Electron paramagnetic resonance studies of the iron-sulfur centers from complex I of Rhodothermus marinus.

@article{Fernandes2006ElectronPR,
  title={Electron paramagnetic resonance studies of the iron-sulfur centers from complex I of Rhodothermus marinus.},
  author={Andr{\'e}ia da Silva Fernandes and Filipa L. Sousa and Miguel Teixeira and M Manuela A Pereira},
  journal={Biochemistry},
  year={2006},
  volume={45 3},
  pages={
          1002-8
        }
}
Rhodothermus marinus, a thermohalophilic gram negative bacterium, contains a type I NADH/quinone oxidoreductase (complex I). Its purification was optimized, yielding large amounts of pure and active protein. Furthermore, the stoichiometry of NADH oxidation and quinone reduction was shown to be 1:1. The large amounts of protein enabled a thorough characterization by electron paramagnetic resonance (EPR) spectroscopy at different temperatures and microwave powers, using NADH, NADPH, and… CONTINUE READING

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