Spectral studies of the tryptophan exposure in the enzyme rhodanese

Kathleen Guido, Richard D. Baillie, Paul M. Horowitz

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Tryptophan exposure in the enzyme rhodanese (thiosulfate; cyanide sulfur-transferase, EC 2.8.1.1) has been studied by the methods of solvent perturbation difference spectroscopy, fluorescence spectroscopy and fluorescence quenching. The data from all these techniques are consistent with two classes of tryptophan: surface and buried. The surface residues appear to be relatively shielded and in an anionic environment. The buried residues have spectral characteristics suggesting they are in a very apolar environment and have less than the expected contact with the peptide backbone. The solvent perturbation difference spectra indicate further that additional tyrosine as well as tryptophan residues are buried as rhodanese is converted from the free enzyme to the sulfur-substituted enzyme: forms which are obligatory intermediates with previous results.

Original languageEnglish (US)
Pages (from-to)600-607
Number of pages8
JournalBBA - Protein Structure
Volume427
Issue number2
DOIs
StatePublished - Apr 14 1976
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)

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