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Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the key enzyme of the Calvin cycle, catalyzing the fixation of inorganic carbon dioxide to organic sugars. Unlike most enzymes, RuBisCO is extremely slow, substrate unspecific, and catalyzes undesired side-reactions, which are considered to be responsible for the slow deactivation observed in vitro, a phenomenon known as fallover. | ỊFEBS Journal Slow deactivation of ribulose 1 5-bisphosphate carboxylase oxygenase elucidated by mathematical models Franziska Witzel1 2 Jan Gotze3 and Oliver Ebenhoh1 4 5 1 Max-Planck-Institute for Molecular Plant Physiology Potsdam-Golm Germany 2 Institute for Pathology Charite Berlin Germany 3 Institute for Chemistry University of Potsdam Potsdam Germany 4 Institute for Complex Systems and MathematicalBiology University of Aberdeen Aberdeen UK 5 Institute of MedicalSciences University of Aberdeen Aberdeen UK Keywords carbon fixation enzyme kinetics fallover mathematicalmodel RuBisCO Correspondence O. Ebenhoh Institute for Complex Systems and MathematicalBiology University of Aberdeen Aberdeen AB24 3UE UK Fax 44 0 1224 273105 Tel 44 0 1224 272520 E-mail ebenhoeh@abdn.ac.uk Database The mathematical models described here have been submitted to the Online Cellular Systems Modelling Database and can be accessed at http jjj.biochem.sun.ac.za database witzel1 index.htmland http jjj.biochem.sun.ac.za database witzel2 index.html free of charge Received 4 September 2009 revised 6 November 2009 accepted 4 December 2009 doi 10.1111 j.1742-4658.2009.07541.x Ribulose 1 5-bisphosphate carboxylase oxygenase RuBisCO is the key enzyme of the Calvin cycle catalyzing the fixation of inorganic carbon dioxide to organic sugars. Unlike most enzymes RuBisCO is extremely slow substrate unspecific and catalyzes undesired side-reactions which are considered to be responsible for the slow deactivation observed in vitro a phenomenon known as fallover. Despite the fact that amino acid sequences and the 3D structures of RuBisCO from a variety of species are known the precise molecular mechanisms for the various side reactions are still unclear. In the present study we investigate the kinetic properties of RuBisCO using mathematical models. Initially we formulate a minimal model that quantitatively reflects the kinetic behavior of RuBisCOs from different organisms. By relating rate parameters
