Effect of a modification site on the electron-transfer reaction of glucose oxidase hybrids modified with phenothiazine via a poly(ethylene oxide) spacer

Takeshi Ueki, Sayuri Aoki, Kunikazu Ishii, Shinichiro Imabayashi, Masayoshi Watanabe

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Glucose oxidase [GOx-(PT-PEONH2)] hybrids are synthesized by attaching phenothiazine (PT) groups to aspartic and glutamic acid residues on the enzyme surface via poly(ethylene oxide) (PEO) spacers of different molecular weights. A fast oxidation of FADH2/FADH by PT+ with the aid of the local motion of a hydrophilic, long, flexible PEO spacer is achieved for the GOx-(PT-PEONH2) hybrids and yields greater electron-transfer (ET) rates than that for GOx-(PTNH2) hybrids, in which the PT groups are directly bonded to the GOx surface. The ET rate of GOx-(PT-PEONH2) hybrids depends on the molecular weight of PT-PEONH2, and the maximum is obtained at a molecular weight of 3000. The ET rates of GOx hybrids are compared in terms of the location of the PT modification and the length and structure of the spacer chain connection of the PT mediator to a surface amino acid residue. Greater ET rates are obtained for the modification at aspartic and glutamic acid residues than for the lysine modification when the PT groups are bonded directly or via a short PEO spacer chain. In contrast, no advantage of aspartic and glutamic acid residues over lysine residues in generating a fast oxidation of FADH2/FADH by PT+ is observed for GOx hybrids in which the PT groups are attached via longer PEO spacers. The long PEO spacer is able to compensate the disadvantage of lysine residues locating far from the FAD center in GOx hybrids whose mediation reactions are based on the so-called wipe mechanism.

Original languageEnglish
Pages (from-to)9177-9183
Number of pages7
JournalLangmuir
Volume20
Issue number21
DOIs
Publication statusPublished - 2004 Oct 12
Externally publishedYes

Fingerprint

phenothiazines
Glucose Oxidase
Glucose oxidase
oxidase
ethylene oxide
Polyethylene oxides
glucose
spacers
electron transfer
Electrons
Molecular weight
aspartic acid
glutamic acid
Acids
lysine
Lysine
Glutamic Acid
molecular weight
Oxidation
phenothiazine

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

Cite this

Effect of a modification site on the electron-transfer reaction of glucose oxidase hybrids modified with phenothiazine via a poly(ethylene oxide) spacer. / Ueki, Takeshi; Aoki, Sayuri; Ishii, Kunikazu; Imabayashi, Shinichiro; Watanabe, Masayoshi.

In: Langmuir, Vol. 20, No. 21, 12.10.2004, p. 9177-9183.

Research output: Contribution to journalArticle

@article{8ddfa997a1dd482aa068840b362ecac4,
title = "Effect of a modification site on the electron-transfer reaction of glucose oxidase hybrids modified with phenothiazine via a poly(ethylene oxide) spacer",
abstract = "Glucose oxidase [GOx-(PT-PEONH2)] hybrids are synthesized by attaching phenothiazine (PT) groups to aspartic and glutamic acid residues on the enzyme surface via poly(ethylene oxide) (PEO) spacers of different molecular weights. A fast oxidation of FADH2/FADH by PT+ with the aid of the local motion of a hydrophilic, long, flexible PEO spacer is achieved for the GOx-(PT-PEONH2) hybrids and yields greater electron-transfer (ET) rates than that for GOx-(PTNH2) hybrids, in which the PT groups are directly bonded to the GOx surface. The ET rate of GOx-(PT-PEONH2) hybrids depends on the molecular weight of PT-PEONH2, and the maximum is obtained at a molecular weight of 3000. The ET rates of GOx hybrids are compared in terms of the location of the PT modification and the length and structure of the spacer chain connection of the PT mediator to a surface amino acid residue. Greater ET rates are obtained for the modification at aspartic and glutamic acid residues than for the lysine modification when the PT groups are bonded directly or via a short PEO spacer chain. In contrast, no advantage of aspartic and glutamic acid residues over lysine residues in generating a fast oxidation of FADH2/FADH by PT+ is observed for GOx hybrids in which the PT groups are attached via longer PEO spacers. The long PEO spacer is able to compensate the disadvantage of lysine residues locating far from the FAD center in GOx hybrids whose mediation reactions are based on the so-called wipe mechanism.",
author = "Takeshi Ueki and Sayuri Aoki and Kunikazu Ishii and Shinichiro Imabayashi and Masayoshi Watanabe",
year = "2004",
month = "10",
day = "12",
doi = "10.1021/la0490689",
language = "English",
volume = "20",
pages = "9177--9183",
journal = "Langmuir",
issn = "0743-7463",
publisher = "American Chemical Society",
number = "21",

