A family of structural and functional models for the active site of a unique dioxygenase: Acireductone dioxygenase (ARD).

ABSTRACT: We report the synthesis and biomimetic activity of a family of model complexes with relevance to acireductone dioxygenase (ARD), an enzyme that displays dual function based on metal identity found in the methionine salvage pathway (MSP). Three complexes with related structural motifs were synthesized and characterized derived from phenolate, and pyridine N₄O Schiff-base ligands. They display pseudo-octahedral Ni(II)-N₄O ligand coordination with water at the sixth site, in close alignment to the structure in the resting state of ARD. The three featured complexes exhibit carbon‑carbon bond cleavage activation of lithium acetylacetonate, which was used as a model enzyme substrate. Computationally derived mechanistic routes for the observed reactivity consistent with expe

SUBMITTER: Blade GA 

PROVIDER: S-EPMC7680382 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature