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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

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.

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 Creators:
Peng, Guohong1, 2, Author              
Fritzsch, Günter1, Author              
Zickermann, Volker3, Author
Schaegger, Herrmann3, Author
Mentele, Reinhard4, Author              
Lottspeich, Friedrich4, Author              
Bostina, Mihnea5, Author              
Radermacher, Michael5, Author              
Huber, Robert6, Author
Stetter, Karl Otto6, Author
Michel, Hartmut1, Author              
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2nstitute of Oceanology, Chinese Academy of Sciences,Qingdao, China, ou_persistent22              
3Gustav-Embden Zentrum der Biologischen Chemie, Klinikum der Johann Wolfgang Goethe-Universität, Frankfurt a. M., Germany, ou_persistent22              
4Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565158              
5Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
6UniVersität Regensburg,Lehrstuhl für Mikrobiologie & Archaeenzentrum, Regensburg, Germany, ou_persistent22              

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Free keywords: Peptides and proteins; Bacteria; Membranes; Solubilization; Filtration
 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.

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Language(s): eng - English
 Dates: 2003-01-062002-09-202003-02-202003-03-01
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/bi026876v
 Degree: -

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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 42 (10) Sequence Number: - Start / End Page: 3032 - 3039 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103