Biochemistry (Moscow)

, Volume 76, Issue 13, pp 1391–1401

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

Review

DOI: 10.1134/S0006297911130037

Cite this article as:
Zakharova, G.S., Uporov, I.V. & Tishkov, V.I. Biochemistry Moscow (2011) 76: 1391. doi:10.1134/S0006297911130037

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 peroxidaseHRPhemechemical modificationcatalytic propertiesstabilitycomputer modeling

Abbreviations

ABTS

2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate)

BFR

bifunctional reagent

EH

ethylhydrazine

HRP

horseradish peroxidase isozyme C

MFR

monofunctional reagent

MH

methylhydrazine

n-HRP

native HRP

PEH

phenylethylhydrazine

PHZ

phenylhydrazine

rs-HRP

reconstructed HRP

SASA

solvent accessible surface area

SHD

synthetic heme derivative

Supplementary material

10541_2011_9521_MOESM1_ESM.pdf (274 kb)
Supplementary material, approximately 273 KB.

Copyright information

© Pleiades Publishing, Ltd. 2011

Authors and Affiliations

  • G. S. Zakharova
    • 1
    • 2
  • I. V. Uporov
    • 3
  • V. I. Tishkov
    • 1
    • 2
    • 3
  1. 1.Bach Institute of BiochemistryRussian Academy of SciencesMoscowRussia
  2. 2.Innovations and High Technologies MSU Ltd.MoscowRussia
  3. 3.Chemical FacultyLomonosov Moscow State UniversityMoscowRussia