The Purification and Characterization of the o-type Cytochrome Oxidase from Methylophilus methylotrophus, and its Reconstitution into a ‘Methanol Oxidase’ Electron Transport Chain

@inproceedings{Froud1984ThePA,
  title={The Purification and Characterization of the o-type Cytochrome Oxidase from Methylophilus methylotrophus, and its Reconstitution into a ‘Methanol Oxidase’ Electron Transport Chain},
  author={Stephen J. Froud and Christopher Anthony},
  year={1984}
}
The o-type cytochrome oxidase from methanol-grown Methylophilus methylotrophus has been solubilized and purified (15-fold) to homogeneity. The pure, active oxidase consisted of equal amounts of b-type and c-type cytochromes, corresponding to the two types of protein subunit seen on SDS-PAGE; these had molecular weights of 31 500 and 23800, respectively. The active oxidase probably has two cytochrome c subunits and two cytochrome b subunits, both cytochrome types reacting with CO. The cytochrome… CONTINUE READING

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Cytochromes c

  • Springer Series in Molecular Biology
  • 1987

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