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 journalArticle

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 languageEnglish
Pages (from-to)256-257
Number of pages2
JournalChemistry Letters
Issue number2
DOIs
Publication statusPublished - 2002 Feb 5
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)

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