Tetrad or triad? insights from a versatile Fe(ii) structural and functional model of the 3-histidine 1-carboxylate tetrad in C-C bond cleaving dioxygenase enzymes.

ABSTRACT: A new N₃O coordinate ferrous complex modeling the 3-histidine-1-carboxylate tetrad - a dioxygenase active site - was synthesized and crystallographically characterized, ([Fe(ii)(N-(ethyl-N'Me2)(Py)(2-t-ButPhOH))(OTf)]), 1. Complex 1 displays versatile C-C bond cleavage activity towards 2-hydroxyacetophenone, 3-hydroxyflavone, and 3,3-dihydroxypentan-2,4-dione in the presence of O₂. This reactivity was studied through UV-vis and NMR spectroscopy alongside DFT calculations. The latter suggests that 1 forms an Fe(iii)O₂ adduct during the oxidation of 2-hydroxyacetophenone. Additionally, 1 displays direct activation of O₂ in the absence of substrate, allowing it to access reactivity akin to more traditional N₂O enzymat

SUBMITTER: Fadul A 

PROVIDER: S-EPMC12902916 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature