Investigating the Thermostability of Succinate: Quinone Oxidoreductase Enzymes by Direct Electrochemistry at SWNTs-Modified Electrodes and FTIR Spectroscopy - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue ChemPhysChem Année : 2014

Investigating the Thermostability of Succinate: Quinone Oxidoreductase Enzymes by Direct Electrochemistry at SWNTs-Modified Electrodes and FTIR Spectroscopy

Résumé

Succinate: quinone reductases (SQRs) are the enzymes that couple the oxidation of succinate and the reduction of quinones in the respiratory chain of prokaryotes and eukaryotes. Herein, we compare the temperature-dependent activity and structural stability of two SQRs, the first from the mesophilic bacterium Escherichia coli and the second from the thermophilic bacterium Thermus thermophilus, using a combined electrochemical and infrared spectroscopy approach. Direct electron transfer was achieved with full membrane protein complexes at single-walled carbon nanotube (SWNT)-modified electrodes. The possible structural factors that contribute to the temperature-dependent activity of the enzymes and, in particular, to the thermostability of the Thermus thermophilus SQR are discussed.

Domaines

Chimie

Dates et versions

hal-02323607 , version 1 (21-10-2019)

Identifiants

Citer

Frédéric Mélin, Mohamed Noor, Elodie Pardieu, Fouzia Boulmedais, Florian Banhart, et al.. Investigating the Thermostability of Succinate: Quinone Oxidoreductase Enzymes by Direct Electrochemistry at SWNTs-Modified Electrodes and FTIR Spectroscopy. ChemPhysChem, 2014, 15 (16), pp.3572-3579. ⟨10.1002/cphc.201402354⟩. ⟨hal-02323607⟩
13 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More