Structural and Functional Aspects of the Photosynthetic Fixation of Carbon Dioxide

  • G. Schneider
  • I. Andersson
  • C.-I. Brändén
  • S. Knight
  • Y. Lindqvist
  • T. Lundqvist
Part of the NATO ASI Series book series (ASIC, volume 314)


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.


Large Subunit Metal Binding Site Ribulose Bisphosphate Amino Acid Homology Metal Ligand 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Kluwer Academic Publishers 1990

Authors and Affiliations

  • G. Schneider
    • 1
  • I. Andersson
    • 1
  • C.-I. Brändén
    • 1
  • S. Knight
    • 1
  • Y. Lindqvist
    • 1
  • T. Lundqvist
    • 1
  1. 1.Uppsala Biomedical Center Department of Molecular BiologySwedish University of Agricultural SciencesUppsalaSweden

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