Abstract
Resonance Raman spectra are reported for bilirubin in chloroform, dimethyl sulfoxide, and aqueous solutions, and for the 1:1 bilirubin/albumin complex and the bilirubin complexes of α- and β-cyclodextrin. From the known hydrogen-bonding patterns in the several free solutions, Raman markers for the presence or absence of internal hydrogen bonding are derived. From equilibrium and time-resolved deuteration, partial assignments of the spectra are proposed. The resonance Raman spectrum of the bilirubin/albumin complex demonstrates that the internal hydrogen bonds between propionate groups and the pyrromethenone rings are ruptured. Propionate hydrogen bonding is to amino acid residues of the protein only.
| Original language | English |
|---|---|
| Pages (from-to) | 62-67 |
| Number of pages | 6 |
| Journal | Journal of the American Chemical Society |
| Volume | 110 |
| Issue number | 1 |
| DOIs | |
| State | Published - 1 Jan 1988 |