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.
|Number of pages||2|
|Publication status||Published - 2002 Feb 5|
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