Regular Paper

Photosynthesis Research

, Volume 95, Issue 1, pp 101-109

Ribulose-1,5-bisphosphate carboxylase/oxygenase from thermophilic cyanobacterium Thermosynechococcus elongatus

  • Beata GubernatorAffiliated withDepartment of Biotechnology, University of Wroclaw
  • , Rafal BartoszewskiAffiliated withDepartment of Biotechnology, University of Wroclaw
  • , Jaroslaw KroliczewskiAffiliated withDepartment of Biotechnology, University of Wroclaw
  • , Guenter WildnerAffiliated withDepartment of Biology, Ruhr-University BochumDepartment of Biochemistry and Molecular Biophysics, University of Arizona
  • , Andrzej SzczepaniakAffiliated withDepartment of Biotechnology, University of Wroclaw Email author 

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Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) can be divided into two branches: the “red-like type” of marine algae and the “green-like type” of cyanobacteria, green algae, and higher plants. We found that the “green-like type” rubisco from the thermophilic cyanobacterium Thermosynechococcus elongatus has an almost 2-fold higher specificity factor compared with rubiscos of mesophilic cyanobacteria, reaching the values of higher plants, and simultaneously revealing an improvement in enzyme thermostability. The difference in the activation energies at the transition stages between the oxygenase and carboxylase reactions for Thermosynechococcus elongatus rubisco is very close to that of Galdieria partita and significantly higher than that of spinach. This is the first characterization of a “green-like type” rubisco from thermophilic organism.


Rubisco Specificity factor Thermostability Thermophilic cyanobacteria