CHARACTERISTICS OF THE ENERGY-TRANSDUCING NADH-QUINONE OXIDOREDUCTASE OF PARACOCCUS-DENITRIFICANS AS REVEALED BY BIOCHEMICAL, BIOPHYSICAL, AND MOLECULAR BIOLOGICAL APPROACHES

A comparison of the mitochondrial NADH-ubiquinone oxidoreductase an the energy-transducing NADH-quinone oxidoreductase (NDH-1) of Paracoccus 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 the Paracoccus NDH-1 may serve as a useful model system for the study of the human enzyme complex. The gene cluster encoding the Paracoccus 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 and Paracoccus NDH-1 subunits which may contain the binding sites of substrates and/or electron carriers.