P450-dependent monooxygenase inhibitor

Foroozesh, M., G. Primrose, Z. Guo, L.C. Bell, W.L. Alworth, and F.P. Guengerich (1997). Aryl acetylenes as mechanism-based inhibitors of cytochrome P450-dependent monooxygenase enzymes. Chem. Res. Toxicol. 10, 91-102. 

The enzyme reaction is inhibited by the typical cytochrome P450 inhibitors. Light reverses the inhibition by carbon monoxide. The obtained data strongly indicate that the DH is a novel cytochrome P450-dependent monooxygenase (pH optimum 8.0). The analysis of the presence of the hydroxylase in nine ceU cultures of seven different plant famUies indicates a very limited taxonomic distribution of this enzyme. 

Sortinl decomposes in plant growth media where one of the products resembles the effects of BSO, a GSH biosynthesis inhibitor. This indicates that a series of observed Sortinl effects might be due to an oxidized cellular environment that it creates. It could be that Sortinl or an active decomposition product sequesters GSH or inhibits GSH production. This may induce the transcription of cytochrome P450-dependent monooxygenases and mixed function oxidases, as shown in the transcription profile after Sortinl treatment. Reduced GSH level then affects flavonoid transport. 

---