Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase

J.J. Prompers, C.W. Hilbers, H.A.M. Pepermans

    Research output: Contribution to journalArticleAcademicpeer-review

    70 Citations (Scopus)

    Abstract

    The fluorescence signal of the single tryptophan residue (Trp69) of Fusarium solani pisi cutinase is highly quenched. However, prolonged irradiation of the enzyme in the tryptophan absorption band causes an increase of the tryptophan fluorescence quantum yield by an order of magnitude. By using a combination of NMR spectroscopy and chemical detection of free thiol groups with a sulfhydryl reagent we could unambiguously show that the unusual fluorescence behaviour of Trp69 in cutinase is caused by the breaking of the disulfide bond between Cys31 and Cys109 upon irradiation, while the amide-aromatic hydrogen bond between Ala32 and Trp69 remains intact. This is the first example of tryptophan mediated photoreduction of a disulfide bond in proteins. Copyright (C) 1999 Federation of European Biochemical Societies.
    Original languageEnglish
    Pages (from-to)409-416
    Number of pages8
    JournalFEBS Letters
    Volume456
    Issue number3
    DOIs
    Publication statusPublished - 1999

    Fingerprint

    Dive into the research topics of 'Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase'. Together they form a unique fingerprint.

    Cite this