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Mediator-assisted laccase-catalyzed oxidation of 4-hydroxybiphenyl

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Abstract

The kinetics of oxidation of 4-hydroxybiphenyl (4-HBP) catalyzed by laccase from Polyporus pinsitus was studied in the presence of methyl syringate (MS), which acts as an electron-transfer mediator. Measurements were performed in 0.05 M acetate buffer, pH 5.5, in the presence of 4-HBP, MS, and laccase. It is shown that the oxidation rate of the lowly reactive substrate 4-HBP significantly increases during synergistic action of the highly reactive substrate MS. Bimolecular kinetic constants of interaction between the oxidized form of laccase and MS, the former and 4-HBP, and the oxidized form of MS and 4-HBP were calculated. A kinetic scheme of the synergistic substrate action is suggested; based on this scheme, the dependence of the initial rate on reagent concentration is derived. Analyzing experimental data, we obtained kinetic constants close to those obtained by modeling the processes.

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Abbreviations

4-HBP:

4-hydroxybiphenyl

MS:

methyl syringate

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Authors and Affiliations

  1. Institute of Biochemistry, Mokslininku 12, Vilnius, LT-08662, Lithuania

    I. Bratkovskaya & J. Kulys

  2. Department of Chemistry and Bioengineering, Vilnius Gediminas Technical University, Sauletekio Av. 11, Vilnius, LT-10223, Lithuania

    R. Ivanec & J. Kulys

Authors
  1. I. Bratkovskaya
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  2. R. Ivanec
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  3. J. Kulys
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Corresponding author

Correspondence to I. Bratkovskaya.

Additional information

Original Russian Text © I. Bratkovskaya, R. Ivanec, J. Kulys, 2006, published in Biokhimiya, 2006, Vol. 71, No. 5, pp. 681–686.

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Bratkovskaya, I., Ivanec, R. & Kulys, J. Mediator-assisted laccase-catalyzed oxidation of 4-hydroxybiphenyl. Biochemistry (Moscow) 71, 550–554 (2006). https://doi.org/10.1134/S0006297906050130

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  • DOI: https://doi.org/10.1134/S0006297906050130

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