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- W2000681294 abstract "Resonance Raman (RR) spectroscopy on various ionic species of 8-mercaptoriboflavin in aqueous solution shows large vibrational spectral changes upon ionization of the 8-SH group. These changes and the superposition of the RR excitation profile and the visible spectrum for the 8-S− species indicate that there is a substantial amount of the “quinoid thioketone” resonance form present in aqueous solutions of the 8-S− mercaptoriboflavin. RR spectra of 8-mercaptoriboflavin bound to riboflavin binding protein confirm the conclusion (reached on the basis of visible spectra) that the 8-mercaptoriboflavin binds to the protein in the 8-SH, protonated, form. There are, however, changes in the 1250-cm−1 region of the RR spectrum upon binding aqueous 8-mercaptoflavin to the protein. The 1257-cm−1 band in aqueous solution moves to 1248 cm−1 on the protein surface. This shift is also observed in DMSO solution of 8-mercaptoriboflavin. Since the 1257-cm−1 band shifts upon formation of the N-3 deuteroriboflavin, we interpret this lowering of a δ-H mode at N-3 to mean that there is weaker hydrogen bonding between flavin N-3 and riboflavin binding protein than between flavin and water." @default.
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- W2000681294 date "1982-04-01" @default.
- W2000681294 modified "2023-09-26" @default.
- W2000681294 title "Resonance Raman studies on 8-mercaptoriboflavin" @default.
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- W2000681294 doi "https://doi.org/10.1016/0003-9861(82)90274-0" @default.
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