Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor.

@article{Mirza2009CrystalSO,
  title={Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor.},
  author={Iram Mirza and Brahm J Yachnin and Shaozhao Wang and Stephan Grosse and H{\'e}l{\`e}ne Bergeron and Akihiro Imura and Hiroaki Iwaki and Yoshie Hasegawa and Peter C. K. Lau and Albert M Berghuis},
  journal={Journal of the American Chemical Society},
  year={2009},
  volume={131 25},
  pages={8848-54}
}
Cyclohexanone monooxygenase (CHMO) is a flavoprotein that carries out the archetypical Baeyer-Villiger oxidation of a variety of cyclic ketones into lactones. Using NADPH and O(2) as cosubstrates, the enzyme inserts one atom of oxygen into the substrate in a complex catalytic mechanism that involves the formation of a flavin-peroxide and Criegee intermediate. We present here the atomic structures of CHMO from an environmental Rhodococcus strain bound with FAD and NADP(+) in two distinct states… CONTINUE READING
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