}

TY - JOUR

T1 - Effect of a modification site on the electron-transfer reaction of glucose oxidase hybrids modified with phenothiazine via a poly(ethylene oxide) spacer

AU - Ueki, Takeshi

AU - Aoki, Sayuri

AU - Ishii, Kunikazu

AU - Imabayashi, Shinichiro

AU - Watanabe, Masayoshi

PY - 2004/10/12

Y1 - 2004/10/12

N2 - Glucose oxidase [GOx-(PT-PEONH2)] hybrids are synthesized by attaching phenothiazine (PT) groups to aspartic and glutamic acid residues on the enzyme surface via poly(ethylene oxide) (PEO) spacers of different molecular weights. A fast oxidation of FADH2/FADH by PT+ with the aid of the local motion of a hydrophilic, long, flexible PEO spacer is achieved for the GOx-(PT-PEONH2) hybrids and yields greater electron-transfer (ET) rates than that for GOx-(PTNH2) hybrids, in which the PT groups are directly bonded to the GOx surface. The ET rate of GOx-(PT-PEONH2) hybrids depends on the molecular weight of PT-PEONH2, and the maximum is obtained at a molecular weight of 3000. The ET rates of GOx hybrids are compared in terms of the location of the PT modification and the length and structure of the spacer chain connection of the PT mediator to a surface amino acid residue. Greater ET rates are obtained for the modification at aspartic and glutamic acid residues than for the lysine modification when the PT groups are bonded directly or via a short PEO spacer chain. In contrast, no advantage of aspartic and glutamic acid residues over lysine residues in generating a fast oxidation of FADH2/FADH by PT+ is observed for GOx hybrids in which the PT groups are attached via longer PEO spacers. The long PEO spacer is able to compensate the disadvantage of lysine residues locating far from the FAD center in GOx hybrids whose mediation reactions are based on the so-called wipe mechanism.

AB - Glucose oxidase [GOx-(PT-PEONH2)] hybrids are synthesized by attaching phenothiazine (PT) groups to aspartic and glutamic acid residues on the enzyme surface via poly(ethylene oxide) (PEO) spacers of different molecular weights. A fast oxidation of FADH2/FADH by PT+ with the aid of the local motion of a hydrophilic, long, flexible PEO spacer is achieved for the GOx-(PT-PEONH2) hybrids and yields greater electron-transfer (ET) rates than that for GOx-(PTNH2) hybrids, in which the PT groups are directly bonded to the GOx surface. The ET rate of GOx-(PT-PEONH2) hybrids depends on the molecular weight of PT-PEONH2, and the maximum is obtained at a molecular weight of 3000. The ET rates of GOx hybrids are compared in terms of the location of the PT modification and the length and structure of the spacer chain connection of the PT mediator to a surface amino acid residue. Greater ET rates are obtained for the modification at aspartic and glutamic acid residues than for the lysine modification when the PT groups are bonded directly or via a short PEO spacer chain. In contrast, no advantage of aspartic and glutamic acid residues over lysine residues in generating a fast oxidation of FADH2/FADH by PT+ is observed for GOx hybrids in which the PT groups are attached via longer PEO spacers. The long PEO spacer is able to compensate the disadvantage of lysine residues locating far from the FAD center in GOx hybrids whose mediation reactions are based on the so-called wipe mechanism.

UR - http://www.scopus.com/inward/record.url?scp=6444231732&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=6444231732&partnerID=8YFLogxK

U2 - 10.1021/la0490689

DO - 10.1021/la0490689

M3 - Article

VL - 20

SP - 9177

EP - 9183

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 21

ER -