Role of the tightly bound quinone for the oxygen reaction of cytochrome oxidase from
| Pas de texte intégral | |
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| Auteurs |
Frédéric Melin Sinan Sabuncu Sylvia K. Choi Agathe Leprince Robert B. Gennis Petra Hellwig |
| Unité de recherche du site |
Chimie de la Matière Complexe UMR 7140 Laboratoire de Bioélectrochimie et Spectroscopie CNRS‐Université de Strasbourg France Center for Biophysics and Computational Biology University of Illinois Urbana IL USA Department of Biochemistry University of Illinois Urbana IL USA |
| Langue |
en |
| Volume |
592 |
| Numéro |
20 |
| Page de début |
3380 |
| Page de fin |
3387 |
| Date de première publication |
2018-10 |
| ISSN |
0014-5793 |
| Titre de la source (revue, livre…) |
FEBS Letters |
| Résumé |
The coupling of the reaction of a tightly bound ubiquinone with the reduction of O2 in cytochrome bo3 of Escherichia coli was investigated. In the absence of the quinone, a strongly diminished rate of electrocatalytic reduction of oxygen is detected, Show moreThe coupling of the reaction of a tightly bound ubiquinone with the reduction of O2 in cytochrome bo3 of Escherichia coli was investigated. In the absence of the quinone, a strongly diminished rate of electrocatalytic reduction of oxygen is detected, which can be restored by adding quinones. The correlation of previous EPR data with the electrocatalytic study on mutations in the binding site at positions, Q101, D75, F93, H98, I102 and R71 reveal that the stabilization of the radical is not necessary for the oxygen reaction. The Q101 and F93 variants exhibit both well‐defined catalytic i–V curves, whereas D75H, H98F, I102W and R71H exhibit broad i–V curves with large hysteresis pointing toward a strong alteration in their catalytic activity. Show less |
| DOI | 10.1002/1873-3468.13263 |
| Titre abrégé de la source |
FEBS Lett |
| Type de publication |
ACL |
| Topic |
Sciences du Vivant [q-bio]/Microbiologie et Parasitologie |
| Audience |
Non spécifiée |
| URL | https://univoak.eu/islandora/object/islandora:88830 |