Direct electrochemistry of heme multicofactor-containing enzymes on alkanethiol-modified gold electrodes
(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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https://lup.lub.lu.se/record/151060
- author
- Ferapontova, Elena LU and Gorton, Lo LU
- organization
- publishing date
- 2005
- 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
- pmid:15833703
- ISSN
- 1878-562X
- DOI
- 10.1016/j.bioelechem.2004.04.004
- 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
- e9396e79-b36b-46fd-960a-7a0d99760bf4 (old id 151060)
- date added to LUP
- 2016-04-01 12:22:47
- date last changed
- 2022-01-27 02:54:18
@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}}, keywords = {{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}}, doi = {{10.1016/j.bioelechem.2004.04.004}}, volume = {{66}}, year = {{2005}}, }