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A question of flexibility in cytochrome c oxidase models

Authors :
Mourad Elhabiri
Petra Hellwig
Pauline Vorburger
Nesrine Oueslati
Corinne Boudon
Mamadou Lo
Sylvie Choua
Maxime Bernard
Frederic Melin
Jennifer A. Wytko
Jean Weiss
Source :
Inorganica Chimica Acta. 468:232-238
Publication Year :
2017
Publisher :
Elsevier BV, 2017.

Abstract

The structure-property relationships were compared for the iron and iron-copper complexes of two functional cytochrome c oxidase models, 1 and 2 , both constructed upon a phenanthroline-strapped porphyrin bearing respectively pyridyl or picolinyl built-in proximal and distal ligands. The behavior of these heme models in the absence and in the presence of copper was studied by 1 H NMR, UV–visible absorption, EPR, Raman and FTIR spectroscopies, electrochemistry in solution and deposited on a rotating ring-disk graphite electrode. The distal binding site within the phenanthroline pocket of both 1 and 2 is available for the coordination of exogenic ligands, yet the oxygen binding affinity is higher for all complexes of 2 than for 1 . Despite this difference, [ 1Fe II Cu I ] more efficiently reproduced the electrocatalyzed reduction of oxygen to water than [ 2Fe II Cu I ]. The oxygenated complexes of both iron(II)-copper(I) species mimic the ability of cytochrome c oxidase to reversibly bind O 2 , as shown by competitive binding studies in the presence of CO. Differences in the binding and electrocatalytic properties of these models stem from difference in rigidity of scaffolds upon binding of both the proximal and distal ligands, as well as from the bulkiness of the distal ligand.

Details

ISSN :
00201693
Volume :
468
Database :
OpenAIRE
Journal :
Inorganica Chimica Acta
Accession number :
edsair.doi...........2994ac6b5b542d479adf9d25576d7850