Issue 24, 1985

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.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1985, 1761-1763

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

V. Chunplang and L. J. Wilson, J. Chem. Soc., Chem. Commun., 1985, 1761 DOI: 10.1039/C39850001761

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements