test_moissonnage_selune
type: Agent

Identification of the oxygen reaction intermediates of cytochrome c oxydase and its models by differential infrared spectroscopy
type: Distribution
access URL: https://theses.hal.science/tel-00781055
format: HTML
issued: 2026-05-14T22:08:39.272374
modified: 2026-05-14T22:08:39.214622

Identification of the oxygen reaction intermediates of cytochrome c oxydase and its models by differential infrared spectroscopy
type: Dataset
contact point: Organization
  fn: CCSD
keyword: cytochrome-c-oxidase
keyword: complexe-fer-oxygene
keyword: theses
keyword: ftir-spectroscopy
keyword: metal-ligands-vibrations
keyword: intermediaires-reactionnels
keyword: chimothechemical-sciencesother
keyword: infoeu-reposemanticsdoctoralthesis
keyword: modeles-bimimetiques
keyword: reactionnal-intermediates
keyword: vibrations-metal-ligands
keyword: carbon-monoxide
keyword: cytochrome-c-oxydase
keyword: iron-oxygen-complex
keyword: spectroscopie-irtf
keyword: biomimetic-models
keyword: monoxyde-de-carbone
landing page: https://theses.hal.science/tel-00781055
description: Cytochrome c Oxidase (CcO), a member of the heme-copper oxidase superfamily, is a membrane protein in many aerobic organisms, that catalyses the reduction of dioxygen to water. Dioxygen binding and reduction occurs at a heterobinuclear site that is comprised of a heme a3, and a copper atom (CuB) in close proximity. Despite, the CcO has been the subject of numerous biophysical and spectroscopic investigations, the detailed molecular mechanism of CcO remains still elusive. In order to better define the structure-function relationship for this hemoprotein, two distinct and complementary approaches have been employed: the study of the natural system and the biomimetic approach.Structural changes accompanying the change in the redox state of some CcO intermediates have been characterised by UV-Visible, ATR-FTIR and time-resolved fluorescence spectroscopies. The study of the cytochrome c oxydase active site modified with isotopic substitutions of CuB, and the effect of pH on the structure are discussed. The second part of this work is related to study the role of environment on the reactivity of FeII-CO et FeII-O2 complexes by exploiting a series of superstructured models of the binuclear Fe/Cu active site of CcO. Based upon a porphyrin core, all these models have the iron-histidine ligation of the proximal site and the copper ligand of the distal site of CcO but they differ strongly by the environment around the copper and their rigidity.
identifier: NNT: 2012STRAF027
issued: 2026-05-14T22:08:39.268339
language: fr
modified: 2026-05-14T22:08:39.268345