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, Shin Ichiro Imabayashi, Masayoshi Watanabe

研究成果: Article査読

5 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)9177-9183
ページ数7
ジャーナルLangmuir
20
21
DOI
出版ステータスPublished - 2004 10 12
外部発表はい

ASJC Scopus subject areas

  • 材料科学(全般)
  • 凝縮系物理学
  • 表面および界面
  • 分光学
  • 電気化学

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