Structural stabilization and functional improvement of horseradish peroxidase upon modification of accessible lysines: experiments and simulation.

ABSTRACT: Horseradish peroxidase (HRP) is an important heme enzyme with enormous medical diagnostic, biosensing, and biotechnological applications. Thus, any improvement in the applicability and stability of the enzyme is potentially interesting. We previously reported that covalent attachment of an electron relay (anthraquinone 2-carboxylic acid) to the surface-exposed Lys residues successfully improves electron transfer properties of HRP. Here we investigated structural and functional consequences of this modification, which alters three accessible charged lysines (Lys-174, Lys-232, and Lys-241) to the hydrophobic anthraquinolysine residues. Thermal denaturation and thermoinactivation studies demonstrated that this kind of modification enhances the conformational and operational stability of HRP.

SUBMITTER: Mogharrab N 

PROVIDER: S-EPMC1783884 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature