Nitrate reduction in the periplasm of gram-negative bacteria.
In contrast to the bacterial assimilatory and membrane-associated, respiratory nitrate reductases that have been studied for many years, it is only recently that periplasmic nitrate reductases have attracted growing interest. Recent research has shown that these soluble proteins are widely distributed, but vary greatly between species. All of those so far studied include four essential components: the periplasmic molybdoprotein, NapA, which is associated with a small, di-haem cytochrome, NapB; a putative quinol oxidase, NapC; and a possible pathway-specific chaperone, NapD. At least five other components have been found in different species. Other variations between species include the location of the nap genes on chromosomal or extrachromosomal DNA, and the environmental factors that regulate their expression. Despite the relatively small number of bacteria so far screened, striking correlations are beginning to emerge between the organization of the nap genes, the physiology of the host, the conditions under which the nap genes are expressed, and even the fate of nitrite, the product of Nap activity. Evidence is emerging that Nap fulfills a novel role in nitrate scavenging by some pathogenic bacteria.
Potter
L
L
School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK. l.potter@bham.ac.uk
Angove
H
H
Richardson
D
D
Cole
J
J
D000595:Amino Acid Sequence; D001483:Base Sequence; D015964:Gene Expression Regulation, Bacterial; D006090:Gram-Negative Bacteria / Q000201:enzymology / Q000378:metabolism*; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009565:Nitrate Reductases / Q000378:metabolism*; D009566:Nitrates / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D010084:Oxidation-Reduction; D019897:Periplasm / Q000201:enzymology / Q000378:metabolism*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D009566:Nitrates; D009565:Nitrate Reductases