Abstract
The NADH:menaquinone oxidoreductase (Nqo) is one of the enzymes present in the respiratory chain of the thermohalophilic bacterium Rhodothermus marinus. The genes coding for the R. marinus Nqo subunits were isolated and sequenced, clustering in two operons [ nqo 1 to nqo 7 (nqo A) and nqo 10 to nqo 14 (nqo B)] and two independent genes ( nqo 8 and nqo 9 ). Unexpectedly, two genes encoding homologues of a NhaD Na +/H + antiporter (NhaD) and of a pterin-4α-carbinolamine dehydratase (PCD) were identified within nqo B, flanked by nqo 13 and nqo 14 . Eight conserved motives to harbour iron–sulphur centres are identified in the deduced primary structures, as well as two consensus sequences to bind nucleotides, in this case NADH and FMN. Moreover, the open-reading-frames of the putative NhaD and PCD were shown to be co-transcribed with the other complex I genes encoded by nqo B. The possible role of these two genes in R. marinus complex I is discussed.
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