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- W969709968 abstract "Publisher Summary This chapter describes an improved enzymatic procedure to convert riboflavin analogs to the flavin adenine dinucleotide (FAD) level using Brevibacterium ammoniagenes extracts. High-performance liquid chromatography (HPLC) applications are presented for the purification of flavin analogs and for the study of naturally occurring 5-deazaflavins in methanogenic bacteria. Structural analogs of flavin coenzymes differing in redox potential and reactivity have been used to probe the mechanism for a number of flavoenzymes. Massey and coworkers, among others, have conducted systematic studies of a variety of other flavin analogs at the flavin mononucleotide (FMN) and FAD levels with several apoflavoenzymes. These studies have included 8-thio,2- thio-, and 4-thioflavins among others. The synthetic analogs at the riboflavin level have been converted regiospecifically to the 5′-FMN species and then to the FAD level in a single pot enzymatic incubation with a flavokinase/FAD synthetase mixture from extracts of B. ammoniagenes . Typical incubations produce 50–100 nmol coenzyme analogs, which most conveniently purified by HPLC methods. Analogs at the FMN level are readily prepared from the FAD analogs by treatment with phosphodiesterase from Naja naja ." @default.
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- W969709968 date "1986-01-01" @default.
- W969709968 modified "2023-09-24" @default.
- W969709968 title "[33] Separation of flavins and flavin analogs by high-performance liquid chromatography" @default.
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- W969709968 doi "https://doi.org/10.1016/0076-6879(86)22171-0" @default.
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