Literature DB >> 16023073

A nhaD Na+/H+ antiporter and a pcd homologues are among the Rhodothermus marinus complex I genes.

Ana M P Melo1, Susana A L Lobo, Filipa L Sousa, Andreia S Fernandes, Manuela M Pereira, Gudmundur O Hreggvidsson, Jacob K Kristjansson, Lígia M Saraiva, Miguel Teixeira.   

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 [nqo1 to nqo7 (nqoA) and nqo10 to nqo14 (nqoB)] and two independent genes (nqo8 and nqo9). Unexpectedly, two genes encoding homologues of a NhaD Na+/H+ antiporter (NhaD) and of a pterin-4alpha-carbinolamine dehydratase (PCD) were identified within nqoB, flanked by nqo13 and nqo14. 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 nqoB. The possible role of these two genes in R. marinus complex I is discussed.

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Year:  2005        PMID: 16023073     DOI: 10.1016/j.bbabio.2005.06.003

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  The three-dimensional structure of complex I from Yarrowia lipolytica: a highly dynamic enzyme.

Authors:  M Radermacher; T Ruiz; T Clason; S Benjamin; U Brandt; V Zickermann
Journal:  J Struct Biol       Date:  2006-03-24       Impact factor: 2.867

  1 in total

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