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 language | English |
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Pages (from-to) | 3572-3579 |
Number of pages | 8 |
Journal | ChemPhysChem |
Volume | 15 |
Issue number | 16 |
DOIs | |
Publication status | Published - 3 Nov 2014 |
Keywords
- IR spectroscopy
- Nanotubes
- Reductases
- Thermostability
- Voltammetry