1.1.3.5	FAD	-	673543	
1.1.3.5	FAD	the enzyme possesses a single catalytic FAD center covalently bound through His 79 and Cys 138 residues with improved stability and cofactor integrity. The redox transformation of FAD during biocatalysis involves a 2e?/2H+ transfer reaction, which is essential for enzymatic activities of FAD-containing enzymes. The formal potential of FAD in HOX, immobilized onto graphite electrodes, estimated as a mean value of the anodic and cathodic peak potentials is less negative than that of free FAD adsorbed directly onto graphite electrodes. Consistent with that, in the presence of glucose, bioelectrocatalysis of glucose oxidation by HOX starts from potentials exceeding those of HOX's FAD	742363