The primary structure of cytochrome P460 of Nitrosomonas europaea: presence of a c-heme binding motif.

@article{Bergmann1994ThePS,
  title={The primary structure of cytochrome P460 of Nitrosomonas europaea: presence of a c-heme binding motif.},
  author={Dr. P. J. Bergmann and Alan B. Hooper},
  journal={FEBS letters},
  year={1994},
  volume={353 3},
  pages={324-6}
}
Cytochrome P460 and hydroxyamine oxidoreductase of Nitrosomonas europaea both catalyze the oxidation of hydroxylamine and contain a 460 nm-absorbing chromophore. The gene (cyp) encoding cytochrome P460 was cloned and sequenced. The predicted amino acid sequence contains a single c-heme binding motif (CXXCH) near the carboxy-terminus. Cytochrome P460 shows little sequence homology to other c-cytochromes including hydroxyamine oxidoreductase. The presence of a signal peptide and a possible c-heme… CONTINUE READING

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