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Investigating the Thermostability of Succinate: Quinone Oxidoreductase Enzymes by Direct Electrochemistry at SWNTs‐Modified Electrodes and FTIR Spectroscopy
Author(s) -
Melin Frederic,
Noor Mohamed R.,
Pardieu Elodie,
Boulmedais Fouzia,
Banhart Florian,
Cecchini Gary,
Soulimane Tewfik,
Hellwig Petra
Publication year - 2014
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201402354
Subject(s) - thermus thermophilus , thermostability , chemistry , fourier transform infrared spectroscopy , thermophile , electron transfer , electrochemistry , escherichia coli , enzyme , electrode , biochemistry , organic chemistry , chemical engineering , engineering , gene
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.