Slow Inactivation of Ribulosebisphosphate Carboxylase during Catalysis Is Caused by Accumulation of a Slow, Tight-Binding Inhibitor at the Catalytic Site.

@article{Edmondson1990SlowIO,
  title={Slow Inactivation of Ribulosebisphosphate Carboxylase during Catalysis Is Caused by Accumulation of a Slow, Tight-Binding Inhibitor at the Catalytic Site.},
  author={D L Edmondson and Murray R. Badger and Timothy J. Andrews},
  journal={Plant physiology},
  year={1990},
  volume={93 4},
  pages={1390-7}
}
The slow inactivation which accompanies catalysis by higher-plant ribulose-P(2) carboxylase-oxygenase (Rubisco) in vitro was only partially reversed when the enzyme was gel filtered to remove small molecules. However, gel filtration or dialysis in the presence of high SO(2-) (4) concentrations induced full recovery. This suggests that the inactivation is caused by a tight-binding inhibitor whose effective affinity is reduced by competition with SO(2-) (4) ions, which are known to bind at the… CONTINUE READING