Spectroscopic characterization of a Ru(iii)-OCl intermediate: a structural mimic of haloperoxidase enzymes

Haloperoxidase enzymes utilize metal hypohalite species to halogenate aliphatic and aromatic C-H bonds to C-X (X = Cl, Br, I) in nature. In this work, we report the synthesis and spectroscopic characterization of a unique Ru-III-OCl species as a structural mimic of haloperoxidase enzymes. The reaction of [(BnTPEN)Ru-II(NCCH3)](2+) (BnTPEN = N-1-benzyl-N-1,N-2,N-2-tris(pyridine-2-ylmethyl)ethane-1,2-diamine) with hypochlorite in the presence of an acid in CH3CN : H2O mixtures generated a novel [(BnTPEN)Ru-III-OCl](2+) species that persists for 4.5 h at room temperature. This new species was characterized by UV-vis absorption, EPR, and resonance Raman spectroscopic techniques, and ESI-MS. The Ru-III-OCl species is capable of performing oxygen atom transfer and hydrogen atom abstraction to various organic substrates.

Automated summary

In this study, a synthetic Ru-III-OCl species was reported as a structural mimic of haloperoxidase enzymes. This species can persist for a certain period of time at room temperature and perform oxygen atom transfer and hydrogen atom abstraction to organic substrates.