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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. H., Fritzsch, G., Zickermann, V., Schaagger, 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.

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Genre: Journal Article
Alternative Title : Biochemistry

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 Creators:
Peng, G. H., Author
Fritzsch, G., Author
Zickermann, V., Author
Schaagger, H., Author
Mentele, R.1, Author           
Lottspeich, F.1, Author           
Bostina, M., Author
Radermacher, M., Author
Huber, R.2, Author           
Stetter, K. O., Author
Michel, H., Author
Affiliations:
1Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565158              
2Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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 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 degreesC. The specific activity for electron transfer from NADH to decylubiquinone is 29 U/mg at 80 degreesC. 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 degreesC, with a half-life of about 10 h at 80 degreesC. The activity shows a linear Arrhenius plot at 50- 85 degreesC 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 (90degrees) 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: 2003-03-18
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41804
ISI: 000181535300030
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Title: Biochemistry
  Alternative Title : Biochemistry
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 42 (10) Sequence Number: - Start / End Page: 3032 - 3039 Identifier: ISSN: 0006-2960