Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time-resolved flavin fluorescence.
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.
D000495:Allosteric Site; D008058:Dihydrolipoamide Dehydrogenase / Q000378:metabolism*; D004912:Erythrocytes / Q000201:enzymology; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism*; D005453:Fluorescence; D005980:Glutathione Reductase / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D011487:Protein Conformation
D005182:Flavin-Adenine Dinucleotide; D008058:Dihydrolipoamide Dehydrogenase; D005980:Glutathione Reductase