Publications by authors named "Jacob S Baus"
Article Synopsis
- Acetylacetone dioxygenase (Dke1) is a bacterial enzyme that breaks down β-dicarbonyl compounds using a nonheme iron center that facilitates oxygen binding and reactivity.
- Recent research involved creating ferrous β-diketonato complexes that simulate the enzyme-substrate interaction of Dke1, allowing scientists to investigate their reaction with oxygen and nitric oxide.
- Findings showed that certain complexes can form a stable green chromophore when exposed to O(2), indicating the development of a diiron(III) species, and that modifications in the ligand structure affected reactivity and enzyme mimicry.
A series of high-spin iron(II) β-diketonato complexes have been prepared and characterized with the intent of modeling the substrate-bound form of the enzyme acetylacetone dioxygenase (Dke1). The Dke1 active site features an Fe(II) center coordinated by three histidine residues in a facial geometry--a departure from the standard 2-histidine-1-carboxylate (2H1C) facial triad dominant among nonheme monoiron enzymes. The deprotonated β-diketone substrate binds to the Fe center in a bidentate fashion.
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