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Investigating the thermostability of succinate: quinone oxidoreductase enzymes by direct electrochemistry at SWNTs-modified electrodes and FTIR spectroscopy
Date
2014
Abstract
Succinate Quinone reductases (SQRs) are the enzymes which couple the oxidation of succinate and the reduction of quinones in the respiratory chain of prokaryotes and eukaryotes. We compare herein the temperature-dependent activity and structural stability of two SQRs, the first one from the mesophilic bacterium E. coli and the second one from the thermophilic bacterium T. thermophilus by a combined electrochemical and infrared spectroscopy approach. Direct electron transfer was achieved with the full membrane protein complexes at SWNTs-modified electrodes. The possible structural factors which contribute to the temperature-dependent activity of the enzymes and to the thermostability of the T. thermophiles SQR in particular, are discussed.
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Description
peer-reviewed
Publisher
John Wiley & Sons, Inc.
Citation
Chemphyschem;15 (16),pp. 3572-3579
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Funding Information
International Center for Frontier Research in Chemistry in Strasbourg (RTRA), Institut Universitaire de France (IUF), Irish Research Council (IRC)