Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time‐resolved flavin fluorescence
- 22 June 1987
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 218 (1) , 135-138
- https://doi.org/10.1016/0014-5793(87)81033-5
Abstract
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.Keywords
This publication has 14 references indexed in Scilit:
- Artefact and Distortion Sources in Time Correlated Single Photon CountingInstrumentation Science & Technology, 1985
- SPECTROSCOPIC AND DYNAMIC CHARACTERIZATION OF FMN IN REVERSED MICELLES ENTRAPPED WATER POOLSPhotochemistry and Photobiology, 1984
- Crystallization and preliminary X-ray investigation of lipoamide dehydrogenase from Azotobacter vinelandiiJournal of Molecular Biology, 1983
- Binding and dissociation of the pyruvate dehydrogenase complex of Azotobacter vinelandii on thiol—SepharoseFEBS Letters, 1982
- PYRUVATE DEHYDROGENASE COMPLEX FROM Azotohacter vinelandii: STRUCTURE, FUNCTION, AND INTER‐ENZYME CATALYSIS*Annals of the New York Academy of Sciences, 1982
- Three-dimensional structure of glutathione reductase at 2 Å resolutionJournal of Molecular Biology, 1981
- Fluorescence Polarization and Energy‐Transfer Studies on the Pyruvate Dehydrogenase Complex of Escherichia coliEuropean Journal of Biochemistry, 1980
- Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranesBiophysical Journal, 1980
- Protein Mobility Inside Pyruvate Dehydrogenase Complexes as Reflected by Laser‐Pulse FluorometryEuropean Journal of Biochemistry, 1980
- Synthetic flavinyl peptides related to the active site of mitochondrial monoamine oxidase. II. Fluorescence propertiesBiochemistry, 1976