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Isolation, Characterization and Electron Microscopic Single Particle Analysis of the NADH:Ubiquinone Oxidoreductase (Complex I) from the Hyperthermophilic Eubacterium Aquifex aeolicus

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Peng,  Guohong
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
nstitute of Oceanology, Chinese Academy of Sciences,Qingdao, China;

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Fritzsch,  Günter
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Mentele,  Reinhard
Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society;

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Lottspeich,  Friedrich
Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society;

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Bostina,  Mihnea
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Radermacher,  Michael
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Peng, G., Fritzsch, G., Zickermann, V., Schaegger, H., Mentele, R., Lottspeich, F., et al. (2003). Isolation, Characterization and Electron Microscopic Single Particle Analysis of the NADH:Ubiquinone Oxidoreductase (Complex I) from the Hyperthermophilic Eubacterium Aquifex aeolicus. Biochemistry, 42(10), 3032-3039. doi:10.1021/bi026876v.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DB7D-D
Abstract
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 °C. The specific activity for electron transfer from NADH to decylubiquinone is 29 U/mg at 80 °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 may contain up to 14 subunits. N-terminal amino acid sequencing of the bands indicates the presence of a stable subcomplex, which is composed of subunits E, F, and G. The isolated complex is highly stable and active in a temperature range from 50 to 90 °C, with a half-life of about 10 h at 80 °C. The activity shows a linear Arrhenius plot at 50−85 °C with an activation energy at 31.92 J/mol K. Single particle electron microscopy shows that the A. aeolicus complex I has the typical L-shape. However, visual inspection of averaged images reveals many more details in the external arm of the complex than has been observed for complex I from other sources. In addition, the angle (90°) between the cytoplasmic peripheral arm and the membrane intrinsic arm of the complex appears to be invariant.