The tryptophan fluorescence maxima for semiholo- and holoenzymes of D-amino acid oxidase are blue-shifted from that of the apoenzyme by 10 and 20 nm, respectively. These findings indicate that tryptophan residues of semiholo and holo forms are in a more nonpolar environment and less accessible to water than those in the apoenzyme. Overall, results suggest that some tryptophan residues may be near or at the flavin active site in D-amino acid oxidase.
|Number of pages||5|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - 23 Oct 1970|