Resonance Raman Spectroscopic Study of Bilirubin Hydrogen Bonding in Solutions and in the Albumin Complex

You-Zung Hsieh, Michael D. Morris*

*Corresponding author for this work

Research output: Contribution to journalArticle

40 Scopus citations

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 languageEnglish
Pages (from-to)62-67
Number of pages6
JournalJournal of the American Chemical Society
Volume110
Issue number1
DOIs
StatePublished - 1 Jan 1988

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