Electrical communication between glucose oxidase and electrodes mediated by phenothiazine-labeled poly(ethylene oxide) bonded to lysine residues on the enzyme surface

Kazumichi Ban, Takeshi Ueki, Yoshinori Tamada, Takahiro Saito, Shinichiro Imabayashi, Masayoshi Watanabe

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

A series of glucose oxidase (GOx) hybrids (GOx-phenothiazine-labeled poly(ethylene oxide) (PT-PEO)) capable of direct electrical communication with electrodes is synthesized by covalently modifying PT-PEO to lysine residues on the enzyme surface. The length of the PEO chain and the number of PT groups are systematically altered. After the PT-PEO modification, all the hybrids maintain more than 50% of enzyme activity relative to that of native GOx, although loss of the activity becomes greater with increasing PEO chain length. The catalytic current, icat, is observed at a potential more positive than 0.55 V after the addition of glucose, due to the intramolecular electron transfer (ET) from reduced forms of flavin adenine dinucletide (FADH2/FADH) to PT+ that are electrogenerated at the electrode. The icat value increases with the number of PT groups, indicating that most of the modified PT groups act as mediators. The magnitude of the icat increase depends on the PEO chain length and reveals a maximum for PT-PEO with the molecular weight of 3000. In contrast, the icat is almost constant for GOx-2-(10-phenothiazyl)propionic acid (PT-PA) hybrids with more than two PT groups synthesized by covalently modifying PT-PA to surface lysines, indicating that only a few key PT groups function as mediators. The maximum rate constant (130 s-1) for the ET from FADH2/FADH to PT+ is obtained for the GOx hybrid modified with five PT-PEO groups with the molecular weight of 3000.

Original languageEnglish
Pages (from-to)910-917
Number of pages8
JournalAnalytical Chemistry
Volume75
Issue number4
DOIs
Publication statusPublished - 2003 Feb 15
Externally publishedYes

Fingerprint

Glucose Oxidase
Polyethylene oxides
Lysine
Electrodes
Communication
Enzymes
Chain length
Molecular weight
phenothiazine
Electrons
Enzyme activity
Adenine
Rate constants
Glucose

ASJC Scopus subject areas

  • Analytical Chemistry

Cite this

Electrical communication between glucose oxidase and electrodes mediated by phenothiazine-labeled poly(ethylene oxide) bonded to lysine residues on the enzyme surface. / Ban, Kazumichi; Ueki, Takeshi; Tamada, Yoshinori; Saito, Takahiro; Imabayashi, Shinichiro; Watanabe, Masayoshi.

In: Analytical Chemistry, Vol. 75, No. 4, 15.02.2003, p. 910-917.

Research output: Contribution to journalArticle

@article{a1cc4ddc57284587a16a0e9b8265ea8e,
title = "Electrical communication between glucose oxidase and electrodes mediated by phenothiazine-labeled poly(ethylene oxide) bonded to lysine residues on the enzyme surface",
abstract = "A series of glucose oxidase (GOx) hybrids (GOx-phenothiazine-labeled poly(ethylene oxide) (PT-PEO)) capable of direct electrical communication with electrodes is synthesized by covalently modifying PT-PEO to lysine residues on the enzyme surface. The length of the PEO chain and the number of PT groups are systematically altered. After the PT-PEO modification, all the hybrids maintain more than 50{\%} of enzyme activity relative to that of native GOx, although loss of the activity becomes greater with increasing PEO chain length. The catalytic current, icat, is observed at a potential more positive than 0.55 V after the addition of glucose, due to the intramolecular electron transfer (ET) from reduced forms of flavin adenine dinucletide (FADH2/FADH) to PT+ that are electrogenerated at the electrode. The icat value increases with the number of PT groups, indicating that most of the modified PT groups act as mediators. The magnitude of the icat increase depends on the PEO chain length and reveals a maximum for PT-PEO with the molecular weight of 3000. In contrast, the icat is almost constant for GOx-2-(10-phenothiazyl)propionic acid (PT-PA) hybrids with more than two PT groups synthesized by covalently modifying PT-PA to surface lysines, indicating that only a few key PT groups function as mediators. The maximum rate constant (130 s-1) for the ET from FADH2/FADH to PT+ is obtained for the GOx hybrid modified with five PT-PEO groups with the molecular weight of 3000.",
author = "Kazumichi Ban and Takeshi Ueki and Yoshinori Tamada and Takahiro Saito and Shinichiro Imabayashi and Masayoshi Watanabe",
year = "2003",
month = "2",
day = "15",
doi = "10.1021/ac025872t",
language = "English",
volume = "75",
pages = "910--917",
journal = "Analytical Chemistry",
issn = "0003-2700",
publisher = "American Chemical Society",
number = "4",

