Molecular relaxation spectroscopy of flavin adenine dinucleotide in wild type and mutant lipoamide dehydrogenase from Azotobacter vinelandii.

Abstract excerpt

The temperature dependence of the fluorescence emission spectra of flavin adenine dinucleotide bound to lipoamide dehydrogenase from Azotobacter vinelandii shows that the protein matrix in the vicinity of the prosthetic group is rigid on a nanosecond time scale in a medium of high viscosity (80% glycerol). The active site of a deletion mutant of this enzyme, which lacks 14 C-terminal amino acids, is converted...

Topics

• Azotobacter vinelandii
• Binding Sites
• Dihydrolipoamide Dehydrogenase
• Flavin-Adenine Dinucleotide
• Fluorescence Polarization
• Mutation
• Spectrum Analysis
• Temperature