The kinetics of the bioelectrocatalytic reduction of hydrogen peroxide has been studied at gold electrodes modified with different forms of horseradish peroxidase (HRP). Native HRP, wild type recombinant HRP (rec-HRP) and its two mutant forms containing a six-histidine tag at the C- or N-terminus, C(His)rec-HRP and N(His)rec-HRP, respectively, have been used for an adsorptive modification of the gold electrodes. The histidine sequences, i.e, histidine tags, were introduced into the peroxidase structure by genetic engineering of non-glycosylated rec-HRP using an Escherichia coli expression system. Experiments with a gold rotating disc electrode demonstrated that electrodes with the adsorbed rec-HRP forms exhibited high and stable current response to H2O2 due to its bioelectrocatalytic reduction based on direct (mediatorless) ET between gold and the active site of HRP. The heterogeneous ET rate constants were evaluated to be in the order of 20 or 33 s(-1) between rec-HRP or its histidine mutants and gold, respectively, in 0.01 M phosphate buffer (pH 7.4) containing 0.15 M NaCl. The increase in the heterogeneous ET rate found for C(His)rec-HRP and N(His)rec-HRP is probably due to the interaction of the histidine tag with the electrode surface. The kinetic data demonstrate that new possibilities for enhancing the catalytic activity of the enzyme at the electrode I solution interface can be achieved by genetic engineering design of the enzyme molecules.