In vitro heme O synthesis by the cyoE gene product from Escherichia coli.

@article{Saiki1993InVH,
  title={In vitro heme O synthesis by the cyoE gene product from Escherichia coli.},
  author={Keitarou Saiki and Tatsushi Mogi and Ken-ichi Ogura and Yasuhiro Anraku},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 35},
  pages={26041-4}
}
The cytochrome bo complex is a heme-copper terminal quinol oxidase in the aerobic respiratory chain of Escherichia coli and contains low spin heme B, high spin heme O and CuB as the redox metal centers in subunit I. Based on site-directed mutagenesis studies on the cyoE gene in the cytochrome bo operon, we have postulated that the cyoE gene encodes a protoheme IX farnesyltransferase (heme O synthase) (Saiki, K., Mogi, T., and Anraku, Y. (1992) Biochem. Biophys. Res. Commun. 189, 1491-1497). The… CONTINUE READING

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