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

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posted on 2019-10-31, 12:30 authored by Frederic Melin, Mohamed R. Noor, Elodie Pardieu, Fouzia Boulmedais, Florian Banhart, Gary Cecchini, Tewfik SoulimaneTewfik Soulimane, Petra Hellwig
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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Publication

Chemphyschem;15 (16),pp. 3572-3579

Publisher

Wiley and Sons Ltd

Note

peer-reviewed

Other Funding information

International Center for Frontier Research in Chemistry in Strasbourg (RTRA), Institut Universitaire de France (IUF), IRC

Rights

This is the author's version of the following article: Investigating the thermostability of succinate: quinone oxidoreductase enzymes by direct electrochemistry at SWNTs-modified electrodes and FTIR spectroscopy, published in Chemphyschem, 2014, 15 (16), pp. 3572-3579The definitive version is available at https://doi.org/10.1002/cphc.201402354. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. http://olabout.wiley.com/WileyCDA/Section/id-828039.html#terms

Language

English

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