Electron spin-echo studies of the composition of the paramagnetic intermediate formed during the deamination of propanolamine by ethanolamine ammonia-lyase, and AdoCbl-dependent enzyme.

@article{Tan1986ElectronSS,
  title={Electron spin-echo studies of the composition of the paramagnetic intermediate formed during the deamination of propanolamine by ethanolamine ammonia-lyase, and AdoCbl-dependent enzyme.},
  author={S L Tan and M G Kopczynski and William W. Bachovchin and William H. Orme-Johnson and B M Babior},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 8},
  pages={3483-5}
}
During the deamination of S-2-aminopropanol by the AdoCbl-dependent ethanolamine ammonia-lyase of Clostridia sp., a catalytic intermediate accumulates whose active site contains two paramagnetic species: cob(II)alamin and a free radical derived from the substrate molecule. Spin-echo spectroscopy has revealed that the unpaired electron on the substrate… CONTINUE READING