Detoxication of carboxin
β Scribed by Prof. Dr. H. Lyr; G. Ritter; L. Banasiak
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 427 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0233-111X
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β¦ Synopsis
Abstract
Carboxin (= vitavax = DCMO) is rapidly oxidized by hydrogen peroxide or H~2~O~2~ generating systems as riboflavin, flavin enzymes with or without substrate, to the more water soluble nontoxic sulfoxid (DCMOS). Illumination enhances the inactivation. Peroxidase is without effect. Isolated mitochondria from sensitive as well as from insensitive fungal species have the ability to oxidize DCMO, which leads to a leakage of the compounds mainly in form of DCMOS from the mitochondria. Among several fungal species investigated only Ustilago maydis in vivo oxidizes DCMO to a higher degree. The further oxidation of DCMOS to the corresponding dioxid (DCMOD = plantvax) occurs only under certain conditions to a limited extent. Proteases are unable to attack the β CONHβbounding. It is assumed that in vivo mainly flavin enzymes are responsible for the rapid oxidative inactivation of DCMO (vitavax).
π SIMILAR VOLUMES
83 fungal species were tested for their correlation between carboxin sensitivity and glycolytic ability regarding the taxonomic position of the test fungi. Besides basidiomycetes the ascomycetous orders __Helotiales, Sordariales, Chaetomiales__, and __Dothiorales__ showed carboxin sensitivity which