Effect of pH on direct electron transfer in the system gold electrode-recombinant horseradish peroxidase
(2002) In Bioelectrochemistry 55. p.83-87- Abstract
- The effect of pH on the kinetics of the bioelectrocatalytic reduction of H2O2 catalysed by horseradish peroxidase (HRP) has been studied at –50 mV vs. AgjAgCl on HRP-modified Au electrodes placed in a wall-jet flow-through electrochemical cell. Native HRP (nHRP) and a
nonglycosylated recombinant form containing a six-histidine tag at the C-terminus, CHisrHRP, produced by genetic engineering of nonglycosylated recombinant HRP using an E. coli expression system, have been used for adsorptive modification of Au electrodes. A favourable adsorption of CHisrHRP on preoxidised Au from a protein solution at pH 6.0 provided a high and stable current response to H2O2
due to its bioelectrocatalytic reduction based on direct... (More) - The effect of pH on the kinetics of the bioelectrocatalytic reduction of H2O2 catalysed by horseradish peroxidase (HRP) has been studied at –50 mV vs. AgjAgCl on HRP-modified Au electrodes placed in a wall-jet flow-through electrochemical cell. Native HRP (nHRP) and a
nonglycosylated recombinant form containing a six-histidine tag at the C-terminus, CHisrHRP, produced by genetic engineering of nonglycosylated recombinant HRP using an E. coli expression system, have been used for adsorptive modification of Au electrodes. A favourable adsorption of CHisrHRP on preoxidised Au from a protein solution at pH 6.0 provided a high and stable current response to H2O2
due to its bioelectrocatalytic reduction based on direct (mediatorless) electron transfer (ET) between Au and the active site of HRP. The heterogeneous ET rate constant, ks, calculated from experimental data on direct ET, on mediated ET in the presence of catechol as well as from microbalance data, increased more than 30 times when changing from nHRP to CHisrHRP. For both forms of HRP, the increasing
efficiency of bioelectrocatalysis with increasing [H3O+ ] was observed. The values of the apparent ks between CHisrHRP and Au changed from a value of 12F2 s 1 in PBS at pH 8.0 to a value of 434F62 s 1 at pH 6.0; a similar ks–pH dependence was also observed for nHRP, providing the possibility to consider the reaction mechanism involving the participation of a proton in the rate-determining step of the charge transfer. (Less)
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https://lup.lub.lu.se/record/119259
- author
- Ferapontova, Elena LU and Gorton, Lo LU
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Recombinant horseradish peroxidase, Heterogeneous direct electron transfer, Bioelectrocatalysis, Au electrode, Proton transfer
- in
- Bioelectrochemistry
- volume
- 55
- pages
- 83 - 87
- publisher
- Elsevier
- external identifiers
-
- wos:000176715500022
- pmid:11786347
- scopus:0036148399
- ISSN
- 1878-562X
- DOI
- 10.1016/S1567-5394(01)00158-X
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004)
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- bde1a8d9-300e-4f44-928d-418114d53658 (old id 119259)
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- date added to LUP
- 2016-04-04 08:33:32
- date last changed
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@article{bde1a8d9-300e-4f44-928d-418114d53658,
abstract = {{The effect of pH on the kinetics of the bioelectrocatalytic reduction of H2O2 catalysed by horseradish peroxidase (HRP) has been studied at –50 mV vs. AgjAgCl on HRP-modified Au electrodes placed in a wall-jet flow-through electrochemical cell. Native HRP (nHRP) and a<br/><br>
nonglycosylated recombinant form containing a six-histidine tag at the C-terminus, CHisrHRP, produced by genetic engineering of nonglycosylated recombinant HRP using an E. coli expression system, have been used for adsorptive modification of Au electrodes. A favourable adsorption of CHisrHRP on preoxidised Au from a protein solution at pH 6.0 provided a high and stable current response to H2O2<br/><br>
due to its bioelectrocatalytic reduction based on direct (mediatorless) electron transfer (ET) between Au and the active site of HRP. The heterogeneous ET rate constant, ks, calculated from experimental data on direct ET, on mediated ET in the presence of catechol as well as from microbalance data, increased more than 30 times when changing from nHRP to CHisrHRP. For both forms of HRP, the increasing<br/><br>
efficiency of bioelectrocatalysis with increasing [H3O+ ] was observed. The values of the apparent ks between CHisrHRP and Au changed from a value of 12F2 s 1 in PBS at pH 8.0 to a value of 434F62 s 1 at pH 6.0; a similar ks–pH dependence was also observed for nHRP, providing the possibility to consider the reaction mechanism involving the participation of a proton in the rate-determining step of the charge transfer.}},
author = {{Ferapontova, Elena and Gorton, Lo}},
issn = {{1878-562X}},
keywords = {{Recombinant horseradish peroxidase; Heterogeneous direct electron transfer; Bioelectrocatalysis; Au electrode; Proton transfer}},
language = {{eng}},
pages = {{83--87}},
publisher = {{Elsevier}},
series = {{Bioelectrochemistry}},
title = {{Effect of pH on direct electron transfer in the system gold electrode-recombinant horseradish peroxidase}},
url = {{http://dx.doi.org/10.1016/S1567-5394(01)00158-X}},
doi = {{10.1016/S1567-5394(01)00158-X}},
volume = {{55}},
year = {{2002}},
}