Cyclam-strapped porphyrins and their iron(III)-copper(II) complexes as models for the resting state of cytochrome c oxidase - Université de Rennes Access content directly
Journal Articles New Journal of Chemistry Year : 1999

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

Andrioletti Bruno
  • Function : Author
David Ricard
  • Function : Author

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.
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Dates and versions

hal-01469607 , version 1 (16-02-2017)

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  • HAL Id : hal-01469607 , version 1

Cite

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, 1999, 23 (12), pp.1143-1150. ⟨hal-01469607⟩
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