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Direct electrochemistry of heme multicofactor-containing enzymes on alkanethiol-modified gold electrodes

Ferapontova, Elena LU and Gorton, Lo LU (2005) In Bioelectrochemistry 66(1-2). p.55-63
Abstract
Direct electrochemistry of heme multicofactor-containing enzymes, e.g., microbial theophylline oxidase (ThOx) and D-fructose dehydrogenase (FDH) from Gluconobacter industrius was studied on alkanethiol-modified gold electrodes and was compared with that of some previously studied complex heme enzymes, specifically, cellobiose dehydrogenase (CDH) and sulphite oxidase (SOx). The formal redox potentials for enzymes in direct electronic communication varied for ThOx from -112 to -101 mV (vs. Ag vertical bar AgCl), at pH 7.0, and for FDH from - 158 to -89 mV, at pH 5.0 and pH 4.0, respectively, on differently charged alkanethiol layers. Direct and mediated by cytochrome c electrochemistry of FDH correlated with the existence of two active... (More)
Direct electrochemistry of heme multicofactor-containing enzymes, e.g., microbial theophylline oxidase (ThOx) and D-fructose dehydrogenase (FDH) from Gluconobacter industrius was studied on alkanethiol-modified gold electrodes and was compared with that of some previously studied complex heme enzymes, specifically, cellobiose dehydrogenase (CDH) and sulphite oxidase (SOx). The formal redox potentials for enzymes in direct electronic communication varied for ThOx from -112 to -101 mV (vs. Ag vertical bar AgCl), at pH 7.0, and for FDH from - 158 to -89 mV, at pH 5.0 and pH 4.0, respectively, on differently charged alkanethiol layers. Direct and mediated by cytochrome c electrochemistry of FDH correlated with the existence of two active centres in the protein structure, i.e., the heme and the pyrroloquinoline quinone (PQQ) prosthetic groups. The effect of the alkanethiols of different polarity and charge on the surface properties of the g-old electrodes necessary for adsorption and orientation of ThOx, FDH, CDH and SOx, favourable for the efficient electrode-enzyme electron transfer reaction, is discussed. (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
Alkanethiol self-assembled monolayers, Direct electron transfer, Heme, d-fructose dehydrogenase, Theophylline oxidase
in
Bioelectrochemistry
volume
66
issue
1-2
pages
55 - 63
publisher
Elsevier
external identifiers
  • pmid:15833703
  • wos:000229199900009
  • scopus:17144411517
ISSN
1878-562X
DOI
10.1016/j.bioelechem.2004.04.004
language
English
LU publication?
yes
id
e9396e79-b36b-46fd-960a-7a0d99760bf4 (old id 151060)
date added to LUP
2007-06-26 16:07:31
date last changed
2017-05-28 03:45:48
@article{e9396e79-b36b-46fd-960a-7a0d99760bf4,
  abstract     = {Direct electrochemistry of heme multicofactor-containing enzymes, e.g., microbial theophylline oxidase (ThOx) and D-fructose dehydrogenase (FDH) from Gluconobacter industrius was studied on alkanethiol-modified gold electrodes and was compared with that of some previously studied complex heme enzymes, specifically, cellobiose dehydrogenase (CDH) and sulphite oxidase (SOx). The formal redox potentials for enzymes in direct electronic communication varied for ThOx from -112 to -101 mV (vs. Ag vertical bar AgCl), at pH 7.0, and for FDH from - 158 to -89 mV, at pH 5.0 and pH 4.0, respectively, on differently charged alkanethiol layers. Direct and mediated by cytochrome c electrochemistry of FDH correlated with the existence of two active centres in the protein structure, i.e., the heme and the pyrroloquinoline quinone (PQQ) prosthetic groups. The effect of the alkanethiols of different polarity and charge on the surface properties of the g-old electrodes necessary for adsorption and orientation of ThOx, FDH, CDH and SOx, favourable for the efficient electrode-enzyme electron transfer reaction, is discussed. (c) 2004 Elsevier B.V. All rights reserved.},
  author       = {Ferapontova, Elena and Gorton, Lo},
  issn         = {1878-562X},
  keyword      = {Alkanethiol self-assembled monolayers,Direct electron transfer,Heme,d-fructose dehydrogenase,Theophylline oxidase},
  language     = {eng},
  number       = {1-2},
  pages        = {55--63},
  publisher    = {Elsevier},
  series       = {Bioelectrochemistry},
  title        = {Direct electrochemistry of heme multicofactor-containing enzymes on alkanethiol-modified gold electrodes},
  url          = {http://dx.doi.org/10.1016/j.bioelechem.2004.04.004},
  volume       = {66},
  year         = {2005},
}