Abstract
The binding of flavin-adenine dinucleotide (FAD) in DT-diaphorase was studies. Incubation with 4M guanidine-HCl at 0°C rapidly dissociated FAD from the enzyme, and incubation of the apo-enzyme with FAD at 37°C restored maximally about 50% (for menadione-reducing activity), or 330% (for ferricyanide-reducing activity) of the initial activity. The half-time required to reconstitute the apo-enzyme with FAD was 2min for menadione-reducing activity and the Km value of the apo-enzyme for FAD was 0.23μM. These results show that DT-diaphorase contains non-covalently bound FAD as a prosthetic group.
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