Characteristics of the fluorescence spectra of apoenzyme and flavin portions of D-amino acid oxidase

Felicia Ying Hsiueh Wu*, Shiao Chun Tu, Cheng-Wen Wu Lee, Donald B. McCormick

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)381-385
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume41
Issue number2
DOIs
StatePublished - 23 Oct 1970

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