The periplasmic nitrate reductase in Shewanella: The resolution, distribution and functional implications of two NAP isoforms, NapEDABC and NapDAGHB

Abstract

In the bacterial periplasm, the reduction of nitrate to nitrite is catalysed by a periplasmic nitrate reductase (NAP) system, which is a species-dependent assembly of protein subunits encoded by the nap operon. The reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit, which contains a Mo-bis-molybdopterin guanine dinucleotide cofactor and one [4Fe-4S] iron-sulfur cluster. A review of the nap operons in the genomes of 19 strains of Shewanella shows that most genomes contain two nap operons. This is an unusual feature of this genus. The two NAP isoforms each comprise three isoform-specific subunits - NapA, a di-haem cytochrome NapB, and a maturation chaperone NapD - but have different membrane-intrinsic subunits, and have been named NAP-α (NapEDABC) and NAP-β (NapDAGHB). Sixteen Shewanella genomes encode both NAP-α and NAP-β. The genome of the vigorous denitrifier Shewanella denitrificans OS217 encodes only NAP-α and the genome of the respiratory nitrate ammonifier Shewanella oneidensis MR-1 encodes only NAP-β. This raises the possibility that NAP-α and NAP-β are associated with physiologically distinct processes in the environmentally adaptable genus Shewanella. © 2010 SGM.