- P-ISSN 1225-0163
- E-ISSN 2288-8985
We have examined Raman spectra of cis-peptide model complex, diketopiperazine in water and <TEX>$D_2O$</TEX> with 320 nm through 218 nm excitation. Our study examines assignment of the resonance enhanced amide vibrations and characterizes their enhancement mechanism. Three resonance enhaned cis-peptide marker bands were observed in aqueous solution at 1676, 1533 and <TEX>$806cm^{-1}$</TEX>, which were assigned to the cis-amide I, II and S band, respectively. The <TEX>$1533cm^{-1}$</TEX> amide II band, which is almost pure C-N stretching, was most dominant in water and shifted to <TEX>$1520cm^{-1}$</TEX> upon N-deuteration. This band will be probably a potential probe band for cis-peptide moieties in proteins. The excitation profile data and an Albrecht A-term fit indicated that the cis-peptide vibrations derive their intensities from the 188 nm cis-peptide <TEX>${\pi}-{\pi}^*$</TEX> electronic transition. We Propose that the geometry of cis-peptide <TEX>${\pi}^*$</TEX> excited state is C-N bond displacement relative to that of electronic ground state.