학술논문

Time-resolved fluorescence of flavin adenine dinucleotide in wild-type and mutant NADH peroxidase. Elucidation of quenching sites and discovery of a new fluorescence depolarization mechanism
Document Type
Academic Journal
Source
Journal of Physical Chemistry B. Dec 10, 1998, Vol. 102 Issue 50, p10431, 9 p. 3
Subject
Fluorescence -- Usage
Peroxidase -- Research
Enzymes -- Research
Glutathione -- Research
Language
ISSN
1520-6106
Abstract
A study was conducted to analyze the flavin adenine dinucleotide of tetrameric NADH peroxidase from Enterococcus faecalis and three mutant enzymes using time-resolved polarized fluorescence. The energy transfer between the flavins in various subunits within dimeric flavoproteins were determined by time-resolved fluorescence anisotropy analysis ofthe bound flavin cofactor. Results indicated that fluorescence lifetime heterogeneity was not limited to glutathione reductase.