Dimerization of Recombinant Horseradish Peroxidase in a Reversed Micellar System

N. L. Klyachko,^1,2 Yu. K. Dulkis,¹ I. G. Gazaryan,¹ I. V. Ouporov,¹ and A. V. Levashov¹

¹School of Chemistry, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-0997.

²To whom correspondence should be addressed.

Submitted June 23, 1997; revision submitted July 10, 1997.

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Recombinant horseradish peroxidase reactivated from E. coli inclusion bodies was studied in a reversed micellar system of AOT in octane. The ability of the recombinant enzyme, in contrast to native horseradish peroxidase, to form a dimeric structure was found. The existence of the dimer was proved by results of sedimentation analysis. Dimer/monomer ratio in the enzyme-containing micelles and dimer catalytic activity were found to depend on the substrate used (pyrogallol, guaiacol, o-dianisidine, o-phenylenediamine). Computer modelling was used to describe possible structures of the dimeric recombinant horseradish peroxidase.

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KEY WORDS: recombinant horseradish peroxidase, catalysis, dimer structure, micellar enzymology, computer modelling.

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