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

Abstract

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 = 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)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.