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 RuIII-OCl species as a structural mimic of haloperoxidase enzymes. The reaction of [(BnTPEN)RuII(NCCH3)]2+ (BnTPEN = N1-benzyl-N1,N2,N2-tris(pyridine-2-ylmethyl)ethane-1,2-diamine) with hypochlorite in the presence of an acid in CH3CN : H2O mixtures generated a novel [(BnTPEN)RuIII-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 RuIII-OCl species is capable of performing oxygen atom transfer and hydrogen atom abstraction to various organic substrates. [ABSTRACT FROM AUTHOR]