Investigating the thermostability of succinate: Quinone oxidoreductase enzymes by direct electrochemistry at SWNTs-modified electrodes and FTIR spectroscopy

Frederic Melin, Mohamed R. Noor, Elodie Pardieu, Fouzia Boulmedais, Florian Banhart, Gary Cecchini, Tewfik Soulimane, Petra Hellwig

Research output: Contribution to journalArticlepeer-review

Abstract

Succinate: quinone reductases (SQRs) are the enzymes that couple the oxidation of succinate and the reduction of qui-nones 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 electro-chemical 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.

Original languageEnglish
Pages (from-to)3572-3579
Number of pages8
JournalChemPhysChem
Volume15
Issue number16
DOIs
Publication statusPublished - 3 Nov 2014

Keywords

  • IR spectroscopy
  • Nanotubes
  • Reductases
  • Thermostability
  • Voltammetry

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