Cytochrome c oxidase models. A µ-imidazolato complex from copper(II) and tetraphenylporphyrinatomanganese(II) with the magnetic and e.s.r. signature of the cytochrome c oxidase active site
Abstract
A µ-imidazolato heterobimetallic compound derived from an imidazolate-bearing CuII complex (S= 1/2) and [MnII(TPP)](S= 5/2) possesses the magnetic and e.s.r.-silent signature of the cytochrome c oxidase active site in its resting state; as such, the [Mn(imidazolato)Cu]+ centre appears to mimic electronically the binuclear [Cuu2+(S= 1/2)/Cyt. a33+(S= 5/2)] active site of the enzyme.