Isolation, characterization and electron microscopic single particle analysis of the NADH:ubiquinone oxidoreductase (complex I) from the hyperthermophilic eubacterium Aquifex aeolicus.

@article{Peng2003IsolationCA,
  title={Isolation, characterization and electron microscopic single particle analysis of the NADH:ubiquinone oxidoreductase (complex I) from the hyperthermophilic eubacterium Aquifex aeolicus.},
  author={Guohong Peng and G{\"u}nter Fritzsch and Volker Zickermann and Hermann Sch{\"a}gger and Reinhardt Mentele and Friedrich Lottspeich and Mihnea Bostina and Michael Radermacher and Robert Huber and K. O. Stetter and Hartmut Michel},
  journal={Biochemistry},
  year={2003},
  volume={42 10},
  pages={3032-9}
}
The proton-translocating NADH:ubiquinone oxidoreductase (complex I) has been purified from Aquifex aeolicus, a hyperthermophilic eubacterium of known genome sequence. The purified detergent solubilized enzyme is highly active above 50 degrees C. The specific activity for electron transfer from NADH to decylubiquinone is 29 U/mg at 80 degrees C. The A. aeolicus complex I is completely sensitive to rotenone and 2-n-decyl-quinazoline-4-yl-amine. SDS polyacrylamide gel electrophoresis shows that it… CONTINUE READING

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