Flavine-protein interactions in flavoenzymes. Effect of chemical modification of tryptophan residues upon flavine mononucleotide binding and protein fluorescence in Azotobacter flavodoxin.
D000596:Amino Acids / Q000032:analysis; D001059:Apoproteins / Q000032:analysis; D001395:Azotobacter / Q000032:analysis*; D001426:Bacterial Proteins / Q000032:analysis*; D001565:Benzoates; D001665:Binding Sites; D001965:Bromides; D002848:Chromatography, DEAE-Cellulose; D002942:Circular Dichroism; D004589:Electrophoresis, Disc; D005486:Flavin Mononucleotide; D005420:Flavoproteins / Q000032:analysis*; D010084:Oxidation-Reduction; D011485:Protein Binding; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013386:Succinates; D013438:Sulfhydryl Compounds / Q000032:analysis; D014364:Tryptophan / Q000032:analysis*
D000596:Amino Acids; D001059:Apoproteins; D001426:Bacterial Proteins; D001565:Benzoates; D001965:Bromides; D005420:Flavoproteins; D013386:Succinates; D013438:Sulfhydryl Compounds; D005486:Flavin Mononucleotide; D014364:Tryptophan