Review

Biochemistry (Moscow)

, Volume 76, Issue 13, pp 1391-1401

Horseradish peroxidase: Modulation of properties by chemical modification of protein and heme

  • G. S. ZakharovaAffiliated withBach Institute of Biochemistry, Russian Academy of SciencesInnovations and High Technologies MSU Ltd.
  • , I. V. UporovAffiliated withChemical Faculty, Lomonosov Moscow State University
  • , V. I. TishkovAffiliated withBach Institute of Biochemistry, Russian Academy of SciencesInnovations and High Technologies MSU Ltd.Chemical Faculty, Lomonosov Moscow State University Email author 

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Abstract

Horseradish peroxidase (HRP) is one of the most studied enzymes of the plant peroxidase superfamily. HRP is also widely used in different bioanalytical applications and diagnostic kits. The methods of genetic engineering and protein design are now widely used to study the catalytic mechanism and to improve properties of the enzyme. Here we review the results of another approach to HRP modification—through the chemical modification of amino acids or prosthetic group of the enzyme. Computer models of HRPs with modified hemes are in good agreement with the experimental data.

Key words

horseradish peroxidase HRP heme chemical modification catalytic properties stability computer modeling