Electron transfer reaction of glucose oxidase hybrids modified with phenothiazine via poly(ethylene oxide) spacer on acidic amino acid residues

Sayuri Aoki; Kunikazu Ishii; Takeshi Ueki; Kazumichi Ban; Shin ichiro Imabayashi; Masayoshi Watanabe

doi:10.1246/cl.2002.256

Electron transfer reaction of glucose oxidase hybrids modified with phenothiazine via poly(ethylene oxide) spacer on acidic amino acid residues

Sayuri Aoki, Kunikazu Ishii, Takeshi Ueki, Kazumichi Ban, Shin ichiro Imabayashi, Masayoshi Watanabe

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

GOx hybrids [GOx-(PT-PEO-NH₂)] are prepared by covalently bonding phenothiazine(PT)-labeled poly(ethylene oxide) (PEO) oligomers having an amino end group, PT-PEO-NH₂, to acidic amino acid residues on the enzyme surface. The rate constant for the mediated FADH/FADH₂ oxidation calculated from the catalytic current under substrate-saturated conditions ranges from 1.7 to 388 s^-1, and the largest value is obtained for GOx hybrids with PT-PEO of molecular weight 3000. Surprisingly effective electron transfer from FADH/FADH₂ to PT⁺ is achieved in the GOx-(PT-PEO-NH₂) hybrids due to the PT modification to aspartic or glutamic acid residues, many of which are located close to the FAD center.

Original language	English
Pages (from-to)	256-257
Number of pages	2
Journal	Chemistry Letters
Issue number	2
DOIs	https://doi.org/10.1246/cl.2002.256
Publication status	Published - 2002 Feb 5
Externally published	Yes

ASJC Scopus subject areas

Chemistry(all)

Access to Document

10.1246/cl.2002.256

Cite this

@article{4759349e513e467fa2b498332d02707c,

title = "Electron transfer reaction of glucose oxidase hybrids modified with phenothiazine via poly(ethylene oxide) spacer on acidic amino acid residues",

abstract = "GOx hybrids [GOx-(PT-PEO-NH2)] are prepared by covalently bonding phenothiazine(PT)-labeled poly(ethylene oxide) (PEO) oligomers having an amino end group, PT-PEO-NH2, to acidic amino acid residues on the enzyme surface. The rate constant for the mediated FADH/FADH2 oxidation calculated from the catalytic current under substrate-saturated conditions ranges from 1.7 to 388 s-1, and the largest value is obtained for GOx hybrids with PT-PEO of molecular weight 3000. Surprisingly effective electron transfer from FADH/FADH2 to PT+ is achieved in the GOx-(PT-PEO-NH2) hybrids due to the PT modification to aspartic or glutamic acid residues, many of which are located close to the FAD center.",

author = "Sayuri Aoki and Kunikazu Ishii and Takeshi Ueki and Kazumichi Ban and Imabayashi, {Shin ichiro} and Masayoshi Watanabe",

year = "2002",

month = feb,

day = "5",

doi = "10.1246/cl.2002.256",

language = "English",

pages = "256--257",

journal = "Chemistry Letters",

issn = "0366-7022",

publisher = "Chemical Society of Japan",

number = "2",

}

TY - JOUR

T1 - Electron transfer reaction of glucose oxidase hybrids modified with phenothiazine via poly(ethylene oxide) spacer on acidic amino acid residues

AU - Aoki, Sayuri

AU - Ishii, Kunikazu

AU - Ueki, Takeshi

AU - Ban, Kazumichi

AU - Imabayashi, Shin ichiro

AU - Watanabe, Masayoshi

PY - 2002/2/5

Y1 - 2002/2/5

N2 - GOx hybrids [GOx-(PT-PEO-NH2)] are prepared by covalently bonding phenothiazine(PT)-labeled poly(ethylene oxide) (PEO) oligomers having an amino end group, PT-PEO-NH2, to acidic amino acid residues on the enzyme surface. The rate constant for the mediated FADH/FADH2 oxidation calculated from the catalytic current under substrate-saturated conditions ranges from 1.7 to 388 s-1, and the largest value is obtained for GOx hybrids with PT-PEO of molecular weight 3000. Surprisingly effective electron transfer from FADH/FADH2 to PT+ is achieved in the GOx-(PT-PEO-NH2) hybrids due to the PT modification to aspartic or glutamic acid residues, many of which are located close to the FAD center.

AB - GOx hybrids [GOx-(PT-PEO-NH2)] are prepared by covalently bonding phenothiazine(PT)-labeled poly(ethylene oxide) (PEO) oligomers having an amino end group, PT-PEO-NH2, to acidic amino acid residues on the enzyme surface. The rate constant for the mediated FADH/FADH2 oxidation calculated from the catalytic current under substrate-saturated conditions ranges from 1.7 to 388 s-1, and the largest value is obtained for GOx hybrids with PT-PEO of molecular weight 3000. Surprisingly effective electron transfer from FADH/FADH2 to PT+ is achieved in the GOx-(PT-PEO-NH2) hybrids due to the PT modification to aspartic or glutamic acid residues, many of which are located close to the FAD center.

UR - http://www.scopus.com/inward/record.url?scp=0036003213&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036003213&partnerID=8YFLogxK

U2 - 10.1246/cl.2002.256

DO - 10.1246/cl.2002.256

M3 - Article

AN - SCOPUS:0036003213

SN - 0366-7022

SP - 256

EP - 257

JO - Chemistry Letters

JF - Chemistry Letters

IS - 2

ER -

Electron transfer reaction of glucose oxidase hybrids modified with phenothiazine via poly(ethylene oxide) spacer on acidic amino acid residues

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this