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Dimerization of recombinant horseradish peroxidase in a reversed micellar system
N L Klyachko1, Dulkis YuK, I G Gazaryan
1School of Chemistry, Lomonosov Moscow State University, Moscow, Russia.
Abstract:
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.