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https://doi.org/10.5562/cca2685

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

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

Puni tekst: engleski, pdf (4 MB) str. 297-306 preuzimanja: 433* citiraj
APA 6th Edition
Brkić, H. (2015). Insight of the Iron Binding and Transport in Dke1 - A Molecular Dynamics Study. Croatica Chemica Acta, 88 (3), 297-306. https://doi.org/10.5562/cca2685
MLA 8th Edition
Brkić, Hrvoje. "Insight of the Iron Binding and Transport in Dke1 - A Molecular Dynamics Study." Croatica Chemica Acta, vol. 88, br. 3, 2015, str. 297-306. https://doi.org/10.5562/cca2685. Citirano 18.01.2020.
Chicago 17th Edition
Brkić, Hrvoje. "Insight of the Iron Binding and Transport in Dke1 - A Molecular Dynamics Study." Croatica Chemica Acta 88, br. 3 (2015): 297-306. https://doi.org/10.5562/cca2685
Harvard
Brkić, H. (2015). 'Insight of the Iron Binding and Transport in Dke1 - A Molecular Dynamics Study', Croatica Chemica Acta, 88(3), str. 297-306. https://doi.org/10.5562/cca2685
Vancouver
Brkić H. Insight of the Iron Binding and Transport in Dke1 - A Molecular Dynamics Study. Croatica Chemica Acta [Internet]. 2015 [pristupljeno 18.01.2020.];88(3):297-306. https://doi.org/10.5562/cca2685
IEEE
H. Brkić, "Insight of the Iron Binding and Transport in Dke1 - A Molecular Dynamics Study", Croatica Chemica Acta, vol.88, br. 3, str. 297-306, 2015. [Online]. https://doi.org/10.5562/cca2685

Sažetak
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.

Ključne riječi
metaloenzyme; non-heme; iron; molecular dynamics

Hrčak ID: 150535

URI
https://hrcak.srce.hr/150535

Posjeta: 623 *