Crystal structure of cytochrome P450 CYP105N1 from Streptomyces coelicolor, an oxidase in the coelibactin siderophore biosynthetic pathway.

@article{Lim2012CrystalSO,
  title={Crystal structure of cytochrome P450 CYP105N1 from Streptomyces coelicolor, an oxidase in the coelibactin siderophore biosynthetic pathway.},
  author={Young-ran Lim and Myoung-Ki Hong and Jin-Kwang Kim and Thanh Thi Ngoc Doan and Dong-Hyun Kim and Chul-Ho Yun and Y C Chun and Lin-Woo Kang and Donghak Kim},
  journal={Archives of biochemistry and biophysics},
  year={2012},
  volume={528 2},
  pages={111-7}
}
The genome sequence of Streptomyces coelicolor contains 18 cytochrome P450 enzymes. The recombinant CYP105N1 protein has been expressed in Escherichia coli and purified, and we report the biochemical and structural characterization of CYP105N1 from S. coelicolor. The purified protein exhibited the typical CO-binding spectrum of P450 enzymes and type I binding spectra with estradiol and a coelibactin analog. The oxidation of estradiol by CYP105N1, supported by H(2)O(2), produced estriol. The… CONTINUE READING