Skip to Main content Skip to Navigation
Journal articles

Cyclam-strapped porphyrins and their iron(III)-copper(II) complexes as models for the resting state of cytochrome c oxidase

Abstract : The ESR study of two cyclam-strapped porphyrins in which, on one side, the cyclam is attached with a variable length linker to the porphyrin and, on the other side, a non-coordinating strap protects the iron from any intermolecular interaction, is reported. Variation of the linker length is made possible by the use of either a Michael reaction or a nucleophilic substitution, leading respectively to three or two carbon atom links. It is shown that in the case of the shortest link, the oxidized ironÈcopper complex exhibits a spin interaction. The distance between thetwo metal centers is evaluated to be around 4.5 Å, a value consistent with the one found in the natural enzyme.
Document type :
Journal articles
Complete list of metadatas

https://hal-univ-rennes1.archives-ouvertes.fr/hal-01469607
Contributor : Bernard Boitrel <>
Submitted on : Thursday, February 16, 2017 - 3:47:45 PM
Last modification on : Friday, June 8, 2018 - 2:50:12 PM

Identifiers

  • HAL Id : hal-01469607, version 1

Citation

Bernard Boitrel, Andrioletti Bruno, David Ricard. Cyclam-strapped porphyrins and their iron(III)-copper(II) complexes as models for the resting state of cytochrome c oxidase. New Journal of Chemistry, Royal Society of Chemistry, 1999, 23 (12), pp.1143-1150. ⟨hal-01469607⟩

Share

Metrics

Record views

90