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Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time‐resolved flavin fluorescence
Author(s) -
de Kok A.,
Visser A.J.W.G.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81033-5
Subject(s) - flavin group , glutathione reductase , chemistry , flavin adenine dinucleotide , glutathione , fluorescence , reductase , biochemistry , fluorescence anisotropy , flavoprotein , biophysics , enzyme , cofactor , biology , glutathione peroxidase , physics , optics , membrane
Subnanosecond‐resolved fluorescence measurements of the FAD bound in glutathione reductase and lipoamide dehydrogenase revealed characteristic differences in dynamic properties of both enzymes, which are considered to have common structural features. The flavin fluorescence in glutathione reductase is quenched mainly via a dynamic mechanism, in agreement with enhanced flexibility of the flavin as inferred from rapid depolarization of the fluorescence.