Fluphenazine photoaffinity labelling of binding sites for phenothiazine inhibitors of trypanothione reductase

  • Hong Yin
  • , Cecil Chan
  • , Jacqui Garforth
  • , Kenneth T. Douglas
  • , Mark S. Bolgar
  • , Simon J. Gaskell
  • , Alan H. Fairlamb

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Photolysis of fluphenazine, a competitive inhibitor of trypanothione reductase in the presence of trypanothione reductase leads to irreversible, time-dependent inactivation, which is not dependent on the presence of molecular oxygen in the medium and can be protected against by the presence of trypanothione substrate; MALDI and electrospray mass spectrometric analyses shows that 2-5 equiv. of the phenothiazine are incorporated per enzyme subunit.

    Original languageEnglish
    Pages (from-to)973-974
    Number of pages2
    JournalChemical Communications
    Issue number8
    DOIs
    Publication statusPublished - 1996

    ASJC Scopus subject areas

    • Catalysis
    • Electronic, Optical and Magnetic Materials
    • Ceramics and Composites
    • General Chemistry
    • Surfaces, Coatings and Films
    • Metals and Alloys
    • Materials Chemistry

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