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

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 spectrum doublet lines at 1623 and 1615 cm-1. In D2O solution, the 1623 cm-1 line does not shift, but the 1615 cm-1 line shifts to 1604 cm-1. The line around 1620 cm-1 for the flavin semiquinone will be useful in the determination of the redox state of flavin.