}

TY - JOUR

T1 - Electrical communication between glucose oxidase and electrodes mediated by phenothiazine-labeled poly(ethylene oxide) bonded to lysine residues on the enzyme surface

AU - Ban, Kazumichi

AU - Ueki, Takeshi

AU - Tamada, Yoshinori

AU - Saito, Takahiro

AU - Imabayashi, Shinichiro

AU - Watanabe, Masayoshi

PY - 2003/2/15

Y1 - 2003/2/15

N2 - A series of glucose oxidase (GOx) hybrids (GOx-phenothiazine-labeled poly(ethylene oxide) (PT-PEO)) capable of direct electrical communication with electrodes is synthesized by covalently modifying PT-PEO to lysine residues on the enzyme surface. The length of the PEO chain and the number of PT groups are systematically altered. After the PT-PEO modification, all the hybrids maintain more than 50% of enzyme activity relative to that of native GOx, although loss of the activity becomes greater with increasing PEO chain length. The catalytic current, icat, is observed at a potential more positive than 0.55 V after the addition of glucose, due to the intramolecular electron transfer (ET) from reduced forms of flavin adenine dinucletide (FADH2/FADH) to PT+ that are electrogenerated at the electrode. The icat value increases with the number of PT groups, indicating that most of the modified PT groups act as mediators. The magnitude of the icat increase depends on the PEO chain length and reveals a maximum for PT-PEO with the molecular weight of 3000. In contrast, the icat is almost constant for GOx-2-(10-phenothiazyl)propionic acid (PT-PA) hybrids with more than two PT groups synthesized by covalently modifying PT-PA to surface lysines, indicating that only a few key PT groups function as mediators. The maximum rate constant (130 s-1) for the ET from FADH2/FADH to PT+ is obtained for the GOx hybrid modified with five PT-PEO groups with the molecular weight of 3000.

AB - A series of glucose oxidase (GOx) hybrids (GOx-phenothiazine-labeled poly(ethylene oxide) (PT-PEO)) capable of direct electrical communication with electrodes is synthesized by covalently modifying PT-PEO to lysine residues on the enzyme surface. The length of the PEO chain and the number of PT groups are systematically altered. After the PT-PEO modification, all the hybrids maintain more than 50% of enzyme activity relative to that of native GOx, although loss of the activity becomes greater with increasing PEO chain length. The catalytic current, icat, is observed at a potential more positive than 0.55 V after the addition of glucose, due to the intramolecular electron transfer (ET) from reduced forms of flavin adenine dinucletide (FADH2/FADH) to PT+ that are electrogenerated at the electrode. The icat value increases with the number of PT groups, indicating that most of the modified PT groups act as mediators. The magnitude of the icat increase depends on the PEO chain length and reveals a maximum for PT-PEO with the molecular weight of 3000. In contrast, the icat is almost constant for GOx-2-(10-phenothiazyl)propionic acid (PT-PA) hybrids with more than two PT groups synthesized by covalently modifying PT-PA to surface lysines, indicating that only a few key PT groups function as mediators. The maximum rate constant (130 s-1) for the ET from FADH2/FADH to PT+ is obtained for the GOx hybrid modified with five PT-PEO groups with the molecular weight of 3000.

UR - http://www.scopus.com/inward/record.url?scp=0037442612&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037442612&partnerID=8YFLogxK

U2 - 10.1021/ac025872t

DO - 10.1021/ac025872t

M3 - Article

VL - 75

SP - 910

EP - 917

JO - Analytical Chemistry

JF - Analytical Chemistry

SN - 0003-2700

IS - 4

ER -