Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry.

@article{Kirkman1999MechanismsOP,
  title={Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry.},
  author={Henry N. Kirkman and Michela Rolfo and Anna Maria Ferraris and Gian Franco Gaetani},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 20},
  pages={13908-14}
}
NADPH is known to be tightly bound to mammalian catalase and to offset the ability of the substrate of catalase (H2O2) to convert the enzyme to an inactive state (compound II). In the process, the bound NADPH becomes NADP+ and is replaced by another molecule of NADPH. This protection is believed to occur through electron tunneling between NADPH on the… CONTINUE READING