Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) has attracted a lot of interest due to its central role in the carbon metabolism of plants and photosynthetic microorganisms (for a review see (1)). The dual function of this enzyme, catalyzing the primary steps in both photosynthetic carbon dioxide fixation and photorespiration (Figure 1), makes it a challenging target for attempts to improve the efficiency of photosynthesis. Recombinant DNA-techniques provide a promising tool to modify the carboxylase/oxygenase ratio by genetic engineering. However, the application of these techniques requires a detailed knowledge of the catalytic mechanism of the enzyme and the structure of its active site.
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Schneider, G., Andersson, I., Brändén, CI., Knight, S., Lindqvist, Y., Lundqvist, T. (1990). Structural and Functional Aspects of the Photosynthetic Fixation of Carbon Dioxide. In: Aresta, M., Schloss, J.V. (eds) Enzymatic and Model Carboxylation and Reduction Reactions for Carbon Dioxide Utilization. NATO ASI Series, vol 314. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0663-1_21
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DOI: https://doi.org/10.1007/978-94-009-0663-1_21
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