Copper Amine Oxidases (CAO) utilize a (His)3Tyr ligand field to catalyze post-translational oxidative modification of the tyrosine to a topaquinone (TPQ) cofactor in active holoenzymes. A Cu(II)-peroxoquinone complex resulting from O2 insertion is a consensus intermediate, but mechanistic details remain to be elucidated.  TPQ biogenesis is retained in apoenzymes reconstituted with Ni(II),1,2 constituting new dioxygenase activity for nickel.  We prepared bio-inspired TpR,MeNiOAr (R=Ph, Me) complexes that decompose under O2.  This chemistry will be discussed from biomimetic and mechanistic perspectives.(1) T. Okajima, et al.  Biochemistry  2005 , 44, 12041-12048.  (2) N. M. Samuels, J. P. Klinman  Biochemistry 2005 , 44, 14308-14317.

Dioxygen activation in bio-inspired Ni(II) phenolate complexes

243rd National Meeting (2012)

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