Abstract
1. 1.|Glucose dehydrogenase from Aspergillus oryzae was inhibited by Ag +, Hg 2+ and Cu 2+, but was insensitive to sulfhydryl reagents. 2. 2.|The involvement of a histidyl residue (or residues) in the activity was suggested from photoinactivation in the presence of methylene blue, the pH dependence of K m for glucose, and titration with the histidine-specific reagent, diazo- i-H-tetrazole (DHT). 3. 3.|The inhibiton by Ag + was reversed by dialysis and by addition of a high concentration of glucose. The activity of DHT-inhibited enzyme was not restored by dialysis, and high concentrations of glucose partly protected the enzyme from DHT inhibition only when added prior to the addition of DHT. 4. 4.|The reducton of the enzyme-bound FAD by glucose was prevented in the Ag +- or DHT-treated enzyme, but the reoxidation of the reduced flavin by vitamin K 3 was not impaired in the trested enzyme. 5. 5.|It was concluded that a histidyl residue is involved in the reduction of the flavin by glucose, acting probably as the glucose-binding site.
Published Version
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