Resonance Raman spectra of flavin semiquinones stabilized by N5 methylation.
Resonance Raman spectra are reported for the semiquinone of N5-methyl derivatives of FMN (flavin mononucleotide) in H2O and 2H2O, 8-chloro FMN and FAD (flavin adenine dinucleotide) with 647.1 nm excitation, in the first pi-pi absorption band, using KI to quench fluorescence. The spectral pattern is similar to that of oxidized flavin, in its first absorption band, but with appreciable shifts, up to approx. 50 cm-1, in corresponding frequencies. There are also significant shifts with respect to the previously reported resonance Raman spectrum of flavodoxin semiquinone, reflecting the substitution of CH3 for H at N5. The N5-methyl FAD semiquinone spectrum is also reported for 514.5 nm excitation, in resonance with the second pi-pi transition. The intensity pattern is quite different, the spectrum being dominated by a band at 1611 cm-1, assigned to a mode localized primarily on the central pyrazine ring.
D002352:Carrier Proteins / Q000378:metabolism; D004355:Drug Stability; D005486:Flavin Mononucleotide; D005182:Flavin-Adenine Dinucleotide / Q000031:analogs & derivatives*; D026901:Membrane Transport Proteins; D008745:Methylation; D012256:Riboflavin / Q000378:metabolism; D013053:Spectrophotometry; D013059:Spectrum Analysis, Raman; D013329:Structure-Activity Relationship
D002352:Carrier Proteins; D026901:Membrane Transport Proteins; C019079:riboflavin-binding protein; D005182:Flavin-Adenine Dinucleotide; C029276:flavin semiquinone; D005486:Flavin Mononucleotide; D012256:Riboflavin