of the existence of distinct CO2 activator and CO2 substrate sites, J. Biol. Chem254: 270–272.
Pierce, J., Tolbert, N. E., and Barker, R., 1980. Interaction of ribulosebisphosphate carboxylase/ oxygenase with transition state analogues, Biochemistry19: 934–942.
Robison, P. D., Martin, M. N., Tabita, F. R., 1979. Differential effects of metal ions on Rhodospirillum rubrumribulosebisphosphate carboxylase/oxygenase and stoichiometric incorporation of HCO3 into a Co(III)-enzyme complex, Biochemistry18: 4453–4458.
Siegel, M. I., and Lane, M. D., 1973. Chemical and enzymatic evidence for the participation of a 2-carboxy-3-ketoribitol-1, 5-diphosphate intermediate in the carboxylation of ribulose-1, 5-diphosphate, J. Biol. Chem248: 5486–5498.
Sue, J. M., and Knowles, J. R., 1978. Retention of the oxygens at C2 and C3 of D-ribulose-1, 5bisphosphate in the reaction catalyzed by ribulose-1, 5-bisphosphate carboxylase, Biochemistry17: 4041–4044.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1985 Plenum Press, New York
About this chapter
Cite this chapter
Ingraham, L.L., Meyer, D.L. (1985). Ribulose Biphosphate Oxygenase. In: Biochemistry of Dioxygen. Biochemistry of the Elements, vol 4. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2475-1_17
Download citation
DOI: https://doi.org/10.1007/978-1-4613-2475-1_17
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4612-9501-3
Online ISBN: 978-1-4613-2475-1
eBook Packages: Springer Book Archive