Resonance Raman spectra of semiquinone forms of flavins bound to riboflavin binding protein.

@article{Nishina1980ResonanceRS,
  title={Resonance Raman spectra of semiquinone forms of flavins bound to riboflavin binding protein.},
  author={Y. Nishina and K. Shiga and K. Horiike and H. Tojo and S. Kasai and K. Matsui and H. Watari and T. Yamano},
  journal={Journal of biochemistry},
  year={1980},
  volume={88 2},
  pages={
          411-6
        }
}
  • Y. Nishina, K. Shiga, +5 authors T. Yamano
  • Published 1980
  • Chemistry, Medicine
  • Journal of biochemistry
  • The resonance Raman (RR) spectra of semiquinones of complexes of riboflavin or 8-methoxyriboflavin (8-OCH3-RF) with riboflavin binding protein (RBP) were observed. The RR spectrum of neutral semiquinone of riboflavin-RBP complex in H2O solution has an intense line at 1617 cm-1, not observed for oxidized riboflavin bound to RBP. The line at 1617 cm-1 does not shift in D2O solution. The absorption spectrum of semiquinone of 8-OCH3-RF bound to RBP has maxima at 586, 396, and 344 nm, and the RR… CONTINUE READING
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