REVIEW: Horseradish Peroxidase: Modulation of Properties by Chemical Modification of Protein and Heme

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G. S. Zakharova^1,2, I. V. Uporov³, and V. I. Tishkov^1,2,3*

¹Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071 Moscow, Russia; E-mail: vitishkov@gmail.com

²Innovations and High Technologies MSU Ltd., 109559 Moscow, Russia

³Chemical Faculty, Lomonosov Moscow State University, 119992 Moscow, Russia

^* To whom correspondence should be addressed.

Received June 24, 2011; Revision received July 7, 2011

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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.

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KEY WORDS: horseradish peroxidase, HRP, heme, chemical modification, catalytic properties, stability, computer modeling

DOI: 10.1134/S0006297911130037

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