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Deflavination of flavo-oxidases by nucleophilic reagents.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 2001 Aug 13; Vol. 1548 (2), pp. 213-9. - Publication Year :
- 2001
-
Abstract
- Using spectroscopic techniques we studied the effect of the nucleophilic reagents cyanide, cyanate and thiocyanate on three flavo-oxidases namely alcohol oxidase (AO), glucose oxidase (GOX) and D-amino acid oxidase (DAOX). All three ions, added at concentrations in the mM range, caused release of the flavin adenine dinucleotide (FAD) co-factors from the enzyme molecules. In the case of AO this was accompanied by significant conformational perturbations, which was not observed for GOX and DAOX. As suggested from fluorescence, absorption and circular dichroism spectral changes at least one phenolic hydroxyl group became ionized upon FAD release from AO and a new class of Trp residues, fluorescent only in apo-AO protein, was demasked.
- Subjects :
- Alcohol Oxidoreductases chemistry
Circular Dichroism
Cyanates
Cyanides
D-Amino-Acid Oxidase chemistry
Glucose Oxidase chemistry
Indicators and Reagents
Spectrometry, Fluorescence
Spectrophotometry
Thiocyanates
Flavin-Adenine Dinucleotide chemistry
Flavoproteins chemistry
Oxidoreductases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1548
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 11513966
- Full Text :
- https://doi.org/10.1016/s0167-4838(01)00233-3