Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases.

@article{Edmondson2009MolecularAM,
  title={Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases.},
  author={Dale E. Edmondson and Claudia Binda and Jin Wang and Anup K Upadhyay and Andrea Mattevi},
  journal={Biochemistry},
  year={2009},
  volume={48 20},
  pages={4220-30}
}
The past decade has brought major advances in our knowledge of the structures and mechanisms of MAO A and MAO B, which are pharmacological targets for specific inhibitors. In both enzymes, crystallographic and biochemical data show their respective C-terminal transmembrane helices anchor the enzymes to the outer mitochondrial membrane. Pulsed EPR data show both enzymes are dimeric in their membrane-bound forms with agreement between distances measured in their crystalline forms. Distances… CONTINUE READING