Journal of Bioenergetics and Biomembranes

, Volume 25, Issue 4, pp 339–345 | Cite as

Characteristics of the energy-transducing NADH-quinone oxidoreductase ofParacoccus denitrificans as revealed by biochemical, biophysical, and molecular biological approaches

  • Takao Yagi
  • Takahiro Yano
  • Akemi Matsuno-Yagi


A comparison of the mitochondrial NADH-ubiquinone oxidoreductase and the energy-transducing NADH-quinone oxidoreductase (NDH-1) ofParacoccus denitrificans revealed that both systems have similar electron-transfer and energy-transduction pathways. In addition, both complexes are sensitive to the same inhibitors and contain similar electron carriers, suggesting that theParacoccus NDH-1 may serve as a useful model system for the study of the human enzyme complex. The gene cluster encoding theParacoccus NDH-1 has been cloned and sequenced. It is composed of 18,106 base pairs and contains 14 structural genes and six unidentified reading frames (URFs). The structural genes, URFs, and their polypeptides have been characterized. We also discuss nucleotide sequences which are believed to play a role in the regulation of the NDH-1 gene cluster andParacoccus NDH-1 subunits which may contain the binding sites of substrates and/or electron carriers.

Key words

NADH-quinone oxidoreductase Paracoccus denitrificans gene cluster H+ pump gene expression FMN iron-sulfur cluster 


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Copyright information

© Plenum Publishing Corporation 1993

Authors and Affiliations

  • Takao Yagi
    • 1
  • Takahiro Yano
    • 1
  • Akemi Matsuno-Yagi
    • 1
  1. 1.SBR-15, Division of Biochemistry, Department of Molecular and Experimental MedicineThe Scripps Research InstituteLa Jolla

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