Issue 8, 1996

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

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 pretected 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.

Article information

Article type
Paper

Chem. Commun., 1996, 973-974

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

H. Yin, C. Chan, J. Garforth, K. T. Douglas, M. S. Bolgar, S. J. Gaskell and A. H. Fairlamb, Chem. Commun., 1996, 973 DOI: 10.1039/CC9960000973

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