Original scientific paper

https://doi.org/10.5562/cca2685

Insight of the Iron Binding and Transport in Dke1 - A Molecular Dynamics Study

Hrvoje Brkić orcid.org/0000-0001-6692-6875 ; Faculty of Medicine, J. Huttlera 4, HR-31000 Osijek, Croatia

Abstract

Acetylacetone dioxygenase from Acinetobacter johnsonii (Dke1) is a non-heme Fe2+ dependent enzyme which catalyzes the oxidative degradation of β-dicarbonyl compounds. It is a homotetramer with four active sites, each containing single metal ion. Since the active site is buried, knowledge on transport of the metal ion and reactants (products) is essential for understanding the enzyme mechanism. The goal of this study was to assess the influence of several point mutations on the enzyme activity. The point mutations of hydrophilic amino acid residues (Tyr70, Arg80 and Glu98) that were shown to be important for metal binding and reactants stabilization were of the particular interest. Computational study enabled us to determine the preferred metal ion binding sites as well, as the pathways it utilizes to enter the enzyme active site. Besides, influence of the point mutations on the hydrogen bond network within enzyme was determined.

Keywords

metaloenzyme; non-heme; iron; molecular dynamics

Hrčak ID:

150535

URI

https://hrcak.srce.hr/150535

Publication date:

30.12.2015.

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