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Spectroelectrochemical study of heme- and molybdopterin cofactor-containing chicken liver sulphite oxidase

Ferapontova, Elena LU ; Christenson, Andreas LU ; Hellmark, Anja and Ruzgas, Tautgirdas LU (2004) In Bioelectrochemistry 63(1-2). p.49-53
Abstract
Electron transfer (ET) in sulphite oxidase (SOx), a heme- and molybdopterin cofactor-containing enzyme, was studied spectroelectrochemically using capillary gold electrode modified with aldrithiol. Direct electron exchange between SOx and the surface of modified gold was observed, with a formal potential of -115 mV vs. AgAgCl, KClsat at pH 7.0. This value agreed well with that previously reported for redox transformation of the heme domain of SOx. However, no bioelectrocatalysis of sulphite oxidation was observed in phosphate buffer solutions. This fact evidently correlated with known inhibition of intramolecular ET in SOx by the presence of bivalent inorganic anions. After changing to a Tris buffer solution, spectra variations and cyclic... (More)
Electron transfer (ET) in sulphite oxidase (SOx), a heme- and molybdopterin cofactor-containing enzyme, was studied spectroelectrochemically using capillary gold electrode modified with aldrithiol. Direct electron exchange between SOx and the surface of modified gold was observed, with a formal potential of -115 mV vs. AgAgCl, KClsat at pH 7.0. This value agreed well with that previously reported for redox transformation of the heme domain of SOx. However, no bioelectrocatalysis of sulphite oxidation was observed in phosphate buffer solutions. This fact evidently correlated with known inhibition of intramolecular ET in SOx by the presence of bivalent inorganic anions. After changing to a Tris buffer solution, spectra variations and cyclic voltammetry data designated direct ET-based bioelectrocatalysis of sulphite oxidation, upon addition of sulphite. Thus, the bioelectrocatalytic 2e(-) oxidation of sulphite catalysed by SOx due to direct ET exchange with the electrode was attained at aldrithiol-modified gold electrodes and shown to depend essentially on the nature of the buffer solution. (C) 2004 Elsevier B.V. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Bioelectrocatalysis, Spectroelectrochemistry, Direct electron transfer, Sulphite oxidase
in
Bioelectrochemistry
volume
63
issue
1-2
pages
49 - 53
publisher
Elsevier
external identifiers
  • pmid:15110247
  • wos:000221786900010
  • scopus:2042421498
ISSN
1878-562X
DOI
10.1016/j.bioelechem.2003.09.013
language
English
LU publication?
yes
id
f9913763-4ebf-48f7-ac98-1d8921b5b14e (old id 138516)
date added to LUP
2007-06-26 16:03:17
date last changed
2017-09-03 03:56:27
@article{f9913763-4ebf-48f7-ac98-1d8921b5b14e,
  abstract     = {Electron transfer (ET) in sulphite oxidase (SOx), a heme- and molybdopterin cofactor-containing enzyme, was studied spectroelectrochemically using capillary gold electrode modified with aldrithiol. Direct electron exchange between SOx and the surface of modified gold was observed, with a formal potential of -115 mV vs. AgAgCl, KClsat at pH 7.0. This value agreed well with that previously reported for redox transformation of the heme domain of SOx. However, no bioelectrocatalysis of sulphite oxidation was observed in phosphate buffer solutions. This fact evidently correlated with known inhibition of intramolecular ET in SOx by the presence of bivalent inorganic anions. After changing to a Tris buffer solution, spectra variations and cyclic voltammetry data designated direct ET-based bioelectrocatalysis of sulphite oxidation, upon addition of sulphite. Thus, the bioelectrocatalytic 2e(-) oxidation of sulphite catalysed by SOx due to direct ET exchange with the electrode was attained at aldrithiol-modified gold electrodes and shown to depend essentially on the nature of the buffer solution. (C) 2004 Elsevier B.V. All rights reserved.},
  author       = {Ferapontova, Elena and Christenson, Andreas and Hellmark, Anja and Ruzgas, Tautgirdas},
  issn         = {1878-562X},
  keyword      = {Bioelectrocatalysis,Spectroelectrochemistry,Direct electron transfer,Sulphite oxidase},
  language     = {eng},
  number       = {1-2},
  pages        = {49--53},
  publisher    = {Elsevier},
  series       = {Bioelectrochemistry},
  title        = {Spectroelectrochemical study of heme- and molybdopterin cofactor-containing chicken liver sulphite oxidase},
  url          = {http://dx.doi.org/10.1016/j.bioelechem.2003.09.013},
  volume       = {63},
  year         = {2004},
}