Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: possible role of the hydroxy amino acid in oxygen activation.

@article{Imai1989UncouplingOT,
  title={Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: possible role of the hydroxy amino acid in oxygen activation.},
  author={Massao Alberto Imai and Hideo Shimada and Yoshihito Watanabe and Yuko Matsushima-Hibiya and Ryu Makino and Hideo Koga and Takao Horiuchi and Yuzuru Ishimura},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1989},
  volume={86 20},
  pages={7823-7}
}
Site-directed mutants of cytochrome P-450cam (the cytochrome P-450 that acts as the terminal monooxygenase in the d-camphor monooxygenase system), in which threonine-252 had been changed to alanine, valine, or serine, were employed to study the role of the hydroxy amino acid in the monooxygenase reaction. The mutant enzymes were expressed in Escherichia coli and were purified by a conventional method. All the mutant enzymes in the presence of d-camphor exhibited optical absorption spectra… CONTINUE READING
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