Biocatalytic oxidation of phenolic compounds by bovine methemoglobin in the presence of H2O2: quantitative structure-activity relationships Articles uri icon

publication date

  • November 2012

start page

  • 207

end page

  • 215


  • 241-242

International Standard Serial Number (ISSN)

  • 0304-3894

Electronic International Standard Serial Number (EISSN)

  • 1873-3336


  • In the present work, 13 p-substituted phenols with different functional groups have been systematically evaluated as metHb substrates by means of HPLC analysis. Non-hyperbolic kinetics were observed and Hill coefficients in the 0.37&-1.00 range were obtained. The catalytic constants and the Hill coefficients were found to be quantitatively correlated with two independent variables: the energy level of the highest-occupied molecular orbital (EHOMO), which describes the intrinsic redox activity of the substrates and the pKa-values, which are related to substrate ionization. Oxygen evolution in the presence of each phenol derivative was also measured, and good correlation between peroxidase-like and catalase-like activities of the protein was observed. It is also shown that bovine metHb, although less active than other peroxidases, may represent a good alternative from an economical point of view for phenol removal processes. The equations here obtained may serve as a basis to further explore the potential use of metHb-mediated reactions in the treatment of phenols in wastewaters and to predict which phenol will be removed most efficiently under this treatment with satisfactory reliability.


  • Materials science and engineering


  • hemoglobin; qsar; phenolic compounds; peroxidase-like activity; catalase-like activity