The oxygenated form of L-tryptophan 2,3-dioxygenase as reaction intermediate.

@article{Ishimura1970TheOF,
  title={The oxygenated form of L-tryptophan 2,3-dioxygenase as reaction intermediate.},
  author={Yuzuru Ishimura and Mitsuhiro Nozaki and Osamu Hayaishi},
  journal={The Journal of biological chemistry},
  year={1970},
  volume={245 14},
  pages={3593-602}
}
In order to clarify the reaction mechanism of Mryptophan 2,3-dioxygenase (L-tryptophan: oxygen oxidoreductase, EC 1.13.1.12), a hemoprotein, spectral and kinetic studies were carried out with highly puritied enzyme preparations from Pseudomonas fluorescens (ATCC 11299). A new spectrally distinct species of the enzyme heme omx; 418,545, and 580 mp) was observed during the steady state of the catalytic reaction. The formation of the new spectral species was absolutely dependent on the… CONTINUE READING
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