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 language | English |
|---|---|
| Pages (from-to) | 973-974 |
| Number of pages | 2 |
| Journal | Chemical Communications |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - 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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