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- W2917178455 abstract "4-Thioflavins react with sulfite under aerobic conditions to yield highly fluorescent products with absorption maxima around 410 nm. These products have been identified as 4-hydroxy-4-sulfonylflavins, and have been shown to arise from a series of reactions following the Oa-dependent reoxidation of an intermediate with absorption maxima at 363 and 465 nm. Under anaerobic conditions, the same intermediate is formed, but decays to a 350 nm absorbing species, which is probably the N(5)-sulfite adduct of 4-thioflavin. A plausible mechanism is described for the formation of the derivatives, and several of their chemical and physical properties are described. Distinctly different results between different proteins are obtained when sulfite reacts with enzyme-bound 4-thioflavins. 4-Thio-FAD-~-amino acid oxidase and 4-thio-FMNlactate oxidase react rapidly to yield the N(S)-sulfite adducts, as occurs with the native enzymes. 4-ThioFAD-p-hydroxybenzoate hydroxylase reacts slowly in a manner paralleling the reaction with the free 4thioflavins." @default.
- W2917178455 created "2019-03-02" @default.
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- W2917178455 date "1984-01-01" @default.
- W2917178455 modified "2023-09-27" @default.
- W2917178455 title "4-Thioflavins as Active Site Probes of Flavoproteins" @default.
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