Direct heterogeneous electron transfer of recombinant horseradish peroxidases on gold.
Clean polycrystalline gold electrodes were modified with native glycosylated horseradish peroxidases (HRP) or two different recombinant (carbohydrate free) HRPs; recombinant wild-type HRP (rec-HRP) and recombinant HRP containing a six histidine-tag at the C-terminus of the polypeptide chain (rec-HRP-His), respectively. Only the electrodes modified with the recombinant HRPs exhibited high current responses to H2O2 due to relatively rapid direct electron transfer (ET) between recombinant HRP and gold. The absence of a carbohydrate shell on rec-HRP and the additionally existing histidine-tag on rec-HRP-His improved the electrode sensitivity to H2O2 by more than 100 times if compared with the response observed at gold modified with native HRP. Rotating disk electrode experiments indicated that the heterogeneous electron transfer rates are equal to 4.7 and 7.5 s-1 for direct electron transfer between the gold electrode and rec-HRP or rec-HRP-His, respectively.
Presnova
G
G
Moscow State University, 119899 Vorobyevy Gory, Moscow, Russia.
Grigorenko
V
V
Egorov
A
A
Ruzgas
T
T
Lindgren
A
A
Gorton
L
L
Börchers
T
T
D004563:Electrochemistry; D004579:Electron Transport; D004800:Enzymes, Immobilized; D006046:Gold / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
D004800:Enzymes, Immobilized; D011994:Recombinant Proteins; D006046:Gold; D006735:Horseradish Peroxidase