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Direct electron transfer reactions between human ceruloplasmin and electrodes.

Haberska, Karolina LU ; Vaz Dominguez, Cristina LU ; De Lacey, Antonio L ; Dagys, Marius ; Reimann, Curt LU and Shleev, Sergey LU (2009) In Bioelectrochemistry 76. p.34-41
Abstract
In an effort to find conditions favouring bioelectrocatalytic reduction of oxygen by surface-immobilised human ceruloplasmin (Cp), direct electron transfer (DET) reactions between Cp and an extended range of surfaces were considered. Exploiting advances in surface nanotechnology, bare and carbon-nanotube-modified spectrographic graphite electrodes as well as bare, thiol- and gold-nanoparticle-modified gold electrodes were considered, and ellipsometry provided clues as to the amount and form of adsorbed Cp. DET was studied under different conditions by cyclic voltammetry and chronoamperometry. Two Faradaic processes with midpoint potentials of about 400 mV and 700 mV vs. NHE, corresponding to the redox transformation of copper sites of Cp,... (More)
In an effort to find conditions favouring bioelectrocatalytic reduction of oxygen by surface-immobilised human ceruloplasmin (Cp), direct electron transfer (DET) reactions between Cp and an extended range of surfaces were considered. Exploiting advances in surface nanotechnology, bare and carbon-nanotube-modified spectrographic graphite electrodes as well as bare, thiol- and gold-nanoparticle-modified gold electrodes were considered, and ellipsometry provided clues as to the amount and form of adsorbed Cp. DET was studied under different conditions by cyclic voltammetry and chronoamperometry. Two Faradaic processes with midpoint potentials of about 400 mV and 700 mV vs. NHE, corresponding to the redox transformation of copper sites of Cp, were clearly observed. In spite of the significant amount of Cp adsorbed on the electrode surfaces, as well as the quite fast DET reactions between the redox enzyme and electrodes, bioelectrocatalytic reduction of oxygen by immobilised Cp was never registered. The bioelectrocatalytic inertness of this complex multi-functional redox enzyme interacting with a variety of surfaces might be associated with a very complex mechanism of intramolecular electron transfer involving a kinetic trapping behaviour. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Bioelectrochemistry
volume
76
pages
34 - 41
publisher
Elsevier
external identifiers
  • wos:000270014400008
  • pmid:19535300
  • scopus:68549118693
  • pmid:19535300
ISSN
1878-562X
DOI
10.1016/j.bioelechem.2009.05.012
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)
id
83f69401-8d14-42bf-aaa0-a88c1dea0d8f (old id 1434174)
date added to LUP
2016-04-01 12:15:06
date last changed
2020-02-26 03:12:20
@article{83f69401-8d14-42bf-aaa0-a88c1dea0d8f,
  abstract     = {In an effort to find conditions favouring bioelectrocatalytic reduction of oxygen by surface-immobilised human ceruloplasmin (Cp), direct electron transfer (DET) reactions between Cp and an extended range of surfaces were considered. Exploiting advances in surface nanotechnology, bare and carbon-nanotube-modified spectrographic graphite electrodes as well as bare, thiol- and gold-nanoparticle-modified gold electrodes were considered, and ellipsometry provided clues as to the amount and form of adsorbed Cp. DET was studied under different conditions by cyclic voltammetry and chronoamperometry. Two Faradaic processes with midpoint potentials of about 400 mV and 700 mV vs. NHE, corresponding to the redox transformation of copper sites of Cp, were clearly observed. In spite of the significant amount of Cp adsorbed on the electrode surfaces, as well as the quite fast DET reactions between the redox enzyme and electrodes, bioelectrocatalytic reduction of oxygen by immobilised Cp was never registered. The bioelectrocatalytic inertness of this complex multi-functional redox enzyme interacting with a variety of surfaces might be associated with a very complex mechanism of intramolecular electron transfer involving a kinetic trapping behaviour.},
  author       = {Haberska, Karolina and Vaz Dominguez, Cristina and De Lacey, Antonio L and Dagys, Marius and Reimann, Curt and Shleev, Sergey},
  issn         = {1878-562X},
  language     = {eng},
  pages        = {34--41},
  publisher    = {Elsevier},
  series       = {Bioelectrochemistry},
  title        = {Direct electron transfer reactions between human ceruloplasmin and electrodes.},
  url          = {http://dx.doi.org/10.1016/j.bioelechem.2009.05.012},
  doi          = {10.1016/j.bioelechem.2009.05.012},
  volume       = {76},
  year         = {2009},
}