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Tryptophan repressor-binding proteins from Escherichia coli and Archaeoglobus fulgidus as new catalysts for 1,4-dihydronicotinamide adenine dinucleotide-dependent amperometric biosensors and biofuel cells.

Zafar, MNadeem LU ; Tasca, Federico LU ; Gorton, Lo LU ; Patridge, Eric V; Ferry, James G and Nöll, Gilbert LU (2009) In Analytical Chemistry 81(10). p.4082-4088
Abstract
The tryptophan (W) repressor-binding proteins (WrbA) from Escherichia coli (EcWrbA) and Archaeoglobus fulgidus (AfWrbA) were investigated for possible use in 1,4-dihydronicotinamide adenine dinucleotide (NADH) dependent amperometric biosensors and biofuel cells. EcWrbA and AfWrbA are oligomeric flavoproteins binding one flavin mononucleotide (FMN) per monomer and belonging to a new family of NAD(P)H:quinone oxidoreductases (NQOs). The enzymes were covalently linked to a low potential Os redox polymer onto graphite in the presence of single-walled carbon nanotube (SWCNT) preparations of varying average lengths. The performance of the enzyme modified electrodes for NADH oxidation was strongly depending on the average length of the applied... (More)
The tryptophan (W) repressor-binding proteins (WrbA) from Escherichia coli (EcWrbA) and Archaeoglobus fulgidus (AfWrbA) were investigated for possible use in 1,4-dihydronicotinamide adenine dinucleotide (NADH) dependent amperometric biosensors and biofuel cells. EcWrbA and AfWrbA are oligomeric flavoproteins binding one flavin mononucleotide (FMN) per monomer and belonging to a new family of NAD(P)H:quinone oxidoreductases (NQOs). The enzymes were covalently linked to a low potential Os redox polymer onto graphite in the presence of single-walled carbon nanotube (SWCNT) preparations of varying average lengths. The performance of the enzyme modified electrodes for NADH oxidation was strongly depending on the average length of the applied SWCNTs. By blending the Os redox polymer with SWCNTs, the electrocatalytic current could be increased up to a factor of 5. Results obtained for AfWrbA modified electrodes were better than those for EcWrbA. For NADH detection, a linear range between 5 microM and 1 mM, a lower limit of detection of 3 microM, and a sensitivity of 56.5 nA microM(-1) cm(-2) could be reached. Additionally spectroelectrochemical measurements were carried out in order to determine the midpoint potentials of the enzymes (-115 mV vs NHE for EcWrbA and -100 mV vs NHE for AfWrbA pH 7.0). Furthermore, an AfWrbA modified electrode was used as an anode in combination with a Pt black cathode as a biofuel cell prototype. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Analytical Chemistry
volume
81
issue
10
pages
4082 - 4088
publisher
The American Chemical Society
external identifiers
  • wos:000266095100050
  • pmid:19438267
  • scopus:66149090360
ISSN
1520-6882
DOI
10.1021/ac900365n
language
English
LU publication?
yes
id
da95f364-11aa-43f7-9b0f-31f0633123fc (old id 1412343)
date added to LUP
2009-06-11 09:39:42
date last changed
2017-01-01 05:11:56
@article{da95f364-11aa-43f7-9b0f-31f0633123fc,
  abstract     = {The tryptophan (W) repressor-binding proteins (WrbA) from Escherichia coli (EcWrbA) and Archaeoglobus fulgidus (AfWrbA) were investigated for possible use in 1,4-dihydronicotinamide adenine dinucleotide (NADH) dependent amperometric biosensors and biofuel cells. EcWrbA and AfWrbA are oligomeric flavoproteins binding one flavin mononucleotide (FMN) per monomer and belonging to a new family of NAD(P)H:quinone oxidoreductases (NQOs). The enzymes were covalently linked to a low potential Os redox polymer onto graphite in the presence of single-walled carbon nanotube (SWCNT) preparations of varying average lengths. The performance of the enzyme modified electrodes for NADH oxidation was strongly depending on the average length of the applied SWCNTs. By blending the Os redox polymer with SWCNTs, the electrocatalytic current could be increased up to a factor of 5. Results obtained for AfWrbA modified electrodes were better than those for EcWrbA. For NADH detection, a linear range between 5 microM and 1 mM, a lower limit of detection of 3 microM, and a sensitivity of 56.5 nA microM(-1) cm(-2) could be reached. Additionally spectroelectrochemical measurements were carried out in order to determine the midpoint potentials of the enzymes (-115 mV vs NHE for EcWrbA and -100 mV vs NHE for AfWrbA pH 7.0). Furthermore, an AfWrbA modified electrode was used as an anode in combination with a Pt black cathode as a biofuel cell prototype.},
  author       = {Zafar, MNadeem and Tasca, Federico and Gorton, Lo and Patridge, Eric V and Ferry, James G and Nöll, Gilbert},
  issn         = {1520-6882},
  language     = {eng},
  number       = {10},
  pages        = {4082--4088},
  publisher    = {The American Chemical Society},
  series       = {Analytical Chemistry},
  title        = {Tryptophan repressor-binding proteins from Escherichia coli and Archaeoglobus fulgidus as new catalysts for 1,4-dihydronicotinamide adenine dinucleotide-dependent amperometric biosensors and biofuel cells.},
  url          = {http://dx.doi.org/10.1021/ac900365n},
  volume       = {81},
  year         = {2009},
}