Characterization of the bifunctional mitochondrial processing peptidase (MPP)/bc1 complex in Spinacia oleracea.

@article{Eriksson1996CharacterizationOT,
  title={Characterization of the bifunctional mitochondrial processing peptidase (MPP)/bc1 complex in Spinacia oleracea.},
  author={Ann Christin Eriksson and Sara Sj{\"o}ling and Elzbieta Glaser},
  journal={Journal of bioenergetics and biomembranes},
  year={1996},
  volume={28 3},
  pages={285-92}
}
The mitochondrial general processing peptidase (MPP) in plant mitochondria constitutes an integral part of the cytochrome bc1 complex of the respiratory chain. Here we present a characterization of this bifunctional complex from spinach leaf mitochondria. The purified MPP/bc1 complex has a molecular mass of 550 kDa, which corresponds to a dimer. Increased ionic strength results in partial dissociation of the dimer as well as loss of the processing activity. Micellar concentrations of nonionic… CONTINUE READING

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